HEADER TRANSFERASE 20-JUL-09 3IDC
TITLE CRYSTAL STRUCTURE OF (102-265)RIIB:C HOLOENZYME OF CAMP-DEPENDENT
TITLE 2 PROTEIN KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ISOFORM 1 (C-ALPHA-1): UNP RESIDUES 2-351;
COMPND 5 SYNONYM: PKA C-ALPHA;
COMPND 6 EC: 2.7.11.11;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: (102-265)RIIB:C HOLOENZYME OF CAMP-DEPENDENT PROTEIN
COMPND 9 KINASE;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY
COMPND 12 SUBUNIT;
COMPND 13 CHAIN: B;
COMPND 14 FRAGMENT: UNP RESIDUES 102-265;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PKACA, PRKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 12 ORGANISM_COMMON: RAT;
SOURCE 13 ORGANISM_TAXID: 10116;
SOURCE 14 GENE: PRKAR2B;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PRSET
KEYWDS PKA, CAMP, SPR, AFFINITY, KINASE, LINKER, RII HOLOENZYME, ALTERNATIVE
KEYWDS 2 SPLICING, ATP-BINDING, CYTOPLASM, LIPOPROTEIN, MYRISTATE,
KEYWDS 3 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-
KEYWDS 4 PROTEIN KINASE, TRANSFERASE, ACETYLATION, CAMP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.J.BROWN,J.WU,C.KIM,K.ALBERTO,S.S.TAYLOR
REVDAT 3 24-JUL-19 3IDC 1 REMARK LINK
REVDAT 2 10-NOV-09 3IDC 1 JRNL
REVDAT 1 29-SEP-09 3IDC 0
JRNL AUTH S.H.BROWN,J.WU,C.KIM,K.ALBERTO,S.S.TAYLOR
JRNL TITL NOVEL ISOFORM-SPECIFIC INTERFACES REVEALED BY PKA RIIBETA
JRNL TITL 2 HOLOENZYME STRUCTURES.
JRNL REF J.MOL.BIOL. V. 393 1070 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19748511
JRNL DOI 10.1016/J.JMB.2009.09.014
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 25383
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) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.319
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3872
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 43
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 29.46000
REMARK 3 B22 (A**2) : 5.70000
REMARK 3 B33 (A**2) : -35.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 13.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3IDC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054269.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5200
REMARK 200 MONOCHROMATOR : KOHZU: 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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25383
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.700
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: PDB ENTRY 1ATP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, 40 MM BIS-TRIS PH 7.5,
REMARK 280 0.05 MM NA ACETATE, VAPOR DIFFUSION UNDER OIL (VDUO),
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 89.63600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.71700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 89.63600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.71700
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: 3080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 PRO B 102
REMARK 465 SER B 129
REMARK 465 ARG B 130
REMARK 465 ILE B 131
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 A 8 CG CD CE NZ
REMARK 470 GLN A 12 CG CD OE1 NE2
REMARK 470 LYS A 16 CG CD CE NZ
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 THR A 32 OG1 CG2
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 SER A 65 OG
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 LEU A 82 CG CD1 CD2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 LYS A 111 CG CD CE NZ
