HEADER TRANSFERASE 22-DEC-16 5MRD
TITLE HUMAN PDK1-PKCIOTA KINASE CHIMERA IN COMPLEX WITH ALLOSTERIC COMPOUND
TITLE 2 PS267 BOUND TO THE PIF-POCKET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HPDK1;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: PDPK1, PDK1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROTEIN KINASE, ALLOSTERIC REGULATION, SMALL COMPOUNDS, PIF-POCKET,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.ARENCIBIA,W.FROEHNER,M.KRUPA,D.PASTOR-FLORES,P.MERKER,
AUTHOR 2 T.OELLERICH,S.NEIMANIS,C.SCHMITHALS,V.KOEBERLE,E.SUESS,S.ZEUZEM,
AUTHOR 3 H.STARK,A.PIIPER,D.ODADZIC,J.O.SCHULZE,R.M.BIONDI
REVDAT 5 17-JAN-24 5MRD 1 REMARK
REVDAT 4 16-OCT-19 5MRD 1 REMARK
REVDAT 3 01-MAR-17 5MRD 1 JRNL
REVDAT 2 25-JAN-17 5MRD 1 JRNL
REVDAT 1 18-JAN-17 5MRD 0
JRNL AUTH J.M.ARENCIBIA,W.FROHNER,M.KRUPA,D.PASTOR-FLORES,P.MERKER,
JRNL AUTH 2 T.OELLERICH,S.NEIMANIS,C.SCHMITHALS,V.KOBERLE,E.SU,S.ZEUZEM,
JRNL AUTH 3 H.STARK,A.PIIPER,D.ODADZIC,J.O.SCHULZE,R.M.BIONDI
JRNL TITL AN ALLOSTERIC INHIBITOR SCAFFOLD TARGETING THE PIF-POCKET OF
JRNL TITL 2 ATYPICAL PROTEIN KINASE C ISOFORMS.
JRNL REF ACS CHEM. BIOL. V. 12 564 2017
JRNL REFN ESSN 1554-8937
JRNL PMID 28045490
JRNL DOI 10.1021/ACSCHEMBIO.6B00827
REMARK 2
REMARK 2 RESOLUTION. 1.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 57631
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2882
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 46.7974 - 3.8892 0.98 2735 144 0.1479 0.1521
REMARK 3 2 3.8892 - 3.0871 0.97 2655 140 0.1364 0.1563
REMARK 3 3 3.0871 - 2.6969 0.97 2636 139 0.1429 0.1736
REMARK 3 4 2.6969 - 2.4504 0.98 2643 139 0.1384 0.1760
REMARK 3 5 2.4504 - 2.2747 0.98 2645 139 0.1208 0.1535
REMARK 3 6 2.2747 - 2.1406 0.98 2642 139 0.1138 0.1758
REMARK 3 7 2.1406 - 2.0334 0.98 2604 137 0.1189 0.1484
REMARK 3 8 2.0334 - 1.9449 0.98 2625 139 0.1215 0.1599
REMARK 3 9 1.9449 - 1.8700 0.98 2598 136 0.1192 0.1620
REMARK 3 10 1.8700 - 1.8055 0.97 2597 137 0.1321 0.1630
REMARK 3 11 1.8055 - 1.7490 0.98 2629 138 0.1302 0.1713
REMARK 3 12 1.7490 - 1.6990 0.97 2582 136 0.1361 0.1976
REMARK 3 13 1.6990 - 1.6543 0.97 2561 135 0.1453 0.2074
REMARK 3 14 1.6543 - 1.6140 0.97 2624 138 0.1496 0.2282
REMARK 3 15 1.6140 - 1.5773 0.97 2598 137 0.1499 0.2092
REMARK 3 16 1.5773 - 1.5437 0.97 2561 135 0.1625 0.2234
REMARK 3 17 1.5437 - 1.5128 0.96 2587 136 0.1716 0.2309
REMARK 3 18 1.5128 - 1.4843 0.96 2519 133 0.1770 0.2579
REMARK 3 19 1.4843 - 1.4578 0.96 2586 136 0.2067 0.2395
REMARK 3 20 1.4578 - 1.4330 0.96 2575 135 0.2228 0.2641
REMARK 3 21 1.4330 - 1.4099 0.96 2547 134 0.2441 0.2781
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.610
