HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-OCT-12 4HPT
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN
TITLE 2 KINASE DISPLAYING COMPLETE PHOSPHORYL TRANSFER OF AMP-PNP ONTO A
TITLE 3 SUBSTRATE PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 9 CHAIN: I;
COMPND 10 FRAGMENT: SP20 DERIVED FROM PKI (UNP RESIDUES 6-25);
COMPND 11 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,
COMPND 12 MUSCLE/BRAIN ISOFORM;
COMPND 13 ENGINEERED: YES;
COMPND 14 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;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS PROTEIN KINASE, PHOSPHOTRANSFERASE, REGULATORY SUBUNITS, PKI,
KEYWDS 2 MAGNESIUM, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.BASTIDAS,J.M.STEICHEN,J.WU,S.S.TAYLOR
REVDAT 4 15-NOV-17 4HPT 1 REMARK
REVDAT 3 10-APR-13 4HPT 1 JRNL
REVDAT 2 27-MAR-13 4HPT 1 JRNL
REVDAT 1 20-MAR-13 4HPT 0
JRNL AUTH A.C.BASTIDAS,M.S.DEAL,J.M.STEICHEN,Y.GUO,J.WU,S.S.TAYLOR
JRNL TITL PHOSPHORYL TRANSFER BY PROTEIN KINASE A IS CAPTURED IN A
JRNL TITL 2 CRYSTAL LATTICE.
JRNL REF J.AM.CHEM.SOC. V. 135 4788 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 23458248
JRNL DOI 10.1021/JA312237Q
REMARK 2
REMARK 2 RESOLUTION. 2.15 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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.8
REMARK 3 NUMBER OF REFLECTIONS : 20161
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1076
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1098
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2908
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : 1.98000
REMARK 3 B33 (A**2) : -1.84000
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): 0.277
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.208
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.412
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
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): 3018 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4089 ; 1.155 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 358 ; 5.512 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;35.923 ;23.878
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 522 ;14.545 ;15.057
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;15.757 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 433 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2280 ; 0.005 ; 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): 1776 ; 0.497 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2864 ; 0.936 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1242 ; 1.344 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1223 ; 2.201 ; 4.500
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 : 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 14 E 350
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0983 -2.5511 -2.5763
REMARK 3 T TENSOR
REMARK 3 T11: 0.0041 T22: 0.0602
REMARK 3 T33: 0.0196 T12: -0.0093
REMARK 3 T13: -0.0023 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 0.2947 L22: 0.6288
REMARK 3 L33: 0.9711 L12: -0.2414
REMARK 3 L13: 0.0375 L23: 0.2677
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: 0.0076 S13: 0.0208
REMARK 3 S21: -0.0103 S22: -0.0145 S23: 0.0125
REMARK 3 S31: -0.0151 S32: 0.1377 S33: 0.0135
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 23
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7290 1.1935 9.2946
REMARK 3 T TENSOR
REMARK 3 T11: 0.0611 T22: 0.0606
REMARK 3 T33: 0.0209 T12: -0.0223
REMARK 3 T13: 0.0065 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 1.7121 L22: 1.6413
REMARK 3 L33: 2.7390 L12: -0.9867
REMARK 3 L13: -0.5716 L23: 1.8433
REMARK 3 S TENSOR
REMARK 3 S11: -0.0820 S12: -0.0896 S13: -0.0985
REMARK 3 S21: -0.0646 S22: 0.0218 S23: 0.0920
REMARK 3 S31: -0.0125 S32: -0.1422 S33: 0.0602
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 401 E 401
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5930 -10.1383 2.5248
REMARK 3 T TENSOR
REMARK 3 T11: 0.0242 T22: 0.1567
REMARK 3 T33: 0.0884 T12: -0.0277
REMARK 3 T13: -0.0040 T23: 0.0525
REMARK 3 L TENSOR
REMARK 3 L11: 3.8988 L22: 27.6818
REMARK 3 L33: 0.1838 L12: -10.3884
REMARK 3 L13: -0.8459 L23: 2.2533
REMARK 3 S TENSOR
REMARK 3 S11: -0.1716 S12: -0.0718 S13: 0.2778
REMARK 3 S21: 0.4920 S22: 0.2211 S23: -0.7315
REMARK 3 S31: 0.0411 S32: 0.0094 S33: -0.0495
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 402 E 402
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4696 -7.2082 0.5280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0550 T22: 0.0781
REMARK 3 T33: 0.0585 T12: -0.0254
REMARK 3 T13: 0.0036 T23: 0.0605
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 : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 501 E 659
REMARK 3 RESIDUE RANGE : I 101 I 118
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5477 -2.2906 -1.3541
REMARK 3 T TENSOR
REMARK 3 T11: 0.0410 T22: 0.0465
REMARK 3 T33: 0.0573 T12: 0.0097
REMARK 3 T13: 0.0002 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 0.6696 L22: 0.3291
REMARK 3 L33: 1.0758 L12: -0.3965
REMARK 3 L13: -0.1794 L23: 0.3962
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: 0.0114 S13: -0.0020
REMARK 3 S21: 0.0056 S22: 0.0035 S23: 0.0176
REMARK 3 S31: 0.0174 S32: 0.0808 S33: 0.0178
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 403 E 403
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0937 -8.5463 -3.3910
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.2109
REMARK 3 T33: 0.2470 T12: -0.0718
REMARK 3 T13: 0.0368 T23: 0.1783
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 4HPT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075768.