REMARK 470 GLU A 248 CG CD OE1 OE2
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 ILE A 305 CG1 CG2 CD1
REMARK 470 VAL A 310 CG1 CG2
REMARK 470 GLU A 311 CG CD OE1 OE2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 ARG A 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 339 CG1 CG2 CD1
REMARK 470 ILE B 104 CG1 CG2 CD1
REMARK 470 ASN B 105 CG OD1 ND2
REMARK 470 ASN B 119 CG OD1 ND2
REMARK 470 GLU B 122 CG CD OE1 OE2
REMARK 470 GLU B 123 CG CD OE1 OE2
REMARK 470 GLU B 124 CG CD OE1 OE2
REMARK 470 ASP B 125 CG OD1 OD2
REMARK 470 ASP B 126 CG OD1 OD2
REMARK 470 GLU B 128 CA C O CB CG CD OE1
REMARK 470 GLU B 128 OE2
REMARK 470 LYS B 135 CG CD CE NZ
REMARK 470 ASP B 138 CG OD1 OD2
REMARK 470 GLN B 139 CG CD OE1 NE2
REMARK 470 ASN B 141 CG OD1 ND2
REMARK 470 GLN B 144 CG CD OE1 NE2
REMARK 470 GLU B 145 CG CD OE1 OE2
REMARK 470 LYS B 148 CG CD CE NZ
REMARK 470 ASP B 149 CG OD1 OD2
REMARK 470 LYS B 154 CG CD CE NZ
REMARK 470 GLN B 163 CG CD OE1 NE2
REMARK 470 VAL B 164 CG1 CG2
REMARK 470 LEU B 165 CG CD1 CD2
REMARK 470 GLU B 170 CG CD OE1 OE2
REMARK 470 LEU B 172 CG CD1 CD2
REMARK 470 VAL B 173 CG1 CG2
REMARK 470 LYS B 174 CG CD CE NZ
REMARK 470 GLU B 177 CG CD OE1 OE2
REMARK 470 VAL B 179 CG1 CG2
REMARK 470 ILE B 180 CG1 CG2 CD1
REMARK 470 ILE B 192 CG1 CG2 CD1
REMARK 470 ARG B 194 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 201 CG1 CG2
REMARK 470 LYS B 202 CG CD CE NZ
REMARK 470 CYS B 203 SG
REMARK 470 ASP B 204 CG OD1 OD2
REMARK 470 VAL B 206 CG1 CG2
REMARK 470 ARG B 216 CG CD NE CZ NH1 NH2
REMARK 470 THR B 235 OG1 CG2
REMARK 470 THR B 237 OG1 CG2
REMARK 470 SER B 238 OG
REMARK 470 LEU B 242 CG CD1 CD2
REMARK 470 ARG B 251 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 256 CG CD CE NZ
REMARK 470 TYR B 265 OH
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 MN MN A 401 O2G ANP A 450 1.50
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 PRO A 33 -133.53 -70.79
REMARK 500 ASN A 36 70.18 37.33
REMARK 500 ASP A 41 27.41 -62.76
REMARK 500 ILE A 46 -72.88 -51.26
REMARK 500 GLN A 84 42.79 -92.18
REMARK 500 ALA A 124 -5.41 -57.81
REMARK 500 ASP A 161 39.53 73.07
REMARK 500 ASP A 166 64.94 -157.45
REMARK 500 ASP A 184 96.34 68.22
REMARK 500 TPO A 197 117.95 -29.36
REMARK 500 PRO A 202 -78.30 -16.73
REMARK 500 GLU A 203 -5.54 -54.66
REMARK 500 LYS A 217 -6.94 -53.85
REMARK 500 LEU A 273 45.52 -92.34
REMARK 500 LYS A 319 -106.38 -78.73
REMARK 500 ASP A 328 -174.20 -58.36
REMARK 500 GLU A 331 90.16 -53.77
REMARK 500 GLU A 334 146.24 -30.30
REMARK 500 VAL A 337 -126.62 -64.45
REMARK 500 PHE A 347 12.27 -143.57
REMARK 500 THR A 348 -17.52 -48.59
REMARK 500 ILE B 104 -164.97 69.16
REMARK 500 ASN B 105 -155.37 166.49
REMARK 500 ARG B 106 3.57 80.23
REMARK 500 THR B 108 131.99 148.64
REMARK 500 ARG B 109 134.26 -28.61
REMARK 500 ASN B 119 111.82 -160.77
REMARK 500 PRO B 120 -108.52 -49.08
REMARK 500 ASP B 121 78.00 39.54
REMARK 500 GLU B 122 -90.73 -145.40
REMARK 500 GLU B 123 -73.41 -133.55
REMARK 500 GLU B 124 41.95 98.40
REMARK 500 ASP B 125 -121.43 -55.41
REMARK 500 ASP B 126 -122.45 65.38
REMARK 500 ALA B 127 -70.31 -173.20
REMARK 500 ASP B 137 -70.18 25.79
REMARK 500 GLN B 144 -8.48 -57.51
REMARK 500 LYS B 148 7.61 -58.85
REMARK 500 LEU B 152 -2.89 -58.26
REMARK 500 LYS B 174 -89.93 -79.07
REMARK 500 VAL B 201 21.50 -65.76
REMARK 500 LYS B 202 92.29 -21.96
REMARK 500 CYS B 203 -178.45 172.45
REMARK 500 ASP B 204 -22.80 89.50
