HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-JAN-12 4DFX
TITLE CRYSTAL STRUCTURE OF MYRISTOYLATED K7C 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 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: UNP RESIDUES 6-25;
COMPND 13 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,
COMPND 14 MUSCLE/BRAIN ISOFORM;
COMPND 15 ENGINEERED: YES;
COMPND 16 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 ONTO SER/THR, MG,
KEYWDS 2 PKI, PKA REGULATORY SUBUNITS, PHOSPHORYLATED ON S139, T197, S338,
KEYWDS 3 MYRISTOYLATED ON G1, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.BASTIDAS,J.M.STEICHEN,S.S.TAYLOR
REVDAT 2 02-JAN-13 4DFX 1 JRNL
REVDAT 1 06-JUN-12 4DFX 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. 1.35 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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 90882
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4783
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6327
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 327
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3015
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 453
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : -0.05000
REMARK 3 B33 (A**2) : -0.08000
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): 0.054
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.050
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.027
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.415
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3237 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4394 ; 1.335 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 396 ; 5.518 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 155 ;35.524 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 567 ;12.252 ;15.053
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;19.245 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 463 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2435 ; 0.007 ; 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): 1888 ; 0.902 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3056 ; 1.451 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1349 ; 2.091 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1325 ; 3.122 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3236 ; 1.124 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 455 ; 3.013 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3148 ; 2.744 ; 3.000
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 1 E 350
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4570 5.5500 -24.0260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0204 T22: 0.0238
REMARK 3 T33: 0.0462 T12: -0.0010
REMARK 3 T13: 0.0100 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.5944 L22: 1.0858
REMARK 3 L33: 1.5212 L12: 0.1273
REMARK 3 L13: -0.0601 L23: 0.4537
REMARK 3 S TENSOR
REMARK 3 S11: 0.0206 S12: -0.0351 S13: 0.0033
REMARK 3 S21: 0.0298 S22: -0.0258 S23: 0.0359
REMARK 3 S31: -0.0066 S32: 0.0191 S33: 0.0051
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): 3.5410 -6.1120 -32.0100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0254 T22: 0.0506
REMARK 3 T33: 0.0806 T12: 0.0261
REMARK 3 T13: 0.0074 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.1823 L22: 4.5115
REMARK 3 L33: 4.7012 L12: -0.7517
REMARK 3 L13: -0.2582 L23: 3.5141
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: -0.0077 S13: 0.0690
REMARK 3 S21: -0.0325 S22: 0.1116 S23: -0.2999
REMARK 3 S31: 0.0369 S32: 0.1946 S33: -0.1196
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): -3.6210 0.2750 -17.3320
REMARK 3 T TENSOR
REMARK 3 T11: 0.1040 T22: 0.0636
REMARK 3 T33: 0.0315 T12: 0.0343
REMARK 3 T13: -0.0071 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 2.5425 L22: 3.0138
REMARK 3 L33: 1.6064 L12: 2.1418
REMARK 3 L13: -0.4699 L23: -0.9898
REMARK 3 S TENSOR
REMARK 3 S11: -0.0454 S12: -0.0682 S13: -0.1437
REMARK 3 S21: 0.1705 S22: 0.0766 S23: -0.1413
REMARK 3 S31: 0.1299 S32: 0.1261 S33: -0.0313
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 403 E 403
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7180 1.8730 -21.0280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0348 T22: 0.0020
REMARK 3 T33: 0.0249 T12: 0.0031
REMARK 3 T13: -0.0016 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0003 L22: 0.0001
REMARK 3 L33: 0.0003 L12: -0.0001
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0006 S13: -0.0025
REMARK 3 S21: 0.0006 S22: -0.0001 S23: 0.0008
REMARK 3 S31: -0.0034 S32: -0.0003 S33: 0.0002
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 404 E 404
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0400 5.2880 -20.3450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0337 T22: 0.0273
REMARK 3 T33: 0.0384 T12: -0.0073
REMARK 3 T13: 0.0135 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.0014 L22: 0.0017
REMARK 3 L33: 0.0003 L12: 0.0012
REMARK 3 L13: 0.0004 L23: 0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0016 S12: 0.0007 S13: -0.0009
REMARK 3 S21: 0.0020 S22: -0.0024 S23: -0.0025
REMARK 3 S31: 0.0001 S32: -0.0015 S33: 0.0008
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 501 E 865
REMARK 3 RESIDUE RANGE : I 101 I 138
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5700 5.4040 -23.0930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1105 T22: 0.1227
REMARK 3 T33: 0.1507 T12: 0.0015
REMARK 3 T13: 0.0082 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.6370 L22: 1.0394
REMARK 3 L33: 1.6062 L12: 0.0012
REMARK 3 L13: -0.0932 L23: 0.4798
REMARK 3 S TENSOR
REMARK 3 S11: 0.0206 S12: -0.0347 S13: 0.0092
REMARK 3 S21: 0.0263 S22: -0.0213 S23: 0.0334
REMARK 3 S31: -0.0090 S32: 0.0211 S33: 0.0006
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 4DFX 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 RCSB070278.