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
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 : 8.2.2
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21475
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 44.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.7
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.44400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER: 50 MM BICINE, 150 MM
REMARK 280 AMMONIUM ACETATE, 10 MM DTT, ~7-10 MG/ML PROTEIN WELL SOLUTION:
REMARK 280 1 ML OF 2% MPD, 80 UL METHANOL ADDED TO THE WELL IMMEDIATELY
REMARK 280 BEFORE SEALING 8 UL DROPS OF 1:1 PROTEIN:WELL WERE USED., VAPOR
REMARK 280 DIFFUSION, 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 35.77250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.04500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.53000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.04500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.77250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.53000
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: 3180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 465 SER E 10
REMARK 465 GLU E 11
REMARK 465 GLN E 12
REMARK 465 GLU E 13
REMARK 465 ASP I 24
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 16 CE NZ
REMARK 470 LYS E 105 CD CE NZ
REMARK 470 ARG E 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 285 CG CD CE NZ
REMARK 470 LYS E 317 CE NZ
REMARK 470 LYS E 319 CG CD CE NZ
REMARK 470 GLU E 333 CG CD OE1 OE2
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 O HOH E 548 O HOH E 655 2.01
REMARK 500 O LYS E 213 O HOH E 643 2.07
REMARK 500 O HOH E 609 O HOH E 630 2.14
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 -154.85 -130.43
REMARK 500 ASP E 166 38.25 -142.90
REMARK 500 ASP E 184 81.09 67.73
REMARK 500 LEU E 273 48.56 -86.48
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 MG E 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP E 401 N3B
REMARK 620 2 ANP E 401 O2A 80.0
REMARK 620 3 HOH I 104 O 88.0 162.1
REMARK 620 4 ASN E 171 OD1 172.7 92.8 99.1
REMARK 620 5 HOH E 520 O 89.5 90.4 102.8 90.0
REMARK 620 6 ASP E 184 OD2 86.9 87.1 78.9 93.2 176.0
REMARK 620 N 1 2 3 4 5
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 SEP I 21 O1P
REMARK 620 2 ANP E 401 O1B 87.7
REMARK 620 3 HOH E 519 O 83.5 152.1
REMARK 620 4 HOH I 101 O 93.2 115.2 91.8
REMARK 620 5 ASP E 184 OD1 123.4 87.7 75.4 138.4
REMARK 620 6 ASP E 184 OD2 75.3 74.9 77.2 164.8 49.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 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 CHAIN I OF CAMP-DEPENDENT
REMARK 800 PROTEIN KINASE INHIBITOR ALPHA
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH IP20
REMARK 900 RELATED ID: 1L3R RELATED DB: PDB
REMARK 900 TRANSITION STATE MIMIC OF SAME PROTEIN IN COMPLEX WITH THE SAME
REMARK 900 SUBSTRATE PEPTIDE
REMARK 900 RELATED ID: 4DFX RELATED DB: PDB
REMARK 900 MYRISTYLATED CATALYTIC SUBUNIT WITH A K7C MUTATION IN COMPLEX WITH
REMARK 900 AMP-PNP AND THE SAME SUBSTRATE PEPTIDE WITHOUT TRANSFER
REMARK 900 RELATED ID: 4DG0 RELATED DB: PDB
REMARK 900 MYRISTYLATED CATALYTIC SUBUNIT IN COMPLEX WITH AMP-PNP AND THE SAME
REMARK 900 SUBSTRATE PEPTIDE WITHOUT TRANSFER
REMARK 900 RELATED ID: 1JLU RELATED DB: PDB
REMARK 900 SAME PROTEIN IN A COMPLEX WITH THE SAME SUBSTRATE PEPTIDE THAT WAS
REMARK 900 PHOSPHORYLATED PRIOR TO CRYSTALLIZATION
REMARK 900 RELATED ID: 1JBP RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH THE SAME SUBSTRATE PEPTIDE AND ADP
REMARK 900 RELATED ID: 4DH1 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SAME PROTEIN WITH LOW MAGNESIUM SHOWING OCCUPANCY
REMARK 900 OF ONLY ONE MAGNESIUM SITE, MG2.
