HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-JAN-12 4DG0
TITLE CRYSTAL STRUCTURE OF MYRISTOYLATED WT CATALYTIC SUBUNIT OF CAMP-
TITLE 2 DEPENDENT PROTEIN KINASE IN COMPLEX WITH SP20 AND AMP-PNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: E;
COMPND 4 FRAGMENT: UNP RESIDUES 2-351;
COMPND 5 SYNONYM: PKA C-ALPHA;
COMPND 6 EC: 2.7.11.11;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 10 CHAIN: I;
COMPND 11 FRAGMENT: UNP RESIDUES 6-25;
COMPND 12 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,
COMPND 13 MUSCLE/BRAIN ISOFORM;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRKACA, PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090
KEYWDS PROTEIN KINASE, MYRISTOYLATED, PHOSPHOTRANSFERASE OF SER/THR, MG,
KEYWDS 2 PKI, PKA REGULATORY SUBUNITS, PHOSPHORYLATED ON S139, T197, S338,
KEYWDS 3 MYRISTOYLATED ON G1, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.BASTIDAS,J.M.STEICHEN,S.S.TAYLOR
REVDAT 2 02-JAN-13 4DG0 1 JRNL
REVDAT 1 06-JUN-12 4DG0 0
JRNL AUTH A.C.BASTIDAS,M.S.DEAL,J.M.STEICHEN,M.M.KESHWANI,Y.GUO,
JRNL AUTH 2 S.S.TAYLOR
JRNL TITL ROLE OF N-TERMINAL MYRISTYLATION IN THE STRUCTURE AND
JRNL TITL 2 REGULATION OF CAMP-DEPENDENT PROTEIN KINASE.
JRNL REF J.MOL.BIOL. V. 422 215 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22617327
JRNL DOI 10.1016/J.JMB.2012.05.021
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 39.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 29601
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1572
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) : 2165
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2951
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 344
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.09000
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): 0.180
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.302
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3096 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4190 ; 0.951 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 369 ; 4.529 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 150 ;34.244 ;23.933
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 545 ;12.971 ;15.055
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;15.595 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 441 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2322 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1810 ; 0.232 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2920 ; 0.444 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1286 ; 0.593 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1265 ; 0.996 ; 4.500
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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 10 E 350
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3317 -13.5081 21.0208
REMARK 3 T TENSOR
REMARK 3 T11: 0.0042 T22: 0.0311
REMARK 3 T33: 0.0743 T12: 0.0015
REMARK 3 T13: 0.0024 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.4681 L22: 1.1342
REMARK 3 L33: 2.2173 L12: -0.0323
REMARK 3 L13: 0.2103 L23: 0.7866
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: 0.0024 S13: 0.0082
REMARK 3 S21: 0.0273 S22: -0.0067 S23: 0.0557
REMARK 3 S31: 0.0175 S32: -0.0105 S33: 0.0202
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 5 I 24
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0853 -2.4947 26.2690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0456 T22: 0.0475
REMARK 3 T33: 0.0502 T12: -0.0011
REMARK 3 T13: 0.0074 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 2.0923 L22: 6.4736
REMARK 3 L33: 6.2554 L12: 2.5318
REMARK 3 L13: 2.4898 L23: 4.3371
REMARK 3 S TENSOR
REMARK 3 S11: -0.0276 S12: 0.1346 S13: -0.1904
REMARK 3 S21: 0.0304 S22: 0.1666 S23: -0.4190
REMARK 3 S31: 0.2849 S32: 0.2854 S33: -0.1390
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 402 E 402
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7369 -8.4045 13.9098
REMARK 3 T TENSOR
REMARK 3 T11: 0.0827 T22: 0.1160
REMARK 3 T33: 0.0686 T12: 0.0103
REMARK 3 T13: -0.0131 T23: -0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 1.1953 L22: 7.7681
