HEADER TRANSFERASE 06-DEC-10 3PVB
TITLE CRYSTAL STRUCTURE OF (73-244)RIA: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: UNP RESIDUES 7-351;
COMPND 5 SYNONYM: PKA C-ALPHA;
COMPND 6 EC: 2.7.11.11;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY
COMPND 10 SUBUNIT;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UNP RESIDUES 85-244;
COMPND 13 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 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 10 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 11 ORGANISM_TAXID: 9913;
SOURCE 12 GENE: PRKAR1A;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PRSET
KEYWDS KINASE, RIA HOLOENZYME, TETRAMERIC PROTEIN KINASE A, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.BOETTCHER,J.WU,C.KIM,J.YANG,J.BRUYSTENS,N.CHEUNG,J.K.PENNYPACKER,
AUTHOR 2 D.A.BLUMENTHAL,A.P.KORNEV,S.S.TAYLOR
REVDAT 2 19-JUN-13 3PVB 1 JRNL VERSN
REVDAT 1 02-FEB-11 3PVB 0
JRNL AUTH A.J.BOETTCHER,J.WU,C.KIM,J.YANG,J.BRUYSTENS,N.CHEUNG,
JRNL AUTH 2 J.K.PENNYPACKER,D.A.BLUMENTHAL,A.P.KORNEV,S.S.TAYLOR
JRNL TITL CRYSTAL STRUCTURE OF (73-244)RIA:C HOLOENZYME OF
JRNL TITL 2 CAMP-DEPENDENT PROTEIN KINASE
JRNL REF STRUCTURE V. 19 265 2011
JRNL REFN ISSN 0969-2126
JRNL PMID 21300294
JRNL DOI 10.1016/J.STR.2010.12.005
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 27860
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 SET) : 0.242
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 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 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 15
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PVB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-10.
REMARK 100 THE RCSB ID CODE IS RCSB062855.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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) : 1.00
REMARK 200 MONOCHROMATOR : GRAPHITE
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27860
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
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: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 2QCS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE RIA(73-244):C COMPLEX WAS
REMARK 280 CRYSTALLIZED IN 0.1M MES PH 6.0 AND 12% PEG 20,000 BY USING A
REMARK 280 DOUGLAS INSTRUMENTS ORYX8 CRYSTALLOGRAPHY ROBOT AS 1:1 PROTEIN
REMARK 280 SOLUTION:CRYSTALLIZING SOLUTION, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298.0 K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.40200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.70100
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.70100
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 93.40200
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 300 REMARK: ONE MOLECULE PER ASYMMETRICAL UNIT
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: 4680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 7 CG CD CE NZ
REMARK 470 LYS A 8 CG CD CE NZ
REMARK 470 GLU A 11 CG CD OE1 OE2
REMARK 470 GLN A 12 CG CD OE1 NE2
REMARK 470 LYS A 16 CG CD CE NZ
REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 LYS A 254 CG CD CE NZ
REMARK 470 SER A 263 OG
REMARK 470 ARG A 270 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 295 CG CD CE NZ
REMARK 470 LYS A 309 CG CD CE NZ
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 LYS A 345 CG CD CE NZ
REMARK 470 ASN B 86 CG OD1 ND2
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 GLU B 106 CG CD OE1 OE2
REMARK 470 SER B 110 OG
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 LYS B 128 CG CD CE NZ
REMARK 470 LYS B 132 CG CD CE NZ
REMARK 470 LYS B 240 CG CD CE NZ
REMARK 470 ARG B 241 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 242 CG CD CE NZ
REMARK 470 MET B 243 CG SD CE
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 PHE A 185 N PHE A 187 2.04
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 VAL A 98 CB - CA - C ANGL. DEV. = -18.7 DEGREES
REMARK 500 ALA A 233 CB - CA - C ANGL. DEV. = 11.8 DEGREES
REMARK 500 PRO B 117 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 ALA B 215 N - CA - CB ANGL. DEV. = -12.0 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 LYS A 7 -5.01 169.82
REMARK 500 LYS A 8 -88.80 -5.30
REMARK 500 PRO A 33 159.17 -44.52