REMARK 500 VAL B 206 -157.40 -94.39
REMARK 500 ARG B 208 -147.77 -80.07
REMARK 500 VAL B 210 -1.76 -152.60
REMARK 500 THR B 228 147.82 -171.85
REMARK 500 ALA B 232 149.23 -175.72
REMARK 500 SER B 238 -153.24 -62.16
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 171 OD1
REMARK 620 2 ANP A 450 O2A 81.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 184 OD1
REMARK 620 2 ANP A 450 O2B 68.5
REMARK 620 3 ANP A 450 O1G 91.8 84.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 450
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IDB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF (108-268)RIIB:C HOLOENZYME OF CAMP-DEPENDENT
REMARK 900 PROTEIN KINASE
REMARK 900 RELATED ID: 1CX4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A DELETION MUTANT OF THE TYPE II BETA
REMARK 900 REGULATORY SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE
REMARK 900 RELATED ID: 1RGS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A DELETION MUTANT OF THE TYPE I ALPHA
REMARK 900 REGULATORY SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE
REMARK 900 RELATED ID: 2QCS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PKA RIA:C HOLOENZYME
REMARK 900 RELATED ID: 2QVS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PKA RIIA:C HOLOENZYME
DBREF 3IDC A 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 3IDC B 102 265 UNP P12369 KAP3_RAT 102 265
SEQRES 1 A 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 A 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 A 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 A 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 A 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 A 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 A 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 A 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 A 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 A 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 A 350 HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA
SEQRES 12 A 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 A 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 A 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 A 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 A 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 A 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 A 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 A 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 A 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 A 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 A 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 A 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 A 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 A 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 A 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 A 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 B 164 PRO VAL ILE ASN ARG PHE THR ARG ARG ALA SER VAL CYS
SEQRES 2 B 164 ALA GLU ALA TYR ASN PRO ASP GLU GLU GLU ASP ASP ALA
SEQRES 3 B 164 GLU SER ARG ILE ILE HIS PRO LYS THR ASP ASP GLN ARG
SEQRES 4 B 164 ASN ARG LEU GLN GLU ALA CYS LYS ASP ILE LEU LEU PHE
SEQRES 5 B 164 LYS ASN LEU ASP PRO GLU GLN MET SER GLN VAL LEU ASP
SEQRES 6 B 164 ALA MET PHE GLU LYS LEU VAL LYS GLU GLY GLU HIS VAL
SEQRES 7 B 164 ILE ASP GLN GLY ASP ASP GLY ASP ASN PHE TYR VAL ILE
SEQRES 8 B 164 ASP ARG GLY THR PHE ASP ILE TYR VAL LYS CYS ASP GLY