REMARK 3 L33: 6.6145 L12: 2.7857
REMARK 3 L13: 1.6212 L23: 1.4061
REMARK 3 S TENSOR
REMARK 3 S11: -0.1000 S12: 0.0044 S13: -0.1839
REMARK 3 S21: -0.5048 S22: 0.2296 S23: -0.4522
REMARK 3 S31: -0.0852 S32: -0.2311 S33: -0.1297
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 501 E 731
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2980 -12.2726 19.4716
REMARK 3 T TENSOR
REMARK 3 T11: 0.0669 T22: 0.1070
REMARK 3 T33: 0.1238 T12: -0.0032
REMARK 3 T13: 0.0121 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.3526 L22: 0.7526
REMARK 3 L33: 1.5628 L12: 0.0840
REMARK 3 L13: 0.2960 L23: 0.4030
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: -0.0236 S13: 0.0136
REMARK 3 S21: 0.0052 S22: -0.0301 S23: 0.0562
REMARK 3 S31: 0.0142 S32: -0.0026 S33: 0.0564
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 403 E 403
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5390 -13.6204 15.9170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0498 T22: 0.1079
REMARK 3 T33: 0.1365 T12: -0.0032
REMARK 3 T13: -0.0428 T23: 0.1064
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 404 E 404
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8390 -10.0623 17.0670
REMARK 3 T TENSOR
REMARK 3 T11: 0.0733 T22: 0.0126
REMARK 3 T33: 0.0898 T12: -0.0246
REMARK 3 T13: -0.0633 T23: 0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4DG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB070281.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31277
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11400
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.38700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MOTHER LIQUOR: 10% MPD PROTEIN
REMARK 280 SOLUTION: 50 MM BICINE, 150 MM AMMONIUM ACETATE, 8-10 MG/ML 9%
REMARK 280 MEOH ADDED TO THE WELL IMMEDIATELY BEFORE SEALING. 8 UL DROP SIZE
REMARK 280 WITH 1:1 PROTEIN:MOTHER LIQUOR, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277.15K, PH 8.0
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 28.90000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.50000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.36500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.50000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.36500
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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 E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 3
REMARK 465 ALA E 4
REMARK 465 ALA E 5
REMARK 465 ALA E 6
REMARK 465 LYS E 7
REMARK 465 LYS E 8
REMARK 465 GLY E 9
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 GLU E 11 CG CD OE1 OE2
REMARK 470 GLN E 12 CG CD OE1 NE2
REMARK 470 GLU E 13 CG CD OE1 OE2
REMARK 470 SER E 14 OG
REMARK 470 PHE E 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS E 319 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS E 87 NE2 HIS E 87 CD2 -0.067
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 E 112 -162.28 -126.67
REMARK 500 ASP E 166 45.63 -146.43
REMARK 500 ASP E 184 79.89 65.44
REMARK 500 LYS E 319 56.06 -97.86
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 E 513 DISTANCE = 6.44 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 MYR E 401
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 MG E 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP E 402 O3G
REMARK 620 2 HOH E 597 O 112.2
REMARK 620 3 ANP E 402 O1B 86.0 102.1
REMARK 620 4 HOH E 598 O 100.0 87.3 166.2
REMARK 620 5 ASP E 184 OD1 147.8 99.4 81.5 87.0
REMARK 620 6 ASP E 184 OD2 93.9 153.5 83.5 83.7 55.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP E 402 O2G
REMARK 620 2 ANP E 402 O2A 147.9
REMARK 620 3 ASN E 171 OD1 114.6 96.7
REMARK 620 4 HOH E 599 O 101.5 88.0 84.5
REMARK 620 5 ASP E 184 OD2 85.4 88.1 89.2 172.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT
REMARK 800 PROTEIN KINASE INHIBITOR ALPHA
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DFX RELATED DB: PDB
REMARK 900 SAME COMPLEX WITH MYR-K7C
REMARK 900 RELATED ID: 4DFZ RELATED DB: PDB
REMARK 900 MYR-K7C IN COMPLEX WITH SP20
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 THE CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH ATP AND IP20.