REMARK 900 RELATED ID: 4HPU RELATED DB: PDB
DBREF 4HPT E 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 4HPT I 5 24 UNP P63248 IPKA_MOUSE 6 25
SEQADV 4HPT ALA I 20 UNP P63248 ASN 21 ENGINEERED MUTATION
SEQADV 4HPT SEP 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 SER 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 SEP ILE HIS ASP
MODRES 4HPT TPO E 197 THR PHOSPHOTHREONINE
MODRES 4HPT SEP E 338 SER PHOSPHOSERINE
MODRES 4HPT SEP I 21 SER PHOSPHOSERINE
HET TPO E 197 11
HET SEP E 338 10
HET SEP I 21 10
HET ANP E 401 27
HET MG E 402 1
HET MG E 403 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 ANP C10 H17 N6 O12 P3
FORMUL 4 MG 2(MG 2+)
FORMUL 6 HOH *177(H2 O)
HELIX 1 1 SER E 14 THR E 32 1 19
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 SER 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 SER E 252 1 11
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 SER I 13 1 8
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 GLU E 107 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
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 C ALA I 20 N SEP I 21 1555 1555 1.33
LINK C SEP I 21 N ILE I 22 1555 1555 1.32
LINK N3B ANP E 401 MG MG E 402 1555 1555 2.02
LINK O2A ANP E 401 MG MG E 402 1555 1555 2.05
LINK O1P SEP I 21 MG MG E 403 1555 1555 2.10
LINK O1B ANP E 401 MG MG E 403 1555 1555 2.15
LINK MG MG E 402 O HOH I 104 1555 1555 2.16
LINK OD1 ASN E 171 MG MG E 402 1555 1555 2.17
LINK MG MG E 402 O HOH E 520 1555 1555 2.27
LINK OD2 ASP E 184 MG MG E 402 1555 1555 2.28
LINK MG MG E 403 O HOH E 519 1555 1555 2.30
LINK MG MG E 403 O HOH I 101 1555 1555 2.42
LINK OD1 ASP E 184 MG MG E 403 1555 1555 2.51
LINK OD2 ASP E 184 MG MG E 403 1555 1555 2.74
SITE 1 AC1 26 GLY E 50 GLY E 52 VAL E 57 ALA E 70
SITE 2 AC1 26 LYS E 72 VAL E 104 MET E 120 GLU E 121
SITE 3 AC1 26 TYR E 122 VAL E 123 GLU E 127 GLU E 170
SITE 4 AC1 26 ASN E 171 LEU E 173 THR E 183 ASP E 184
SITE 5 AC1 26 PHE E 327 MG E 402 MG E 403 HOH E 520
SITE 6 AC1 26 HOH E 556 HOH E 594 HOH E 646 ARG I 18
SITE 7 AC1 26 SEP I 21 HOH I 104
SITE 1 AC2 5 ASN E 171 ASP E 184 ANP E 401 HOH E 520
SITE 2 AC2 5 HOH I 104
SITE 1 AC3 5 ASP E 184 ANP E 401 HOH E 519 SEP I 21
SITE 2 AC3 5 HOH I 101
SITE 1 AC4 53 SER E 53 GLN E 84 GLU E 86 ARG E 93
SITE 2 AC4 53 GLU E 127 PHE E 129 ARG E 133 ASP E 166
SITE 3 AC4 53 LYS E 168 PRO E 169 GLU E 170 ASP E 184
SITE 4 AC4 53 PHE E 187 ARG E 190 LYS E 192 LEU E 198
SITE 5 AC4 53 CYS E 199 GLY E 200 PRO E 202 GLU E 203
SITE 6 AC4 53 GLU E 230 TYR E 235 PRO E 236 PHE E 239
SITE 7 AC4 53 ALA E 240 ASP E 241 ILE E 246 TYR E 330
SITE 8 AC4 53 GLU E 349 ANP E 401 MG E 403 HOH E 519
SITE 9 AC4 53 HOH E 530 HOH E 544 HOH E 558 HOH E 576
SITE 10 AC4 53 HOH E 596 HOH E 603 HOH E 622 HOH I 101
SITE 11 AC4 53 HOH I 102 HOH I 103 HOH I 104 HOH I 105
SITE 12 AC4 53 HOH I 106 HOH I 109 HOH I 110 HOH I 111
SITE 13 AC4 53 HOH I 112 HOH I 113 HOH I 114 HOH I 116
SITE 14 AC4 53 HOH I 117
CRYST1 71.545 79.060 80.090 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 0.013977 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012649 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012486 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
