HEADER TRANSFERASE/INHIBITOR 15-MAR-07 2UVX
TITLE STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH 7-AZAINDOLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PROTEIN KINASE A, PKA C-ALPHA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 10 CHAIN: I;
COMPND 11 FRAGMENT: RESIDUES 5-24;
COMPND 12 SYNONYM: PKI, PKI-ALPHA, MUSCLE/BRAIN ISOFORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606
KEYWDS TRANSFERASE/INHIBITOR, CAMP, KINASE, MYRISTATE,
KEYWDS 2 TRANSFERASE, LIPOPROTEIN, SERINE/THREONINE-PROTEIN KINASE,
KEYWDS 3 TRANSFERASE/INHIBITOR COMPLEX, NUCLEOTIDE-BINDING, PROTEIN
KEYWDS 4 KINASE INHIBITOR, ATP- BINDING, NUCLEAR PROTEIN,
KEYWDS 5 PHOSPHORYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.G.DAVIES,A.DONALD,T.MCHARDY,M.G.ROWLANDS,L.J.HUNTER,
AUTHOR 2 R.G.BOYLE,G.W.AHERNE,M.D.GARRETT,I.COLLINS
REVDAT 4 24-FEB-09 2UVX 1 VERSN
REVDAT 3 20-MAY-08 2UVX 1 VERSN
REVDAT 2 22-MAY-07 2UVX 1 JRNL
REVDAT 1 08-MAY-07 2UVX 0
JRNL AUTH A.DONALD,T.MCHARDY,M.G.ROWLANDS,L.J.HUNTER,
JRNL AUTH 2 T.G.DAVIES,V.BERDINI,R.G.BOYLE,G.W.AHERNE,
JRNL AUTH 3 M.D.GARRETT,I.COLLINS
JRNL TITL RAPID EVOLUTION OF 6-PHENYLPURINE INHIBITORS OF
JRNL TITL 2 PROTEIN KINASE B THROUGH STRUCTURE-BASED DESIGN
JRNL REF J.MED.CHEM. V. 50 2289 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17451235
JRNL DOI 10.1021/JM0700924
REMARK 2
REMARK 2 RESOLUTION. 2.0 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019G
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 30.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 27518
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1466
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1782
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 117
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 382
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.21000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : -0.96000
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): 0.171
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.120
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.320
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3026 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2118 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4082 ; 1.316 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5129 ; 0.865 ; 2.997
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 355 ; 5.757 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 150 ;35.827 ;23.800
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 540 ;15.451 ;15.028
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;20.073 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 423 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3324 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 659 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 633 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2259 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1487 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1520 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 75 ; 0.081 ; 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): 12 ; 0.141 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 24 ; 0.287 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.028 ; 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): 1777 ; 0.101 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2866 ; 0.128 ; 6.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1249 ; 0.126 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1216 ; 0.156 ; 7.500
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2UVX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-07.
REMARK 100 THE PDBE ID CODE IS EBI-31920.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27518
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 36.26850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.93450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.93450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.26850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.20000