REMARK 900 RELATED ID: 1JBP RELATED DB: PDB
REMARK 900 THE CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH ADP AND SP20.
REMARK 900 RELATED ID: 1CTP RELATED DB: PDB
REMARK 900 MYRISTOYLATED CATALYTIC SUBUNIT OF PKA BOUND TO IP20.
REMARK 900 RELATED ID: 4DG2 RELATED DB: PDB
DBREF 4DG0 E 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 4DG0 I 5 24 UNP P63248 IPKA_MOUSE 6 25
SEQADV 4DG0 ALA I 20 UNP P63248 ASN 21 ENGINEERED MUTATION
SEQADV 4DG0 SER I 21 UNP P63248 ALA 22 ENGINEERED MUTATION
SEQRES 1 E 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 E 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 E 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 E 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 E 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 E 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 E 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 E 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 E 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 E 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 E 350 HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA
SEQRES 12 E 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 E 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 E 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 E 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 E 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 E 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 E 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 E 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 E 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 E 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 E 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 E 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 E 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 E 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 E 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 E 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR 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 ALA SER ILE HIS ASP
MODRES 4DG0 SEP E 139 SER PHOSPHOSERINE
MODRES 4DG0 TPO E 197 THR PHOSPHOTHREONINE
MODRES 4DG0 SEP E 338 SER PHOSPHOSERINE
HET SEP E 139 10
HET TPO E 197 11
HET SEP E 338 10
HET MYR E 401 15
HET ANP E 402 31
HET MG E 403 1
HET MG E 404 1
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM MYR MYRISTIC ACID
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 MYR C14 H28 O2
FORMUL 4 ANP C10 H17 N6 O12 P3
FORMUL 5 MG 2(MG 2+)
FORMUL 7 HOH *344(H2 O)
HELIX 1 1 GLN E 12 THR E 32 1 21
HELIX 2 2 GLN E 39 ASP E 41 5 3
HELIX 3 3 LYS E 76 LEU E 82 1 7
HELIX 4 4 GLN E 84 GLN E 96 1 13
HELIX 5 5 GLU E 127 GLY E 136 1 10
HELIX 6 6 SEP E 139 LEU E 160 1 22
HELIX 7 7 LYS E 168 GLU E 170 5 3
HELIX 8 8 THR E 201 LEU E 205 5 5
HELIX 9 9 ALA E 206 LEU E 211 1 6
HELIX 10 10 LYS E 217 GLY E 234 1 18
HELIX 11 11 GLN E 242 GLY E 253 1 12
