HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-JAN-12 4DG2
TITLE CRYSTAL STRUCTURE OF MYRISTOYLATED WT CATALYTIC SUBUNIT OF CAMP-
TITLE 2 DEPENDENT PROTEIN KINASE IN COMPLEX WITH SP20
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 3 02-JAN-13 4DG2 1 JRNL
REVDAT 2 25-JUL-12 4DG2 1 REMARK
REVDAT 1 06-JUN-12 4DG2 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) : 39.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.8
REMARK 3 NUMBER OF REFLECTIONS : 24598
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1310
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) : 1760
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2987
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 308
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.39000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -1.44000
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): 0.226
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.063
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3083 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4162 ; 0.866 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 372 ; 4.383 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;35.823 ;23.986
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 536 ;12.802 ;15.028
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.499 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 442 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2330 ; 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): 1844 ; 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): 2964 ; 0.446 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1239 ; 0.598 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1196 ; 1.022 ; 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 : 3
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 5 E 350
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5360 5.3970 -24.0760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0072 T22: 0.0084
REMARK 3 T33: 0.0342 T12: -0.0003
REMARK 3 T13: 0.0120 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.6299 L22: 1.5369
REMARK 3 L33: 2.6666 L12: 0.2652
REMARK 3 L13: 0.0096 L23: 0.8567
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: -0.0459 S13: -0.0042
REMARK 3 S21: 0.0719 S22: -0.0488 S23: 0.0469
REMARK 3 S31: 0.0340 S32: 0.0127 S33: 0.0182
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): 3.4900 -6.0210 -32.4200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0630 T22: 0.0488
REMARK 3 T33: 0.0591 T12: 0.0217
REMARK 3 T13: -0.0090 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.6749 L22: 10.4797
REMARK 3 L33: 13.5178 L12: -1.1096
REMARK 3 L13: 0.8087 L23: 9.7888
REMARK 3 S TENSOR
REMARK 3 S11: -0.1103 S12: -0.2097 S13: 0.2035
REMARK 3 S21: -0.2621 S22: 0.0949 S23: -0.4301
REMARK 3 S31: -0.5304 S32: 0.0336 S33: 0.0154
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 501 E 752
REMARK 3 RESIDUE RANGE : I 101 I 130
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2010 5.3810 -23.9280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1263 T22: 0.1483
REMARK 3 T33: 0.1596 T12: -0.0032
REMARK 3 T13: 0.0016 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.3405 L22: 0.7034
REMARK 3 L33: 1.2425 L12: 0.1191
REMARK 3 L13: -0.2437 L23: 0.5135
REMARK 3 S TENSOR
REMARK 3 S11: 0.0314 S12: -0.0454 S13: -0.0063
REMARK 3 S21: 0.0369 S22: -0.0353 S23: 0.0274
REMARK 3 S31: 0.0085 S32: -0.0059 S33: 0.0038
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 4DG2 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 RCSB070283.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-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 : 25942
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07300
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 (%) : 80.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.900
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 (%): 53.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MOTHER LIQUOR: 6% MPD PROTEIN
REMARK 280 SOLUTION: 50 MM BICINE, 150 MM AMMONIUM ACETATE, 10 MM DTT, 8-10
REMARK 280 MG/ML 9% MEOH, 1:1 PROTEIN:MOTHER LIQUOR, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 24.24000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.94500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.81500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.94500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.24000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.81500
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: 2610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 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 LYS E 8 CG CD CE NZ
REMARK 470 GLU E 13 CG CD OE1 OE2
REMARK 470 GLU E 17 CG CD OE1 OE2
REMARK 470 LYS E 21 CD CE NZ
REMARK 470 LYS E 83 CE NZ
REMARK 470 SEP E 139 P O1P O2P O3P
REMARK 470 ARG E 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 317 CG CD CE NZ
REMARK 470 PHE E 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU E 334 CG CD OE1 OE2
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 166 40.43 -147.04
REMARK 500 ASP E 184 88.02 63.45
REMARK 500 ASN E 216 -160.09 -128.26
REMARK 500 LEU E 273 49.84 -88.77
REMARK 500 LYS E 319 32.94 -99.35
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 534 DISTANCE = 5.02 ANGSTROMS
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 CHAIN I OF CAMP-DEPENDENT
REMARK 800 PROTEIN KINASE INHIBITOR ALPHA
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DG0 RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH AMP-PNP AND SP20.
