HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-JAN-12 4DG3
TITLE CRYSTAL STRUCTURE OF R336A MUTANT OF CAMP-DEPENDENT PROTEIN KINASE
TITLE 2 WITH UNPHOSPHORYLATED TURN MOTIF.
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 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 10 CHAIN: A;
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
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: SYNTHESIZED
KEYWDS PROTEIN KINASE, PHOSPHOTRANSFERASE, SERINE/THREONINE PROTEIN KINASE,
KEYWDS 2 REGULATORY SUBUNIT, PKI, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE
KEYWDS 3 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.STEICHEN,J.YANG,S.S.TAYLOR
REVDAT 2 06-NOV-24 4DG3 1 REMARK SEQADV LINK
REVDAT 1 13-FEB-13 4DG3 0
JRNL AUTH J.M.STEICHEN,J.YANG,S.S.TAYLOR
JRNL TITL TURN MOTIF PHOSPHORYLATION REGULATES PROCESSING OF
JRNL TITL 2 CAMP-DEPENDENT PROTEIN KINASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 35158
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1862
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2565
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 113
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2889
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 249
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.56000
REMARK 3 B22 (A**2) : 2.35000
REMARK 3 B33 (A**2) : -1.79000
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): 0.132
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.125
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.976
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2994 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4057 ; 1.135 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 354 ; 5.199 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;34.310 ;23.958
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 508 ;12.693 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.587 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 431 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2264 ; 0.004 ; 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): 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 14 E 126
REMARK 3 RESIDUE RANGE : E 328 E 350
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0753 15.5905 -5.7273
REMARK 3 T TENSOR
REMARK 3 T11: 0.0433 T22: 0.1055
REMARK 3 T33: 0.0553 T12: 0.0584
REMARK 3 T13: -0.0207 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.4659 L22: 1.9968
REMARK 3 L33: 3.8185 L12: -0.5546
REMARK 3 L13: -0.9407 L23: -0.0862
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: 0.0666 S13: 0.1863
REMARK 3 S21: -0.0242 S22: 0.0181 S23: 0.0539
REMARK 3 S31: -0.3102 S32: -0.3279 S33: -0.0303
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 : E 127 E 327
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2759 -6.8346 -0.7348
REMARK 3 T TENSOR
REMARK 3 T11: 0.0920 T22: 0.0447
REMARK 3 T33: 0.0512 T12: -0.0477
REMARK 3 T13: 0.0214 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 1.7449 L22: 2.2166
REMARK 3 L33: 3.3028 L12: -0.3248
REMARK 3 L13: 0.1908 L23: -0.7746
REMARK 3 S TENSOR
REMARK 3 S11: -0.0308 S12: -0.0312 S13: -0.2568
REMARK 3 S21: -0.1065 S22: -0.0134 S23: 0.1440
REMARK 3 S31: 0.5326 S32: -0.2365 S33: 0.0442
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4DG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070284.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-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 : 37095
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 38.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
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 (%): 50.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-14% MPD, 100 MM TRIS, 10 MM DTT. 11
REMARK 280 -13% METHANOL ADDED TO WELL BEFORE SEALING, PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 36.14500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.15500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.34500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.15500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.14500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.34500
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: 3230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, A
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 MET E -20
REMARK 465 GLY E -19
REMARK 465 SER E -18
REMARK 465 SER E -17
REMARK 465 HIS E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 SER E -10
REMARK 465 SER E -9
REMARK 465 GLY E -8
REMARK 465 LEU E -7
REMARK 465 VAL E -6
REMARK 465 PRO E -5
REMARK 465 ARG E -4
REMARK 465 GLY E -3
REMARK 465 SER E -2
REMARK 465 HIS E -1
REMARK 465 MET E 0
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 A 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 CD CE NZ
REMARK 470 GLU E 17 CG CD OE1 OE2
REMARK 470 LYS E 21 CE NZ
REMARK 470 LYS E 28 CG CD CE NZ
REMARK 470 ARG E 256 NE CZ NH1 NH2
REMARK 470 LYS E 285 CG CD CE NZ
REMARK 470 LYS E 317 CE NZ
REMARK 470 PHE E 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS E 319 CG CD CE NZ
REMARK 470 LYS E 345 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 NH2 ARG E 308 O HOH E 642 2.00
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 A 15 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -4.2 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 PHE E 54 18.67 -160.78
REMARK 500 ASP E 112 -164.59 -126.94
REMARK 500 ASP E 166 42.87 -149.23
REMARK 500 ASP E 184 77.98 61.62
REMARK 500 ASN E 216 -159.76 -136.02
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 ASN E 171 OD1
REMARK 620 2 ASP E 184 OD2 94.7
REMARK 620 3 ANP E 401 O2A 99.0 92.3
REMARK 620 4 ANP E 401 O2G 110.2 89.1 150.6
REMARK 620 5 HOH E 715 O 90.9 174.4 86.7 89.1
REMARK 620 N 1 2 3 4
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 ASP E 184 OD2
REMARK 620 2 ASP E 184 OD1 59.5
REMARK 620 3 ANP E 401 O3G 96.3 155.6
REMARK 620 4 ANP E 401 O1B 91.0 88.4 89.3
REMARK 620 5 HOH E 694 O 87.1 90.2 91.4 178.0
REMARK 620 6 HOH E 701 O 156.3 97.0 107.4 91.3 90.3
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 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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN
REMARK 900 KINASE COMPLEXED WITH ATP AND IP20.