SEQRES 9 B 164 VAL GLY ARG CYS VAL GLY ASN TYR ASP ASN ARG GLY SER
SEQRES 10 B 164 PHE GLY GLU LEU ALA LEU MET TYR ASN THR PRO ARG ALA
SEQRES 11 B 164 ALA THR ILE THR ALA THR SER PRO GLY ALA LEU TRP GLY
SEQRES 12 B 164 LEU ASP ARG VAL THR PHE ARG ARG ILE ILE VAL LYS ASN
SEQRES 13 B 164 ASN ALA LYS LYS ARG LYS MET TYR
MODRES 3IDC TPO A 197 THR PHOSPHOTHREONINE
MODRES 3IDC SEP A 338 SER PHOSPHOSERINE
HET TPO A 197 11
HET SEP A 338 10
HET MN A 401 1
HET MN A 402 1
HET ANP A 450 31
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM MN MANGANESE (II) ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 MN 2(MN 2+)
FORMUL 5 ANP C10 H17 N6 O12 P3
FORMUL 6 HOH *43(H2 O)
HELIX 1 1 LYS A 8 GLN A 12 5 5
HELIX 2 2 VAL A 15 THR A 32 1 18
HELIX 3 3 GLN A 39 ASP A 41 5 3
HELIX 4 4 LYS A 76 LYS A 83 1 8
HELIX 5 5 GLN A 84 GLN A 96 1 13
HELIX 6 6 GLU A 127 ILE A 135 1 9
HELIX 7 7 SER A 139 LEU A 160 1 22
HELIX 8 8 LYS A 168 GLU A 170 5 3
HELIX 9 9 THR A 201 LEU A 205 5 5
HELIX 10 10 ALA A 206 LEU A 211 1 6
HELIX 11 11 LYS A 217 GLY A 234 1 18
HELIX 12 12 GLN A 242 GLY A 253 1 12
HELIX 13 13 SER A 262 LEU A 273 1 12
HELIX 14 14 VAL A 288 ASN A 293 1 6
HELIX 15 15 HIS A 294 THR A 300 5 7
HELIX 16 16 ASP A 301 ARG A 308 1 8
HELIX 17 17 ASP B 137 CYS B 147 1 11
HELIX 18 18 ILE B 150 ASN B 155 1 6
HELIX 19 19 ASP B 157 MET B 168 1 12
HELIX 20 20 GLY B 220 LEU B 224 5 5
HELIX 21 21 ARG B 247 LYS B 261 1 15
SHEET 1 A 5 PHE A 43 THR A 51 0
SHEET 2 A 5 GLY A 55 HIS A 62 -1 O LEU A 59 N LYS A 47
SHEET 3 A 5 HIS A 68 ASP A 75 -1 O ILE A 73 N ARG A 56
SHEET 4 A 5 ASN A 115 GLU A 121 -1 O MET A 120 N ALA A 70
SHEET 5 A 5 LEU A 106 LYS A 111 -1 N GLU A 107 O VAL A 119
SHEET 1 B 2 LEU A 162 ILE A 163 0
SHEET 2 B 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 C 2 LEU A 172 ILE A 174 0
SHEET 2 C 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
SHEET 1 D 2 CYS A 199 GLY A 200 0
SHEET 2 D 2 VAL B 113 CYS B 114 -1 O VAL B 113 N GLY A 200
SHEET 1 E 4 PHE B 169 VAL B 173 0
SHEET 2 E 4 GLY B 240 ASP B 246 -1 O LEU B 242 N LYS B 171
SHEET 3 E 4 ASN B 188 ILE B 192 -1 N VAL B 191 O TRP B 243
SHEET 4 E 4 SER B 218 PHE B 219 -1 O PHE B 219 N TYR B 190
SHEET 1 F 2 THR B 196 ASP B 198 0
SHEET 2 F 2 ASN B 212 ASP B 214 -1 O TYR B 213 N PHE B 197
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.34
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK OD1 ASN A 171 MN MN A 401 1555 1555 2.36
LINK OD1 ASP A 184 MN MN A 402 1555 1555 2.42
LINK MN MN A 401 O2A ANP A 450 1555 1555 2.21
LINK MN MN A 402 O2B ANP A 450 1555 1555 2.14
LINK MN MN A 402 O1G ANP A 450 1555 1555 2.09
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
CISPEP 1 SER B 238 PRO B 239 0 0.21
SITE 1 AC1 4 LYS A 168 ASN A 171 ASP A 184 ANP A 450
SITE 1 AC2 2 ASP A 184 ANP A 450
SITE 1 AC3 23 GLY A 52 VAL A 57 ALA A 70 LYS A 72
SITE 2 AC3 23 VAL A 104 MET A 120 GLU A 121 TYR A 122
SITE 3 AC3 23 VAL A 123 GLU A 127 LYS A 168 GLU A 170
SITE 4 AC3 23 ASN A 171 LEU A 173 THR A 183 ASP A 184
SITE 5 AC3 23 PHE A 327 MN A 401 MN A 402 HOH A 501
SITE 6 AC3 23 ARG B 109 ALA B 111 SER B 112
CRYST1 179.272 67.434 47.325 90.00 99.51 90.00 C 1 2 1 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 0.005578 0.000000 0.000934 0.00000
SCALE2 0.000000 0.014829 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021425 0.00000
(ATOM LINES ARE NOT SHOWN.)
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