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 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 104 TO THR
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 123 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU 173 TO MET
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLN 181 TO LYS
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 0
REMARK 465 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
REMARK 465 GLN A 12
REMARK 465 GLU A 13
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 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 47 143.56 -171.62
REMARK 500 ASN A 99 109.65 -167.31
REMARK 500 ASP A 166 42.79 -148.39
REMARK 500 ASP A 184 90.66 67.75
REMARK 500 ALA A 240 -177.01 -170.63
REMARK 500 LEU A 273 48.53 -88.93
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVH A1351
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CMK RELATED DB: PDB
REMARK 900 RELATED ID: 1XH4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B
REMARK 900 SELECTIVE INHIBITORSIN COMPLEX WITH PROTEIN
REMARK 900 KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B
REMARK 900 SELECTIVE INHIBITORSIN COMPLEX WITH PROTEIN
REMARK 900 KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B
REMARK 900 SELECTIVE INHIBITORSIN COMPLEX WITH PROTEIN
REMARK 900 KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B
REMARK 900 SELECTIVE INHIBITORSIN COMPLEX WITH PROTEIN
REMARK 900 KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B
REMARK 900 SELECTIVE INHIBITORSIN COMPLEX WITH PROTEIN
REMARK 900 KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B
REMARK 900 SELECTIVE INHIBITORSIN COMPLEX WITH PROTEIN
REMARK 900 KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XHA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B
REMARK 900 SELECTIVE INHIBITORSIN COMPLEX WITH PROTEIN
REMARK 900 KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1YDR RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE,
REMARK 900 ALPHA-CATALYTICSUBUNIT IN COMPLEX WITH H7
REMARK 900 PROTEIN KINASE INHIBITOR1-(5-
REMARK 900 ISOQUINOLINESULFONYL)-2-METHYLPIPERAZINE
REMARK 900 RELATED ID: 2C1A RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE
REMARK 900 COMPLEXED WITH ISOQUINOLINE-5-SULFONIC ACID (
REMARK 900 2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)
REMARK 900 AMIDE
REMARK 900 RELATED ID: 2C1B RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE
REMARK 900 COMPLEXED WITH (4R,2S)-5'-(4-(4-
REMARK 900 CHLOROBENZYLOXY)PYRROLIDIN-2-YLMETHANESULFONYL)
REMARK 900 ISOQUINOLINE
REMARK 900 RELATED ID: 2F7E RELATED DB: PDB
REMARK 900 PKA COMPLEXED WITH (S)-2-(1H-INDOL-3-YL
REMARK 900 )-1-(5-ISOQUINOLIN-6-YL-PYRIDIN-3-
REMARK 900 YLOXYMETHYL-ETYLAMINE
REMARK 900 RELATED ID: 2GNI RELATED DB: PDB
REMARK 900 PKA FIVEFOLD MUTANT MODEL OF RHO-KINASE
REMARK 900 WITH INHIBITORFASUDIL (HA1077)
REMARK 900 RELATED ID: 2JDS RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE
REMARK 900 COMPLEXED WITH A-443654
REMARK 900 RELATED ID: 2JDT RELATED DB: PDB
REMARK 900 STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH
REMARK 900 ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-
REMARK 900 CHLOROBENZYLOXY) ETHYLAMINO)ETHYL)AMIDE
REMARK 900 RELATED ID: 2JDV RELATED DB: PDB
REMARK 900 STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH
REMARK 900 A-443654
REMARK 900 RELATED ID: 1KMU RELATED DB: PDB
REMARK 900 MODEL STRUCTURE OF THE CATALYTIC SUBUNIT-
REMARK 900 REGULATORY SUBUNITDIMERIC COMPLEX OF THE CAMP
REMARK 900 -DEPENDENT PROTEIN KINASE
REMARK 900 RELATED ID: 1KMW RELATED DB: PDB
REMARK 900 MODEL STRUCTURE OF THE CATALYTIC SUBUNIT-
REMARK 900 REGULATORY SUBUNITDIMERIC COMPLEX OF THE C-
REMARK 900 AMP-DEPENDENT PROTEIN KINASE
REMARK 900 RELATED ID: 1Q24 RELATED DB: PDB
REMARK 900 PKA DOUBLE MUTANT MODEL OF PKB IN COMPLEX
REMARK 900 WITH MGATP