REMARK 900 RELATED ID: 4DFX RELATED DB: PDB
REMARK 900 MYR-K7C CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH SP20 AND
REMARK 900 AMP-PNP.
REMARK 900 RELATED ID: 4DFZ RELATED DB: PDB
REMARK 900 MYR-K7C CATALYTIC SUBUNIT OF PKA 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: 1CTP RELATED DB: PDB
REMARK 900 MYRISTOYLATED CATALYTIC SUBUNIT OF PKA BOUND TO IP20.
REMARK 900 RELATED ID: 1JBP RELATED DB: PDB
REMARK 900 THE CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH ADP AND SP20.
DBREF 4DG2 E 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 4DG2 I 5 24 UNP P63248 IPKA_MOUSE 6 25
SEQADV 4DG2 ALA I 20 UNP P63248 ASN 21 ENGINEERED MUTATION
SEQADV 4DG2 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 4DG2 SEP E 139 SER PHOSPHOSERINE
MODRES 4DG2 TPO E 197 THR PHOSPHOTHREONINE
MODRES 4DG2 SEP E 338 SER PHOSPHOSERINE
HET SEP E 139 6
HET TPO E 197 11
HET SEP E 338 10
HET MYR E 401 15
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM MYR MYRISTIC ACID
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 HOH *308(H2 O)
HELIX 1 1 GLY E 1 LYS E 7 1 7
HELIX 2 2 GLU E 11 THR E 32 1 22
HELIX 3 3 GLN E 39 ASP E 41 5 3
HELIX 4 4 LYS E 76 LEU E 82 1 7
HELIX 5 5 GLN E 84 GLN E 96 1 13
HELIX 6 6 GLU E 127 GLY E 136 1 10
HELIX 7 7 SEP E 139 LEU E 160 1 22
HELIX 8 8 LYS E 168 GLU E 170 5 3
HELIX 9 9 THR E 201 LEU E 205 5 5
HELIX 10 10 ALA E 206 LEU E 211 1 6
HELIX 11 11 LYS E 217 GLY E 234 1 18
HELIX 12 12 GLN E 242 SER E 252 1 11
HELIX 13 13 SER E 262 LEU E 273 1 12
HELIX 14 14 VAL E 288 ASN E 293 1 6
HELIX 15 15 HIS E 294 ALA E 298 5 5
HELIX 16 16 ASP E 301 GLN E 307 1 7
HELIX 17 17 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 MET E 71 N MET E 58
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 108 O VAL E 119
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
SHEET 1 D 2 CYS E 199 GLY E 200 0
SHEET 2 D 2 ILE I 22 HIS I 23 -1 O ILE I 22 N GLY E 200
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 N GLY E 1 C1 MYR E 401 1555 1555 1.50
SITE 1 AC1 7 GLY E 1 ASN E 2 ALA E 3 ALA E 4
SITE 2 AC1 7 SER E 14 LEU E 152 ASP I 24
SITE 1 AC2 61 GLY E 1 ASN E 2 ALA E 3 GLN E 84
SITE 2 AC2 61 GLU E 86 ARG E 93 GLU E 127 PHE E 129
SITE 3 AC2 61 SER E 130 ARG E 133 ASP E 166 LYS E 168
SITE 4 AC2 61 PRO E 169 GLU E 170 PHE E 187 LYS E 189
SITE 5 AC2 61 ARG E 190 VAL E 191 LYS E 192 LEU E 198
SITE 6 AC2 61 CYS E 199 GLY E 200 PRO E 202 GLU E 203
SITE 7 AC2 61 GLU E 230 GLY E 234 TYR E 235 PRO E 236
SITE 8 AC2 61 PHE E 239 ASP E 241 ASP E 328 TYR E 330
SITE 9 AC2 61 GLU E 349 MYR E 401 HOH E 507 HOH E 543
SITE 10 AC2 61 HOH E 544 HOH E 665 HOH E 679 HOH E 680
SITE 11 AC2 61 HOH E 731 HOH I 103 HOH I 104 HOH I 106
SITE 12 AC2 61 HOH I 108 HOH I 110 HOH I 111 HOH I 112
SITE 13 AC2 61 HOH I 113 HOH I 114 HOH I 115 HOH I 117
SITE 14 AC2 61 HOH I 119 HOH I 120 HOH I 121 HOH I 122
SITE 15 AC2 61 HOH I 125 HOH I 126 HOH I 127 HOH I 130
SITE 16 AC2 61 HOH I 131
CRYST1 48.480 79.630 117.890 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 0.020627 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012558 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008482 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