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 : 0.010 2532
REMARK 3 ANGLE : 1.610 3471
REMARK 3 CHIRALITY : 0.097 382
REMARK 3 PLANARITY : 0.009 437
REMARK 3 DIHEDRAL : 16.413 972
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 5MRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002896.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-12
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 : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57639
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.410
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 3HRC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M NA CITRATE, 0.1 M HEPES PH 7.5,
REMARK 280 10 MM DTT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 74.55500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.24000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 74.55500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.24000
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: 1330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 ALA A 50
REMARK 465 MET A 51
REMARK 465 ASP A 52
REMARK 465 GLY A 53
REMARK 465 THR A 54
REMARK 465 ALA A 55
REMARK 465 ALA A 56
REMARK 465 GLU A 57
REMARK 465 PRO A 58
REMARK 465 ARG A 59
REMARK 465 PRO A 60
REMARK 465 GLY A 61
REMARK 465 ALA A 62
REMARK 465 GLY A 63
REMARK 465 SER A 64
REMARK 465 LEU A 65
REMARK 465 GLN A 66
REMARK 465 HIS A 67
REMARK 465 ALA A 68
REMARK 465 GLN A 69
REMARK 465 PRO A 70
REMARK 465 PRO A 71
REMARK 465 PRO A 72
REMARK 465 GLN A 73
REMARK 465 PRO A 74
REMARK 465 ARG A 75
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 ARG A 78 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 83 NZ
REMARK 470 GLU A 114 CD OE1 OE2
REMARK 470 ARG A 116 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 117 ND1 CD2 CE1 NE2
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 LYS A 123 CD CE NZ
REMARK 470 ILE A 124 CD1
REMARK 470 LYS A 173 CE NZ
REMARK 470 LYS A 199 CE NZ
REMARK 470 LYS A 235 CE NZ
REMARK 470 LYS A 257 CD CE NZ
REMARK 470 GLU A 303 CG CD OE1 OE2
REMARK 470 LYS A 304 CD CE NZ
REMARK 470 LYS A 357 CD 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 HZ3 LYS A 261 OE2 GLU A 328 1.54
REMARK 500 HZ1 LYS A 261 O HOH A 502 1.54
REMARK 500 O HOH A 708 O HOH A 751 2.10
REMARK 500 O HOH A 576 O HOH A 760 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 OG SER A 105 O GLU A 348 2555 2.08
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 ASP A 138 74.32 -150.75
REMARK 500 ARG A 204 -10.58 77.26
REMARK 500 ASP A 223 73.90 74.21
