HEADER TRANSFERASE 10-JUN-07 2Q8H
TITLE STRUCTURE OF PYRUVATE DEHYDROGENASE KINASE ISOFORM 1 IN COMPLEX WITH
TITLE 2 DICHLOROACETATE (DCA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: [PYRUVATE DEHYDROGENASE [LIPOAMIDE]] KINASE ISOZYME 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PYRUVATE DEHYDROGENASE KINASE ISOFORM 1;
COMPND 5 EC: 2.7.11.2;
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: PDK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS GHKL ATPASE/KINASE FAMILY, PYRUVATE DEHYDROGENASE COMPLEX,
KEYWDS 2 MITOCHONDRIAL KINASE, DICHROLOACETATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KATO,J.LI,J.L.CHUANG,D.T.CHUANG
REVDAT 6 30-AUG-23 2Q8H 1 REMARK LINK
REVDAT 5 18-OCT-17 2Q8H 1 REMARK
REVDAT 4 13-JUL-11 2Q8H 1 VERSN
REVDAT 3 24-FEB-09 2Q8H 1 VERSN
REVDAT 2 28-AUG-07 2Q8H 1 JRNL
REVDAT 1 24-JUL-07 2Q8H 0
JRNL AUTH M.KATO,J.LI,J.L.CHUANG,D.T.CHUANG
JRNL TITL DISTINCT STRUCTURAL MECHANISMS FOR INHIBITION OF PYRUVATE
JRNL TITL 2 DEHYDROGENASE KINASE ISOFORMS BY AZD7545, DICHLOROACETATE,
JRNL TITL 3 AND RADICICOL.
JRNL REF STRUCTURE V. 15 992 2007
JRNL REFN ISSN 0969-2126
JRNL PMID 17683942
JRNL DOI 10.1016/J.STR.2007.07.001
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 36097
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1802
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2495
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3720
REMARK 3 BIN FREE R VALUE SET COUNT : 120
REMARK 3 BIN FREE R VALUE : 0.4410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2952
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : 0.44000
REMARK 3 B33 (A**2) : -0.88000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.827
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3052 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4139 ; 1.378 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 364 ; 6.042 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 150 ;34.332 ;23.533
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 513 ;14.755 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;19.573 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 448 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2347 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1433 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2076 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 235 ; 0.145 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.275 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 52 ; 0.151 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.111 ; 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): 1836 ; 0.820 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2976 ; 1.473 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1239 ; 2.171 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1162 ; 3.174 ; 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Q8H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043281.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37074
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.56100
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2Q8F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.42 M NAK TARTRATE, 0.1 M NA CITRATE,
REMARK 280 PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 55.27950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 49.16150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.16150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.63975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.16150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.16150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 82.91925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.16150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.16150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.63975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.16150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.16150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 82.91925
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 55.27950
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE FOLLOWING OPERATION: Y,X,-Z
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 462 LIES ON A SPECIAL POSITION.