HELIX 12 12 SER E 262 LEU E 273 1 12
HELIX 13 13 VAL E 288 ASN E 293 1 6
HELIX 14 14 HIS E 294 ALA E 298 5 5
HELIX 15 15 ASP E 301 GLN E 307 1 7
HELIX 16 16 THR I 6 ALA I 12 1 7
SHEET 1 A 5 PHE E 43 THR E 51 0
SHEET 2 A 5 GLY E 55 HIS E 62 -1 O LEU E 59 N LYS E 47
SHEET 3 A 5 HIS E 68 ASP E 75 -1 O ILE E 73 N ARG E 56
SHEET 4 A 5 ASN E 115 GLU E 121 -1 O MET E 118 N LYS E 72
SHEET 5 A 5 LEU E 106 LYS E 111 -1 N PHE E 110 O TYR E 117
SHEET 1 B 2 LEU E 162 ILE E 163 0
SHEET 2 B 2 LYS E 189 ARG E 190 -1 O LYS E 189 N ILE E 163
SHEET 1 C 2 LEU E 172 ILE E 174 0
SHEET 2 C 2 ILE E 180 VAL E 182 -1 O GLN E 181 N LEU E 173
LINK C PHE E 138 N SEP E 139 1555 1555 1.33
LINK C SEP E 139 N GLU E 140 1555 1555 1.33
LINK C TRP E 196 N TPO E 197 1555 1555 1.33
LINK C TPO E 197 N LEU E 198 1555 1555 1.33
LINK C VAL E 337 N SEP E 338 1555 1555 1.33
LINK C SEP E 338 N ILE E 339 1555 1555 1.33
LINK O3G ANP E 402 MG MG E 403 1555 1555 1.93
LINK O2G ANP E 402 MG MG E 404 1555 1555 1.93
LINK MG MG E 403 O HOH E 597 1555 1555 1.96
LINK O1B ANP E 402 MG MG E 403 1555 1555 2.05
LINK O2A ANP E 402 MG MG E 404 1555 1555 2.06
LINK OD1 ASN E 171 MG MG E 404 1555 1555 2.16
LINK MG MG E 404 O HOH E 599 1555 1555 2.19
LINK OD2 ASP E 184 MG MG E 404 1555 1555 2.25
LINK MG MG E 403 O HOH E 598 1555 1555 2.29
LINK OD1 ASP E 184 MG MG E 403 1555 1555 2.34
LINK OD2 ASP E 184 MG MG E 403 1555 1555 2.38
CISPEP 1 HIS I 23 ASP I 24 0 0.18
SITE 1 AC1 1 GLU E 155
SITE 1 AC2 28 GLY E 52 VAL E 57 ALA E 70 LYS E 72
SITE 2 AC2 28 VAL E 104 MET E 120 GLU E 121 TYR E 122
SITE 3 AC2 28 VAL E 123 GLU E 127 ASP E 166 LYS E 168
SITE 4 AC2 28 GLU E 170 ASN E 171 LEU E 173 THR E 183
SITE 5 AC2 28 ASP E 184 PHE E 327 MG E 403 MG E 404
SITE 6 AC2 28 HOH E 521 HOH E 522 HOH E 599 HOH E 642
SITE 7 AC2 28 HOH E 748 HOH E 751 ARG I 18 SER I 21
SITE 1 AC3 4 ASP E 184 ANP E 402 HOH E 597 HOH E 598
SITE 1 AC4 4 ASN E 171 ASP E 184 ANP E 402 HOH E 599
SITE 1 AC5 63 LEU E 82 GLN E 84 GLU E 86 HIS E 87
SITE 2 AC5 63 LEU E 89 ARG E 93 GLU E 127 PHE E 129
SITE 3 AC5 63 ARG E 133 ASP E 166 LYS E 168 PRO E 169
SITE 4 AC5 63 GLU E 170 PHE E 187 LYS E 189 ARG E 190
SITE 5 AC5 63 VAL E 191 LYS E 192 TPO E 197 LEU E 198
SITE 6 AC5 63 CYS E 199 GLY E 200 GLU E 203 GLU E 230
SITE 7 AC5 63 TYR E 235 PRO E 236 PHE E 239 ALA E 240
SITE 8 AC5 63 ASP E 241 PRO E 243 TYR E 330 GLU E 349
SITE 9 AC5 63 ANP E 402 HOH E 513 HOH E 514 HOH E 518
SITE 10 AC5 63 HOH E 523 HOH E 594 HOH E 608 HOH E 735
SITE 11 AC5 63 HOH I 101 HOH I 102 HOH I 103 HOH I 104
SITE 12 AC5 63 HOH I 105 HOH I 106 HOH I 107 HOH I 108
SITE 13 AC5 63 HOH I 109 HOH I 111 HOH I 112 HOH I 114
SITE 14 AC5 63 HOH I 115 HOH I 116 HOH I 117 HOH I 118
SITE 15 AC5 63 HOH I 119 HOH I 121 HOH I 124 HOH I 126
SITE 16 AC5 63 HOH I 127 HOH I 130 HOH I 131
CRYST1 57.800 78.730 99.000 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 0.017301 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010101 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