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 827 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 828 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 829 DISTANCE = 6.49 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 S26 A 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue S26 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 405
DBREF 5MRD A 50 359 UNP O15530 PDPK1_HUMAN 50 359
SEQADV 5MRD SER A 76 UNP O15530 LYS 76 ENGINEERED MUTATION
SEQADV 5MRD VAL A 113 UNP O15530 LEU 113 ENGINEERED MUTATION
SEQADV 5MRD VAL A 118 UNP O15530 ILE 118 ENGINEERED MUTATION
SEQADV 5MRD ASN A 119 UNP O15530 ILE 119 ENGINEERED MUTATION
SEQADV 5MRD ILE A 124 UNP O15530 VAL 124 ENGINEERED MUTATION
SEQADV 5MRD GLN A 128 UNP O15530 THR 128 ENGINEERED MUTATION
SEQADV 5MRD LYS A 131 UNP O15530 ARG 131 ENGINEERED MUTATION
SEQADV 5MRD CYS A 148 UNP O15530 THR 148 ENGINEERED MUTATION
SEQADV 5MRD GLY A 288 UNP O15530 TYR 288 CONFLICT
SEQADV 5MRD ALA A 292 UNP O15530 GLN 292 CONFLICT
SEQRES 1 A 310 ALA MET ASP GLY THR ALA ALA GLU PRO ARG PRO GLY ALA
SEQRES 2 A 310 GLY SER LEU GLN HIS ALA GLN PRO PRO PRO GLN PRO ARG
SEQRES 3 A 310 SER LYS ARG PRO GLU ASP PHE LYS PHE GLY LYS ILE LEU
SEQRES 4 A 310 GLY GLU GLY SER PHE SER THR VAL VAL LEU ALA ARG GLU
SEQRES 5 A 310 LEU ALA THR SER ARG GLU TYR ALA ILE LYS ILE VAL GLU
SEQRES 6 A 310 LYS ARG HIS VAL ASN LYS GLU ASN LYS ILE PRO TYR VAL
SEQRES 7 A 310 GLN ARG GLU LYS ASP VAL MET SER ARG LEU ASP HIS PRO
SEQRES 8 A 310 PHE PHE VAL LYS LEU TYR PHE CYS PHE GLN ASP ASP GLU
SEQRES 9 A 310 LYS LEU TYR PHE GLY LEU SER TYR ALA LYS ASN GLY GLU
SEQRES 10 A 310 LEU LEU LYS TYR ILE ARG LYS ILE GLY SER PHE ASP GLU
SEQRES 11 A 310 THR CYS THR ARG PHE TYR THR ALA GLU ILE VAL SER ALA
SEQRES 12 A 310 LEU GLU TYR LEU HIS GLY LYS GLY ILE ILE HIS ARG ASP
SEQRES 13 A 310 LEU LYS PRO GLU ASN ILE LEU LEU ASN GLU ASP MET HIS
SEQRES 14 A 310 ILE GLN ILE THR ASP PHE GLY THR ALA LYS VAL LEU SER
SEQRES 15 A 310 PRO GLU SER LYS GLN ALA ARG ALA ASN SEP PHE VAL GLY
SEQRES 16 A 310 THR ALA GLN TYR VAL SER PRO GLU LEU LEU THR GLU LYS
SEQRES 17 A 310 SER ALA CYS LYS SER SER ASP LEU TRP ALA LEU GLY CYS
SEQRES 18 A 310 ILE ILE TYR GLN LEU VAL ALA GLY LEU PRO PRO PHE ARG
SEQRES 19 A 310 ALA GLY ASN GLU GLY LEU ILE PHE ALA LYS ILE ILE LYS
SEQRES 20 A 310 LEU GLU TYR ASP PHE PRO GLU LYS PHE PHE PRO LYS ALA
SEQRES 21 A 310 ARG ASP LEU VAL GLU LYS LEU LEU VAL LEU ASP ALA THR
SEQRES 22 A 310 LYS ARG LEU GLY CYS GLU GLU MET GLU GLY TYR GLY PRO
SEQRES 23 A 310 LEU LYS ALA HIS PRO PHE PHE GLU SER VAL THR TRP GLU
SEQRES 24 A 310 ASN LEU HIS GLN GLN THR PRO PRO LYS LEU THR
MODRES 5MRD SEP A 241 SER MODIFIED RESIDUE