REMARK 900 RELATED ID: 1Q61 RELATED DB: PDB
REMARK 900 PKA TRIPLE MUTANT MODEL OF PKB
REMARK 900 RELATED ID: 1Q62 RELATED DB: PDB
REMARK 900 PKA DOUBLE MUTANT MODEL OF PKB
REMARK 900 RELATED ID: 1Q8T RELATED DB: PDB
REMARK 900 THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT
REMARK 900 PROTEIN KINASE(PKA) IN COMPLEX WITH RHO-
REMARK 900 KINASE INHIBITOR Y-27632
REMARK 900 RELATED ID: 1Q8U RELATED DB: PDB
REMARK 900 THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT
REMARK 900 PROTEIN KINASE INCOMPLEX WITH RHO-KINASE
REMARK 900 INHIBITOR H-1152P
REMARK 900 RELATED ID: 1Q8W RELATED DB: PDB
REMARK 900 THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT
REMARK 900 PROTEIN KINASE INCOMPLEX WITH RHO-KINASE
REMARK 900 INHIBITOR FASUDIL (HA-1077)
REMARK 900 RELATED ID: 1SMH RELATED DB: PDB
REMARK 900 PROTEIN KINASE A VARIANT COMPLEX WITH
REMARK 900 COMPLETELY ORDERED N-TERMINAL HELIX
REMARK 900 RELATED ID: 1STC RELATED DB: PDB
REMARK 900 CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC
REMARK 900 SUBUNIT INCOMPLEX WITH STAUROSPORINE
REMARK 900 RELATED ID: 1SVE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN KINASE A IN
REMARK 900 COMPLEX WITHAZEPANE DERIVATIVE 1
REMARK 900 RELATED ID: 1SVG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN KINASE A IN
REMARK 900 COMPLEX WITHAZEPANE DERIVATIVE 4
REMARK 900 RELATED ID: 1SVH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN KINASE A IN
REMARK 900 COMPLEX WITHAZEPANE DERIVATIVE 8
REMARK 900 RELATED ID: 1SZM RELATED DB: PDB
REMARK 900 DUAL BINDING MODE OF BISINDOLYLMALEIMIDE 2
REMARK 900 TO PROTEINKINASE A (PKA)
REMARK 900 RELATED ID: 1VEB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN KINASE A IN
REMARK 900 COMPLEX WITHAZEPANE DERIVATIVE 5
REMARK 900 RELATED ID: 1YDS RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE,
REMARK 900 ALPHA-CATALYTICSUBUNIT IN COMPLEX WITH H8
REMARK 900 PROTEIN KINASE INHIBITOR[N-(2-METHYLAMINO)
REMARK 900 ETHYL]-5-ISOQUINOLINESULFONAMIDE
REMARK 900 RELATED ID: 1YDT RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE,
REMARK 900 ALPHA-CATALYTICSUBUNIT IN COMPLEX WITH H89
REMARK 900 PROTEIN KINASE INHIBITORN-[2-(4-
REMARK 900 BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE
REMARK 900 RELATED ID: 2GFC RELATED DB: PDB
REMARK 900 CAMP-DEPENDENT PROTEIN KINASE PKA CATALYTIC
REMARK 900 SUBUNIT WITHPKI-5-24
REMARK 900 RELATED ID: 2GNF RELATED DB: PDB
REMARK 900 PROTEIN KINASE A FIVEFOLD MUTANT MODEL OF
REMARK 900 RHO-KINASE WITH Y-27632
REMARK 900 RELATED ID: 2GNG RELATED DB: PDB
REMARK 900 PROTEIN KINASE A FIVEFOLD MUTANT MODEL OF
REMARK 900 RHO-KINASE
REMARK 900 RELATED ID: 2GNH RELATED DB: PDB
REMARK 900 PKA FIVE FOLD MUTANT MODEL OF RHO-KINASE
REMARK 900 WITH H1152P
REMARK 900 RELATED ID: 2GNJ RELATED DB: PDB
REMARK 900 PKA THREE FOLD MUTANT MODEL OF RHO-KINASE
REMARK 900 WITH Y-27632
REMARK 900 RELATED ID: 2GNL RELATED DB: PDB
REMARK 900 PKA THREEFOLD MUTANT MODEL OF RHO-KINASE
REMARK 900 WITH INHIBITOR H-1152P
REMARK 900 RELATED ID: 2UVY RELATED DB: PDB
REMARK 900 STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH
REMARK 900 METHYL-(4-(9H-PURIN-6-YL)-BENZYL)-AMINE
REMARK 900 RELATED ID: 2UVZ RELATED DB: PDB
REMARK 900 STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH
REMARK 900 C-PHENYL-C-(4-(9H-PURIN-6-YL)-PHENYL
REMARK 900 )-METHYLAMINE
REMARK 900 RELATED ID: 2UW0 RELATED DB: PDB
REMARK 900 STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH
REMARK 900 6-(4-(4-(4-CHLORO-PHENYL)-PIPERIDIN-4-
REMARK 900 YL)-PHENYL)-9H-PURINE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 4 RESIDUES OF THE WILD-TYPE PKA SEQUENCE HAVE BEEN MUTATED
REMARK 999 TO THE CORRESPONDING RESIDUES IN PKB
DBREF 2UVX A 0 0 PDB 2UVX 2UVX 0 0
DBREF 2UVX A 1 350 UNP P00517 KAPCA_BOVIN 1 350
DBREF 2UVX I 5 24 UNP P61925 IPKA_HUMAN 5 24
SEQADV 2UVX THR A 104 UNP P00517 VAL 104 ENGINEERED MUTATION
SEQADV 2UVX ALA A 123 UNP P00517 VAL 123 ENGINEERED MUTATION
SEQADV 2UVX MET A 173 UNP P00517 LEU 173 ENGINEERED MUTATION