DBREF 4DG3 E 0 350 UNP P05132 KAPCA_MOUSE 1 351
DBREF 4DG3 A 5 24 UNP P63248 IPKA_MOUSE 6 25
SEQADV 4DG3 MET E -20 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 GLY E -19 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 SER E -18 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 SER E -17 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 HIS E -16 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 HIS E -15 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 HIS E -14 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 HIS E -13 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 HIS E -12 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 HIS E -11 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 SER E -10 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 SER E -9 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 GLY E -8 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 LEU E -7 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 VAL E -6 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 PRO E -5 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 ARG E -4 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 GLY E -3 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 SER E -2 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 HIS E -1 UNP P05132 EXPRESSION TAG
SEQADV 4DG3 ALA E 336 UNP P05132 ARG 337 ENGINEERED MUTATION
SEQRES 1 E 371 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 371 LEU VAL PRO ARG GLY SER HIS MET GLY ASN ALA ALA ALA
SEQRES 3 E 371 ALA LYS LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE
SEQRES 4 E 371 LEU ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU
SEQRES 5 E 371 THR PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP
SEQRES 6 E 371 ARG ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL
SEQRES 7 E 371 MET LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA
SEQRES 8 E 371 MET LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS
SEQRES 9 E 371 GLN ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN
SEQRES 10 E 371 ALA VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER
SEQRES 11 E 371 PHE LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR
SEQRES 12 E 371 VAL ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE
SEQRES 13 E 371 GLY ARG PHE SEP GLU PRO HIS ALA ARG PHE TYR ALA ALA
SEQRES 14 E 371 GLN ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP
SEQRES 15 E 371 LEU ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE
SEQRES 16 E 371 ASP GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE
SEQRES 17 E 371 ALA LYS ARG VAL LYS GLY ARG THR TRP TPO LEU CYS GLY
SEQRES 18 E 371 THR PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS
SEQRES 19 E 371 GLY TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL
SEQRES 20 E 371 LEU ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE
SEQRES 21 E 371 ALA ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER
SEQRES 22 E 371 GLY LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU
SEQRES 23 E 371 LYS ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR
SEQRES 24 E 371 LYS ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE
SEQRES 25 E 371 LYS ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA
SEQRES 26 E 371 ILE TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS
SEQRES 27 E 371 PHE LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR
SEQRES 28 E 371 GLU GLU GLU GLU ILE ALA VAL SER ILE ASN GLU LYS CYS
SEQRES 29 E 371 GLY LYS GLU PHE THR GLU PHE
SEQRES 1 A 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 A 20 ARG ARG ASN ALA ILE HIS ASP
MODRES 4DG3 SEP E 139 SER PHOSPHOSERINE
MODRES 4DG3 TPO E 197 THR PHOSPHOTHREONINE
HET SEP E 139 10
HET TPO E 197 11
HET ANP E 401 31
HET MG E 402 1
HET MG E 403 1
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 ANP C10 H17 N6 O12 P3
FORMUL 4 MG 2(MG 2+)
FORMUL 6 HOH *249(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 SEP E 139 LEU E 160 1 22
HELIX 7 7 LYS E 168 GLU E 170 5 3
HELIX 8 8 THR E 201 LEU E 205 5 5
HELIX 9 9 ALA E 206 LEU E 211 1 6
HELIX 10 10 LYS E 217 GLY E 234 1 18
HELIX 11 11 GLN E 242 GLY E 253 1 12
HELIX 12 12 SER E 262 LEU E 273 1 12
HELIX 13 13 VAL E 288 ASN E 293 1 6
HELIX 14 14 HIS E 294 ALA E 298 5 5
HELIX 15 15 ASP E 301 GLN E 307 1 7
HELIX 16 16 THR A 6 ALA A 12 1 7
SHEET 1 A 5 PHE E 43 THR E 51 0
SHEET 2 A 5 ARG E 56 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
LINK C PHE E 138 N SEP E 139 1555 1555 1.34
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 OD1 ASN E 171 MG MG E 402 1555 1555 2.02
LINK OD2 ASP E 184 MG MG E 402 1555 1555 2.13
LINK OD2 ASP E 184 MG MG E 403 1555 1555 2.17
LINK OD1 ASP E 184 MG MG E 403 1555 1555 2.24
LINK O2A ANP E 401 MG MG E 402 1555 1555 1.99
LINK O2G ANP E 401 MG MG E 402 1555 1555 2.10
LINK O3G ANP E 401 MG MG E 403 1555 1555 1.98
LINK O1B ANP E 401 MG MG E 403 1555 1555 2.05
LINK MG MG E 402 O HOH E 715 1555 1555 2.10
LINK MG MG E 403 O HOH E 694 1555 1555 2.12
LINK MG MG E 403 O HOH E 701 1555 1555 1.97
SITE 1 AC1 32 ARG A 18 ASN A 20 ALA A 21 HOH A 106
SITE 2 AC1 32 HOH A 108 GLY E 55 VAL E 57 ALA E 70
SITE 3 AC1 32 LYS E 72 VAL E 104 MET E 120 GLU E 121
SITE 4 AC1 32 TYR E 122 VAL E 123 GLU E 127 ASP E 166
SITE 5 AC1 32 LYS E 168 GLU E 170 ASN E 171 LEU E 173
SITE 6 AC1 32 THR E 183 ASP E 184 PHE E 327 MG E 402
SITE 7 AC1 32 MG E 403 HOH E 508 HOH E 509 HOH E 528
SITE 8 AC1 32 HOH E 605 HOH E 694 HOH E 701 HOH E 715
SITE 1 AC2 4 ASN E 171 ASP E 184 ANP E 401 HOH E 715
SITE 1 AC3 4 ASP E 184 ANP E 401 HOH E 694 HOH E 701
CRYST1 72.290 76.690 80.310 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 0.013833 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013040 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012452 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