HET SEP A 241 14
HET S26 A 401 23
HET DTT A 402 18
HET DMS A 403 10
HET DMS A 404 10
HET ATP A 405 43
HETNAM SEP PHOSPHOSERINE
HETNAM S26 ETHYL (2~{S})-1-(6-CHLORANYL-1,3-BENZOTHIAZOL-2-YL)-4-
HETNAM 2 S26 OXIDANYL-5-OXIDANYLIDENE-2-THIOPHEN-2-YL-2~{H}-
HETNAM 3 S26 PYRROLE-3-CARBOXYLATE
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETSYN SEP PHOSPHONOSERINE
HETSYN S26 PS267
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 S26 C18 H13 CL N2 O4 S2
FORMUL 3 DTT C4 H10 O2 S2
FORMUL 4 DMS 2(C2 H6 O S)
FORMUL 6 ATP C10 H16 N5 O13 P3
FORMUL 7 HOH *329(H2 O)
HELIX 1 AA1 ARG A 78 GLU A 80 5 3
HELIX 2 AA2 LYS A 115 GLU A 121 1 7
HELIX 3 AA3 LYS A 123 LEU A 137 1 15
HELIX 4 AA4 LEU A 167 GLY A 175 1 9
HELIX 5 AA5 ASP A 178 LYS A 199 1 22
HELIX 6 AA6 LYS A 207 GLU A 209 5 3
HELIX 7 AA7 THR A 245 VAL A 249 5 5
HELIX 8 AA8 SER A 250 LYS A 257 1 8
HELIX 9 AA9 CYS A 260 GLY A 278 1 19
HELIX 10 AB1 ASN A 286 LEU A 297 1 12
HELIX 11 AB2 PHE A 306 LEU A 317 1 12
HELIX 12 AB3 ASP A 320 ARG A 324 5 5
HELIX 13 AB4 CYS A 327 GLU A 331 5 5
HELIX 14 AB5 GLY A 332 ALA A 338 1 7
HELIX 15 AB6 HIS A 339 GLU A 343 5 5
HELIX 16 AB7 ASN A 349 GLN A 353 5 5
SHEET 1 AA1 5 PHE A 82 GLU A 90 0
SHEET 2 AA1 5 SER A 94 GLU A 101 -1 O LEU A 98 N GLY A 85
SHEET 3 AA1 5 GLU A 107 GLU A 114 -1 O ILE A 112 N THR A 95
SHEET 4 AA1 5 LYS A 154 LEU A 159 -1 O LEU A 159 N ALA A 109
SHEET 5 AA1 5 LEU A 145 GLN A 150 -1 N PHE A 149 O TYR A 156
SHEET 1 AA2 3 GLY A 165 GLU A 166 0
SHEET 2 AA2 3 ILE A 211 LEU A 213 -1 O LEU A 213 N GLY A 165
SHEET 3 AA2 3 ILE A 219 ILE A 221 -1 O GLN A 220 N LEU A 212
SHEET 1 AA3 2 ILE A 201 ILE A 202 0
SHEET 2 AA3 2 LYS A 228 VAL A 229 -1 O LYS A 228 N ILE A 202
LINK C ASN A 240 N SEP A 241 1555 1555 1.33
LINK C SEP A 241 N PHE A 242 1555 1555 1.33
SITE 1 AC1 8 VAL A 118 ASN A 119 ILE A 124 GLN A 128
SITE 2 AC1 8 LYS A 131 GLN A 150 LEU A 155 HOH A 557
SITE 1 AC2 7 GLY A 244 ALA A 246 ARG A 283 GLU A 287
SITE 2 AC2 7 ASP A 300 PRO A 302 HOH A 666
SITE 1 AC3 9 THR A 104 SER A 105 HIS A 139 TRP A 347
SITE 2 AC3 9 GLU A 348 ASN A 349 LEU A 350 HIS A 351
SITE 3 AC3 9 HOH A 604
SITE 1 AC4 3 PRO A 79 PHE A 82 PHE A 84
SITE 1 AC5 14 LEU A 88 GLY A 89 SER A 94 VAL A 96
SITE 2 AC5 14 LYS A 111 TYR A 126 SER A 160 ALA A 162
SITE 3 AC5 14 GLU A 166 LEU A 212 ASP A 223 HOH A 519
SITE 4 AC5 14 HOH A 556 HOH A 693
CRYST1 149.110 44.480 47.810 90.00 101.96 90.00 C 1 2 1 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 0.006706 0.000000 0.001421 0.00000
SCALE2 0.000000 0.022482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021380 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