SEQADV 2UVX LYS A 181 UNP P00517 GLN 181 ENGINEERED MUTATION
SEQRES 1 A 351 MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN
SEQRES 2 A 351 GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP
SEQRES 3 A 351 PHE LEU LYS LYS TRP GLU ASN PRO ALA GLN ASN THR ALA
SEQRES 4 A 351 HIS LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR
SEQRES 5 A 351 GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS MET GLU
SEQRES 6 A 351 THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN
SEQRES 7 A 351 LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN
SEQRES 8 A 351 GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU
SEQRES 9 A 351 THR LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU
SEQRES 10 A 351 TYR MET VAL MET GLU TYR ALA PRO GLY GLY GLU MET PHE
SEQRES 11 A 351 SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS
SEQRES 12 A 351 ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU
SEQRES 13 A 351 TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS
SEQRES 14 A 351 PRO GLU ASN LEU MET ILE ASP GLN GLN GLY TYR ILE LYS
SEQRES 15 A 351 VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG
SEQRES 16 A 351 THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO
SEQRES 17 A 351 GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP
SEQRES 18 A 351 TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA
SEQRES 19 A 351 GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE
SEQRES 20 A 351 TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER
SEQRES 21 A 351 HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU
SEQRES 22 A 351 LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS
SEQRES 23 A 351 ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA
SEQRES 24 A 351 THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU
SEQRES 25 A 351 ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR
SEQRES 26 A 351 SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL
SEQRES 27 A 351 SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE
SEQRES 1 I 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 I 20 ARG ARG ASN ALA ILE HIS ASP
MODRES 2UVX TPO A 197 THR PHOSPHOTHREONINE
MODRES 2UVX SEP A 338 SER PHOSPHOSERINE
HET TPO A 197 11
HET SEP A 338 10
HET GVH A1351 9
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM GVH 1H-PYRROLO[2,3-B]PYRIDINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 GVH C7 H6 N2
FORMUL 4 HOH *382(H2 O1)
HELIX 1 1 SER A 14 ASN A 32 1 19
HELIX 2 2 HIS A 39 ASP A 41 5 3
HELIX 3 3 LYS A 76 LEU A 82 1 7
HELIX 4 4 GLN A 84 GLN A 96 1 13
HELIX 5 5 GLU A 127 GLY A 136 1 10
HELIX 6 6 SER A 139 LEU A 160 1 22
HELIX 7 7 LYS A 168 GLU A 170 5 3
HELIX 8 8 THR A 201 LEU A 205 5 5
HELIX 9 9 ALA A 206 LEU A 211 1 6
HELIX 10 10 LYS A 217 GLY A 234 1 18
HELIX 11 11 GLN A 242 GLY A 253 1 12
HELIX 12 12 SER A 262 LEU A 273 1 12
HELIX 13 13 VAL A 288 ASN A 293 1 6
HELIX 14 14 HIS A 294 ALA A 298 5 5
HELIX 15 15 ASP A 301 GLN A 307 1 7
HELIX 16 16 THR I 5 SER I 13 1 9
SHEET 1 AA 5 PHE A 43 GLY A 52 0
SHEET 2 AA 5 GLY A 55 HIS A 62 -1 O GLY A 55 N GLY A 52
SHEET 3 AA 5 HIS A 68 ASP A 75 -1 O TYR A 69 N VAL A 60
SHEET 4 AA 5 ASN A 115 GLU A 121 -1 O LEU A 116 N LEU A 74
SHEET 5 AA 5 LEU A 106 LYS A 111 -1 N GLU A 107 O VAL A 119
SHEET 1 AB 2 LEU A 162 ILE A 163 0
SHEET 2 AB 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 AC 2 LEU A 172 ILE A 174 0
SHEET 2 AC 2 ILE A 180 VAL A 182 -1 O LYS A 181 N MET A 173
SHEET 1 AD 2 CYS A 199 GLY A 200 0
SHEET 2 AD 2 ILE I 22 HIS I 23 -1 O ILE I 22 N GLY A 200
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.32
LINK C SEP A 338 N ILE A 339 1555 1555 1.34
SITE 1 AC1 5 LEU A 49 ALA A 70 THR A 104 GLU A 121
SITE 2 AC1 5 ALA A 123
CRYST1 72.537 74.400 79.869 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 0.013786 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013441 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012521 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
