HEADER TRANSFERASE 12-JAN-07 2JDV
TITLE STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH A-443654
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN KINASE A, PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: ALPHA-CATALYTIC SUBUNIT;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: RESIDUES 5-24;
COMPND 13 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR;
COMPND 14 ENGINEERED: YES
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 CAMP, KINASE, MYRISTATE, TRANSFERASE, LIPOPROTEIN, SERINE/THREONINE-
KEYWDS 2 PROTEIN KINASE, NUCLEOTIDE-BINDING, PROTEIN KINASE INHIBITOR, ATP-
KEYWDS 3 BINDING, NUCLEAR PROTEIN, PHOSPHORYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.G.DAVIES,M.L.VERDONK,B.GRAHAM,S.SAALAU-BETHELL,C.C.F.HAMLETT,
AUTHOR 2 T.MCHARDY,I.COLLINS,M.D.GARRETT,P.WORKMAN,S.J.WOODHEAD,H.JHOTI,
AUTHOR 3 D.BARFORD
REVDAT 4 13-DEC-23 2JDV 1 LINK
REVDAT 3 24-FEB-09 2JDV 1 VERSN
REVDAT 2 13-MAR-07 2JDV 1 JRNL
REVDAT 1 13-FEB-07 2JDV 0
JRNL AUTH T.G.DAVIES,M.L.VERDONK,B.GRAHAM,S.SAALAU-BETHELL,
JRNL AUTH 2 C.C.F.HAMLETT,T.MCHARDY,I.COLLINS,M.D.GARRETT,P.WORKMAN,
JRNL AUTH 3 S.J.WOODHEAD,H.JHOTI,D.BARFORD
JRNL TITL A STRUCTURAL COMPARISON OF INHIBITOR BINDING TO PKB, PKA AND
JRNL TITL 2 PKA-PKB CHIMERA
JRNL REF J.MOL.BIOL. V. 367 882 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17275837
JRNL DOI 10.1016/J.JMB.2007.01.004
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019F
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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 24115
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1273
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1601
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 93
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2935
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 303
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.78000
REMARK 3 B33 (A**2) : -0.94000
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): 0.243
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.147
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.369
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3044 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2134 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4109 ; 1.505 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5164 ; 0.953 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 356 ; 6.173 ; 5.084
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;36.676 ;23.882
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 542 ;16.027 ;15.092
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;17.718 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 425 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3337 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 665 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 598 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2226 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1457 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1500 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 79 ; 0.152 ; 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): 5 ; 0.146 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 14 ; 0.355 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.148 ; 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): 1772 ; 0.086 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2858 ; 0.109 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1272 ; 0.113 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1251 ; 0.132 ; 7.500
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 : 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 2JDV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1290031073.
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 : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24115
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 35.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: PDB ENTRY 1YDS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