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 : 95939
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 25.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
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 (%): 53.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MOTHER LIQUOR: 12% MPD, 100 MM BIS-
REMARK 280 TRIS, PROTEIN SOLUTION: 50 MM BICINE, 150 MM AMMONIUM ACETATE, 10
REMARK 280 MM DTT, 8-10 MG/ML 9% MEOH ADDED TO THE WELL IMMEDIATELY BEFORE
REMARK 280 SEALING. 8 UL DROP SIZE WITH 1:1 PROTEIN:MOTHER LIQUOR, 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 24.05000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.61500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.61500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.05000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.85000
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: 3780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16590 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 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 CD CE NZ
REMARK 470 GLU E 334 CG CD OE1 OE2
REMARK 470 LYS E 345 CG CD CE NZ
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 669 O HOH I 136 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG E 144 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG E 144 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP E 166 47.04 -148.20
REMARK 500 ASP E 184 78.01 66.13
REMARK 500 LEU E 273 47.25 -88.34
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 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP E 402 O2A
REMARK 620 2 ANP E 402 O2G 143.8
REMARK 620 3 ASN E 171 OD1 99.6 116.6
REMARK 620 4 HOH E 520 O 90.5 88.4 89.9
REMARK 620 5 ASP E 184 OD2 90.0 88.6 94.2 175.7
REMARK 620 6 ANP E 402 N3B 82.0 61.8 178.4 90.1 85.8
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 O3G
REMARK 620 2 HOH E 526 O 107.4
REMARK 620 3 ANP E 402 O1B 88.5 91.5
REMARK 620 4 HOH E 522 O 92.8 89.3 178.2
REMARK 620 5 ASP E 184 OD2 93.9 158.7 88.7 90.0
REMARK 620 6 ASP E 184 OD1 153.0 99.4 87.7 90.5 59.3
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 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 RESIDUE GOL E 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
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 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: 4DFZ RELATED DB: PDB
REMARK 900 RELATED ID: 4DG0 RELATED DB: PDB
REMARK 900 RELATED ID: 4DG2 RELATED DB: PDB
DBREF 4DFX E 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 4DFX I 5 24 UNP P63248 IPKA_MOUSE 6 25
SEQADV 4DFX CYS E 7 UNP P05132 LYS 8 ENGINEERED MUTATION
SEQADV 4DFX ALA I 20 UNP P63248 ASN 21 ENGINEERED MUTATION
SEQADV 4DFX SER I 21 UNP P63248 ALA 22 ENGINEERED MUTATION
SEQRES 1 E 350 GLY ASN ALA ALA ALA ALA CYS 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 4DFX SEP E 139 SER PHOSPHOSERINE
MODRES 4DFX TPO E 197 THR PHOSPHOTHREONINE
MODRES 4DFX 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
HET GOL E 405 6
HET GOL E 406 6
HET GOL E 407 6
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM MYR MYRISTIC ACID