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 SER A 30
REMARK 465 ASP A 31
REMARK 465 SER A 32
REMARK 465 GLY A 33
REMARK 465 SER A 34
REMARK 465 SER A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 SER A 38
REMARK 465 GLU A 39
REMARK 465 ARG A 40
REMARK 465 VAL A 68
REMARK 465 ASN A 69
REMARK 465 ALA A 70
REMARK 465 GLY A 168
REMARK 465 VAL A 169
REMARK 465 GLY A 204
REMARK 465 LYS A 205
REMARK 465 GLY A 206
REMARK 465 LYS A 207
REMARK 465 GLY A 208
REMARK 465 SER A 209
REMARK 465 PRO A 210
REMARK 465 SER A 211
REMARK 465 HIS A 212
REMARK 465 ARG A 213
REMARK 465 LYS A 214
REMARK 465 HIS A 415
REMARK 465 GLU A 416
REMARK 465 SER A 424
REMARK 465 ARG A 425
REMARK 465 GLU A 426
REMARK 465 PRO A 427
REMARK 465 LYS A 428
REMARK 465 ASP A 429
REMARK 465 MET A 430
REMARK 465 THR A 431
REMARK 465 THR A 432
REMARK 465 PHE A 433
REMARK 465 ARG A 434
REMARK 465 SER A 435
REMARK 465 ALA A 436
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 42 CG1 CG2
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 LYS A 127 130.71 -37.45
REMARK 500 HIS A 149 50.76 -118.34
REMARK 500 ARG A 319 45.92 -108.71
REMARK 500 TYR A 381 -67.05 -126.33
REMARK 500 ASN A 404 -169.75 -160.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 437 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 50 O
REMARK 620 2 ARG A 51 O 73.6
REMARK 620 3 PHE A 52 O 82.7 69.8
REMARK 620 4 ASN A 89 OD1 86.4 144.9 79.4
REMARK 620 5 TYR A 403 O 95.6 124.4 164.7 85.3
REMARK 620 6 HOH A 526 O 134.1 61.8 91.6 137.3 100.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 437
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TF4 A 438
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q8F RELATED DB: PDB
REMARK 900 RELATED ID: 2Q8G RELATED DB: PDB
REMARK 900 RELATED ID: 2Q8I RELATED DB: PDB
DBREF 2Q8H A 30 436 UNP Q15118 PDK1_HUMAN 30 436
SEQRES 1 A 407 SER ASP SER GLY SER SER PRO ALA SER GLU ARG GLY VAL
SEQRES 2 A 407 PRO GLY GLN VAL ASP PHE TYR ALA ARG PHE SER PRO SER
SEQRES 3 A 407 PRO LEU SER MET LYS GLN PHE LEU ASP PHE GLY SER VAL
SEQRES 4 A 407 ASN ALA CYS GLU LYS THR SER PHE MET PHE LEU ARG GLN
SEQRES 5 A 407 GLU LEU PRO VAL ARG LEU ALA ASN ILE MET LYS GLU ILE
SEQRES 6 A 407 SER LEU LEU PRO ASP ASN LEU LEU ARG THR PRO SER VAL
SEQRES 7 A 407 GLN LEU VAL GLN SER TRP TYR ILE GLN SER LEU GLN GLU
SEQRES 8 A 407 LEU LEU ASP PHE LYS ASP LYS SER ALA GLU ASP ALA LYS
SEQRES 9 A 407 ALA ILE TYR ASP PHE THR ASP THR VAL ILE ARG ILE ARG
SEQRES 10 A 407 ASN ARG HIS ASN ASP VAL ILE PRO THR MET ALA GLN GLY
SEQRES 11 A 407 VAL ILE GLU TYR LYS GLU SER PHE GLY VAL ASP PRO VAL
SEQRES 12 A 407 THR SER GLN ASN VAL GLN TYR PHE LEU ASP ARG PHE TYR
SEQRES 13 A 407 MET SER ARG ILE SER ILE ARG MET LEU LEU ASN GLN HIS
SEQRES 14 A 407 SER LEU LEU PHE GLY GLY LYS GLY LYS GLY SER PRO SER