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 36.40450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.18150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.39400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.18150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.40450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.39400
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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 465 SER A 14
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 ARG A 134 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG I 15 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG I 15 NE - CZ - NH2 ANGL. DEV. = -4.0 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 ASP A 166 44.24 -152.17
REMARK 500 ASP A 184 91.79 66.94
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 A2126 DISTANCE = 6.60 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L20 A1351
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KMU RELATED DB: PDB
REMARK 900 MODEL STRUCTURE OF THE CATALYTIC SUBUNIT- REGULATORY SUBUNITDIMERIC
REMARK 900 COMPLEX OF THE CAMP -DEPENDENT PROTEIN KINASE
REMARK 900 RELATED ID: 1KMW RELATED DB: PDB
REMARK 900 MODEL STRUCTURE OF THE CATALYTIC SUBUNIT- REGULATORY SUBUNITDIMERIC
REMARK 900 COMPLEX OF THE C- AMP-DEPENDENT PROTEIN KINASE
REMARK 900 RELATED ID: 1Q24 RELATED DB: PDB
REMARK 900 PKA DOUBLE MUTANT MODEL OF PKB IN COMPLEX 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 PROTEIN KINASE(PKA) IN
REMARK 900 COMPLEX WITH RHO- KINASE INHIBITOR Y-27632
REMARK 900 RELATED ID: 1Q8U RELATED DB: PDB
REMARK 900 THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE INCOMPLEX
REMARK 900 WITH RHO-KINASE INHIBITOR H-1152P
REMARK 900 RELATED ID: 1Q8W RELATED DB: PDB
REMARK 900 THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE INCOMPLEX
REMARK 900 WITH RHO-KINASE INHIBITOR FASUDIL (HA-1077)
REMARK 900 RELATED ID: 1SMH RELATED DB: PDB
REMARK 900 PROTEIN KINASE A VARIANT COMPLEX WITH COMPLETELY ORDERED N-TERMINAL
REMARK 900 HELIX
REMARK 900 RELATED ID: 1STC RELATED DB: PDB
REMARK 900 CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT INCOMPLEX
REMARK 900 WITH STAUROSPORINE
REMARK 900 RELATED ID: 1SVE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN KINASE A IN COMPLEX WITHAZEPANE
REMARK 900 DERIVATIVE 1
REMARK 900 RELATED ID: 1SVG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN KINASE A IN COMPLEX WITHAZEPANE
REMARK 900 DERIVATIVE 4
REMARK 900 RELATED ID: 1SVH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN KINASE A IN COMPLEX WITHAZEPANE
REMARK 900 DERIVATIVE 8
REMARK 900 RELATED ID: 1SZM RELATED DB: PDB
REMARK 900 DUAL BINDING MODE OF BISINDOLYLMALEIMIDE 2 TO PROTEINKINASE A (PKA)
REMARK 900 RELATED ID: 1VEB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEIN KINASE A IN COMPLEX WITHAZEPANE
REMARK 900 DERIVATIVE 5
REMARK 900 RELATED ID: 1XH4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B SELECTIVE INHIBITORSIN
REMARK 900 COMPLEX WITH PROTEIN KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B SELECTIVE INHIBITORSIN
REMARK 900 COMPLEX WITH PROTEIN KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B SELECTIVE INHIBITORSIN
REMARK 900 COMPLEX WITH PROTEIN KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B SELECTIVE INHIBITORSIN
REMARK 900 COMPLEX WITH PROTEIN KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B SELECTIVE INHIBITORSIN
REMARK 900 COMPLEX WITH PROTEIN KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XH9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B SELECTIVE INHIBITORSIN
REMARK 900 COMPLEX WITH PROTEIN KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1XHA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTEIN KINASE B SELECTIVE INHIBITORSIN
REMARK 900 COMPLEX WITH PROTEIN KINASE A AND MUTANTS
REMARK 900 RELATED ID: 1YDR RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTICSUBUNIT
REMARK 900 IN COMPLEX WITH H7 PROTEIN KINASE INHIBITOR1-(5-
REMARK 900 ISOQUINOLINESULFONYL)-2-METHYLPIPERAZINE