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
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 GOL 3(C3 H8 O3)
FORMUL 10 HOH *453(H2 O)
HELIX 1 1 GLY E 1 CYS 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 GLY E 253 1 12
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 GLY E 344 THR E 348 5 5
HELIX 18 18 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 120 N ALA E 70
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 O2A ANP E 402 MG MG E 403 1555 1555 1.97
LINK O3G ANP E 402 MG MG E 404 1555 1555 1.99
LINK O2G ANP E 402 MG MG E 403 1555 1555 1.99
LINK MG MG E 404 O HOH E 526 1555 1555 2.00
LINK O1B ANP E 402 MG MG E 404 1555 1555 2.03
LINK OD1 ASN E 171 MG MG E 403 1555 1555 2.05
LINK MG MG E 403 O HOH E 520 1555 1555 2.06
LINK MG MG E 404 O HOH E 522 1555 1555 2.08
LINK OD2 ASP E 184 MG MG E 403 1555 1555 2.13
LINK OD2 ASP E 184 MG MG E 404 1555 1555 2.21
LINK OD1 ASP E 184 MG MG E 404 1555 1555 2.23
LINK N3B ANP E 402 MG MG E 403 1555 1555 2.76
LINK N GLY E 1 C1 MYR E 401 1555 1555 1.48
SITE 1 AC1 9 GLY E 1 ASN E 2 ALA E 3 ALA E 4
SITE 2 AC1 9 SER E 14 PHE E 18 LEU E 152 ILE E 303
SITE 3 AC1 9 ASP I 24
SITE 1 AC2 32 GLY E 52 VAL E 57 ALA E 70 LYS E 72
SITE 2 AC2 32 VAL E 104 MET E 120 GLU E 121 TYR E 122
SITE 3 AC2 32 VAL E 123 GLU E 127 ASP E 166 LYS E 168
SITE 4 AC2 32 GLU E 170 ASN E 171 LEU E 173 THR E 183
SITE 5 AC2 32 ASP E 184 PHE E 327 MG E 403 MG E 404
SITE 6 AC2 32 HOH E 520 HOH E 521 HOH E 522 HOH E 523
SITE 7 AC2 32 HOH E 526 HOH E 594 HOH E 717 HOH E 718
SITE 8 AC2 32 HOH E 753 ARG I 18 ALA I 20 SER I 21
SITE 1 AC3 4 ASN E 171 ASP E 184 ANP E 402 HOH E 520
SITE 1 AC4 4 ASP E 184 ANP E 402 HOH E 522 HOH E 526
SITE 1 AC5 4 ASN E 36 ALA E 38 GLN E 39 GLN E 42
SITE 1 AC6 6 ARG E 93 HOH E 703 THR I 5 THR I 6
SITE 2 AC6 6 ASP I 9 HOH I 121
SITE 1 AC7 7 PRO E 237 PHE E 238 PHE E 239 LYS E 249
SITE 2 AC7 7 HOH E 533 HOH E 650 HOH E 891
SITE 1 AC8 72 GLY E 1 ASN E 2 ALA E 3 LEU E 82
SITE 2 AC8 72 GLN E 84 GLU E 86 LEU E 89 ARG E 93
SITE 3 AC8 72 GLU E 127 PHE E 129 ARG E 133 ASP E 166
SITE 4 AC8 72 LYS E 168 PRO E 169 GLU E 170 PHE E 187
SITE 5 AC8 72 LYS E 189 ARG E 190 VAL E 191 LYS E 192
SITE 6 AC8 72 LEU E 198 CYS E 199 GLY E 200 THR E 201
SITE 7 AC8 72 PRO E 202 GLU E 203 GLU E 230 TYR E 235
SITE 8 AC8 72 PRO E 236 PHE E 239 ALA E 240 ASP E 241
SITE 9 AC8 72 ILE E 246 TYR E 330 GLU E 349 MYR E 401
SITE 10 AC8 72 ANP E 402 GOL E 406 HOH E 507 HOH E 543
SITE 11 AC8 72 HOH E 594 HOH E 683 HOH E 701 HOH E 820
SITE 12 AC8 72 HOH E 885 HOH I 101 HOH I 102 HOH I 103
SITE 13 AC8 72 HOH I 104 HOH I 106 HOH I 107 HOH I 109
SITE 14 AC8 72 HOH I 110 HOH I 111 HOH I 113 HOH I 114
SITE 15 AC8 72 HOH I 115 HOH I 117 HOH I 118 HOH I 119
SITE 16 AC8 72 HOH I 120 HOH I 121 HOH I 122 HOH I 125
SITE 17 AC8 72 HOH I 126 HOH I 127 HOH I 128 HOH I 129
SITE 18 AC8 72 HOH I 131 HOH I 133 HOH I 134 HOH I 139
CRYST1 48.100 79.700 117.230 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 0.020790 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012547 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008530 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