SEQRES 15 A 407 HIS ARG LYS HIS ILE GLY SER ILE ASN PRO ASN CYS ASN
SEQRES 16 A 407 VAL LEU GLU VAL ILE LYS ASP GLY TYR GLU ASN ALA ARG
SEQRES 17 A 407 ARG LEU CYS ASP LEU TYR TYR ILE ASN SER PRO GLU LEU
SEQRES 18 A 407 GLU LEU GLU GLU LEU ASN ALA LYS SER PRO GLY GLN PRO
SEQRES 19 A 407 ILE GLN VAL VAL TYR VAL PRO SER HIS LEU TYR HIS MET
SEQRES 20 A 407 VAL PHE GLU LEU PHE LYS ASN ALA MET ARG ALA THR MET
SEQRES 21 A 407 GLU HIS HIS ALA ASN ARG GLY VAL TYR PRO PRO ILE GLN
SEQRES 22 A 407 VAL HIS VAL THR LEU GLY ASN GLU ASP LEU THR VAL LYS
SEQRES 23 A 407 MET SER ASP ARG GLY GLY GLY VAL PRO LEU ARG LYS ILE
SEQRES 24 A 407 ASP ARG LEU PHE ASN TYR MET TYR SER THR ALA PRO ARG
SEQRES 25 A 407 PRO ARG VAL GLU THR SER ARG ALA VAL PRO LEU ALA GLY
SEQRES 26 A 407 PHE GLY TYR GLY LEU PRO ILE SER ARG LEU TYR ALA GLN
SEQRES 27 A 407 TYR PHE GLN GLY ASP LEU LYS LEU TYR SER LEU GLU GLY
SEQRES 28 A 407 TYR GLY THR ASP ALA VAL ILE TYR ILE LYS ALA LEU SER
SEQRES 29 A 407 THR ASP SER ILE GLU ARG LEU PRO VAL TYR ASN LYS ALA
SEQRES 30 A 407 ALA TRP LYS HIS TYR ASN THR ASN HIS GLU ALA ASP ASP
SEQRES 31 A 407 TRP CYS VAL PRO SER ARG GLU PRO LYS ASP MET THR THR
SEQRES 32 A 407 PHE ARG SER ALA
HET K A 437 1
HET TF4 A 438 6
HETNAM K POTASSIUM ION
HETNAM TF4 DICHLORO-ACETIC ACID
FORMUL 2 K K 1+
FORMUL 3 TF4 C2 H2 CL2 O2
FORMUL 4 HOH *242(H2 O)
HELIX 1 2 SER A 58 GLY A 66 1 9
HELIX 2 3 CYS A 71 SER A 95 1 25
HELIX 3 4 PRO A 98 ARG A 103 1 6
HELIX 4 5 THR A 104 LEU A 122 1 19
HELIX 5 6 ASP A 131 ASN A 147 1 17
HELIX 6 7 ASP A 151 PHE A 167 1 17
HELIX 7 8 ASP A 170 GLY A 203 1 34
HELIX 8 9 VAL A 225 ILE A 245 1 21
HELIX 9 10 VAL A 269 HIS A 292 1 24
HELIX 10 11 PRO A 324 ASP A 329 1 6
HELIX 11 12 ARG A 330 ASN A 333 5 4
HELIX 12 13 TYR A 357 PHE A 369 1 13
HELIX 13 14 ASN A 404 ASN A 412 1 9
SHEET 1 A 2 ASN A 220 ASN A 224 0
SHEET 2 A 2 GLN A 265 TYR A 268 -1 O TYR A 268 N ASN A 220
SHEET 1 B 5 LEU A 250 ASN A 256 0
SHEET 2 B 5 ILE A 301 LEU A 307 1 O VAL A 303 N GLU A 251
SHEET 3 B 5 ASP A 311 ASP A 318 -1 O SER A 317 N GLN A 302
SHEET 4 B 5 GLY A 382 LYS A 390 -1 O ALA A 385 N MET A 316
SHEET 5 B 5 ASP A 372 LEU A 378 -1 N LEU A 378 O GLY A 382
LINK O ALA A 50 K K A 437 1555 1555 2.37
LINK O ARG A 51 K K A 437 1555 1555 3.51
LINK O PHE A 52 K K A 437 1555 1555 2.64
LINK OD1 ASN A 89 K K A 437 1555 1555 2.71
LINK O TYR A 403 K K A 437 1555 1555 2.51
LINK K K A 437 O HOH A 526 1555 1555 2.48
SITE 1 AC1 7 ALA A 50 ARG A 51 PHE A 52 ASN A 89
SITE 2 AC1 7 VAL A 402 TYR A 403 HOH A 526
SITE 1 AC2 4 LEU A 87 TYR A 114 ARG A 188 ILE A 191
CRYST1 98.323 98.323 110.559 90.00 90.00 90.00 P 41 21 2 8
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 0.010171 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010171 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009045 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