REMARK 900 RELATED ID: 1YDS RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTICSUBUNIT
REMARK 900 IN COMPLEX WITH H8 PROTEIN KINASE INHIBITOR[N-(2-METHYLAMINO) ETHYL]
REMARK 900 -5-ISOQUINOLINESULFONAMIDE
REMARK 900 RELATED ID: 1YDT RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTICSUBUNIT
REMARK 900 IN COMPLEX WITH H89 PROTEIN KINASE INHIBITORN-[2-(4-
REMARK 900 BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE
REMARK 900 RELATED ID: 2C1A RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH
REMARK 900 ISOQUINOLINE-5-SULFONIC ACID ( 2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)
REMARK 900 ETHYL) AMIDE
REMARK 900 RELATED ID: 2C1B RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH (4R,2S)-5'
REMARK 900 -(4-(4- CHLOROBENZYLOXY)PYRROLIDIN-2-YLMETHANESULFONYL) ISOQUINOLINE
REMARK 900 RELATED ID: 2F7E RELATED DB: PDB
REMARK 900 PKA COMPLEXED WITH (S)-2-(1H-INDOL-3-YL )-1-(5-ISOQUINOLIN-6-YL-
REMARK 900 PYRIDIN-3- YLOXYMETHYL-ETYLAMINE
REMARK 900 RELATED ID: 2GFC RELATED DB: PDB
REMARK 900 CAMP-DEPENDENT PROTEIN KINASE PKA CATALYTIC SUBUNIT WITHPKI-5-24
REMARK 900 RELATED ID: 2GNF RELATED DB: PDB
REMARK 900 PROTEIN KINASE A FIVEFOLD MUTANT MODEL OF RHO-KINASE WITH Y-27632
REMARK 900 RELATED ID: 2GNG RELATED DB: PDB
REMARK 900 PROTEIN KINASE A FIVEFOLD MUTANT MODEL OF RHO-KINASE
REMARK 900 RELATED ID: 2GNH RELATED DB: PDB
REMARK 900 PKA FIVE FOLD MUTANT MODEL OF RHO-KINASE WITH H1152P
REMARK 900 RELATED ID: 2GNI RELATED DB: PDB
REMARK 900 PKA FIVEFOLD MUTANT MODEL OF RHO-KINASE WITH INHIBITORFASUDIL
REMARK 900 (HA1077)
REMARK 900 RELATED ID: 2GNJ RELATED DB: PDB
REMARK 900 PKA THREE FOLD MUTANT MODEL OF RHO-KINASE WITH Y-27632
REMARK 900 RELATED ID: 2GNL RELATED DB: PDB
REMARK 900 PKA THREEFOLD MUTANT MODEL OF RHO-KINASE WITH INHIBITOR H-1152P
REMARK 900 RELATED ID: 1CMK RELATED DB: PDB
REMARK 900 RELATED ID: 2JDO RELATED DB: PDB
REMARK 900 STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH ISOQUINOLINE-5-SULFONIC
REMARK 900 ACID (2-(2-(4- CHLOROBENZYLOXY) ETHYLAMINO)ETHYL)AMIDE
REMARK 900 RELATED ID: 2JDR RELATED DB: PDB
REMARK 900 STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH THE INHIBITOR A-443654
REMARK 900 RELATED ID: 2JDS RELATED DB: PDB
REMARK 900 STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A-443654
REMARK 900 RELATED ID: 2JDT RELATED DB: PDB
REMARK 900 STRUCTURE OF PKA-PKB CHIMERA COMPLEXED WITH ISOQUINOLINE-5-SULFONIC
REMARK 900 ACID (2-(2-(4- CHLOROBENZYLOXY) ETHYLAMINO)ETHYL)AMIDE
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 2JDV A 0 0 PDB 2JDV 2JDV 0 0
DBREF 2JDV A 1 350 UNP P00517 KAPCA_BOVIN 1 350
DBREF 2JDV I 5 24 UNP P61925 IPKA_HUMAN 5 24
SEQADV 2JDV THR A 104 UNP P00517 VAL 104 ENGINEERED MUTATION
SEQADV 2JDV ALA A 123 UNP P00517 VAL 123 ENGINEERED MUTATION
SEQADV 2JDV MET A 173 UNP P00517 LEU 173 ENGINEERED MUTATION
SEQADV 2JDV 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 2JDV TPO A 197 THR PHOSPHOTHREONINE
MODRES 2JDV SEP A 338 SER PHOSPHOSERINE
HET TPO A 197 11
HET SEP A 338 10
HET L20 A1351 30
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM L20 (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-
HETNAM 2 L20 YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 L20 C24 H23 N5 O
FORMUL 4 HOH *303(H2 O)
HELIX 1 1 VAL A 15 ASN A 32 1 18
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 VAL A 98 1 15
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
LINK C TRP A 196 N TPO A 197 1555 1555 1.34
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.34
LINK C SEP A 338 N ILE A 339 1555 1555 1.34
SITE 1 AC1 14 LEU A 49 ALA A 70 LYS A 72 THR A 104
SITE 2 AC1 14 GLU A 121 TYR A 122 ALA A 123 GLU A 127
SITE 3 AC1 14 ASN A 171 MET A 173 THR A 183 ASP A 184
SITE 4 AC1 14 PHE A 327 HOH A2271
CRYST1 72.809 74.788 80.363 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 0.013735 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013371 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012444 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