REMARK 500 ASN A 36 83.99 53.13
REMARK 500 ALA A 38 -145.86 -167.71
REMARK 500 PHE A 54 -37.06 -137.76
REMARK 500 LEU A 59 54.56 -116.37
REMARK 500 PHE A 102 56.98 -91.09
REMARK 500 ARG A 165 -18.82 62.24
REMARK 500 ASP A 184 82.89 63.11
REMARK 500 PRO A 202 -60.33 -13.41
REMARK 500 PRO A 207 -60.51 -27.54
REMARK 500 ALA A 233 -55.45 -145.34
REMARK 500 PRO A 243 -70.46 -40.32
REMARK 500 PRO A 258 -158.93 -74.85
REMARK 500 LYS A 279 32.72 -144.13
REMARK 500 ASN A 283 11.15 -144.18
REMARK 500 LEU A 284 -145.75 -80.26
REMARK 500 ALA A 298 -54.40 -6.85
REMARK 500 PHE A 314 89.02 -163.11
REMARK 500 THR A 324 35.22 -76.45
REMARK 500 CYS A 343 114.63 60.33
REMARK 500 THR A 348 -56.58 -27.40
REMARK 500 ASN B 86 62.42 166.73
REMARK 500 PRO B 87 32.52 -147.74
REMARK 500 VAL B 88 93.14 75.65
REMARK 500 PRO B 117 131.85 -8.57
REMARK 500 GLN B 165 150.47 -44.25
REMARK 500 ASP B 170 -58.19 151.81
REMARK 500 TRP B 188 105.62 -43.05
REMARK 500 SER B 197 151.21 178.44
REMARK 500 GLU B 200 21.28 -57.32
REMARK 500 TYR B 205 2.09 -165.85
REMARK 500 ALA B 211 154.00 178.19
REMARK 500 LYS B 216 -65.71 -17.15
REMARK 500 THR B 217 -168.27 -116.16
REMARK 500 LYS B 240 70.14 -112.72
REMARK 500 LYS B 242 121.51 -178.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 SER A 212 25.0 L L OUTSIDE RANGE
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 400 N3B 138.5
REMARK 620 3 ANP A 400 O2A 89.3 73.7
REMARK 620 4 ANP A 400 O2G 122.3 67.2 140.8
REMARK 620 N 1 2 3
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 ANP A 400 O1G
REMARK 620 2 ASP A 184 OD1 125.9
REMARK 620 3 ASP A 184 OD2 94.3 52.5
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 ANP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1
REMARK 900
REMARK 900 RELATED ENTRIES
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
DBREF 3PVB A 6 350 UNP P05132 KAPCA_MOUSE 7 351
DBREF 3PVB B 84 243 UNP P00514 KAP0_BOVIN 85 244
SEQRES 1 A 345 ALA LYS LYS GLY SEP GLU GLN GLU SER VAL LYS GLU PHE
SEQRES 2 A 345 LEU ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU
SEQRES 3 A 345 THR PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP
SEQRES 4 A 345 ARG ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL
SEQRES 5 A 345 MET LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA
SEQRES 6 A 345 MET LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS
SEQRES 7 A 345 GLN ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN
SEQRES 8 A 345 ALA VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER
SEQRES 9 A 345 PHE LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR
SEQRES 10 A 345 VAL ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE
SEQRES 11 A 345 GLY ARG PHE SEP GLU PRO HIS ALA ARG PHE TYR ALA ALA
SEQRES 12 A 345 GLN ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP
SEQRES 13 A 345 LEU ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE
SEQRES 14 A 345 ASP GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE
SEQRES 15 A 345 ALA LYS ARG VAL LYS GLY ARG THR TRP TPO LEU CYS GLY
SEQRES 16 A 345 THR PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS
SEQRES 17 A 345 GLY TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL
SEQRES 18 A 345 LEU ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE
SEQRES 19 A 345 ALA ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER
SEQRES 20 A 345 GLY LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU
SEQRES 21 A 345 LYS ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR
SEQRES 22 A 345 LYS ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE
SEQRES 23 A 345 LYS ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA
SEQRES 24 A 345 ILE TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS
SEQRES 25 A 345 PHE LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR
SEQRES 26 A 345 GLU GLU GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS
SEQRES 27 A 345 GLY LYS GLU PHE THR GLU PHE
SEQRES 1 B 160 PRO PRO ASN PRO VAL VAL LYS GLY ARG ARG ARG ARG GLY
SEQRES 2 B 160 ALA ILE SER ALA GLU VAL TYR THR GLU GLU ASP ALA ALA
SEQRES 3 B 160 SER TYR VAL ARG LYS VAL ILE PRO LYS ASP TYR LYS THR
SEQRES 4 B 160 MET ALA ALA LEU ALA LYS ALA ILE GLU LYS ASN VAL LEU
SEQRES 5 B 160 PHE SER HIS LEU ASP ASP ASN GLU ARG SER ASP ILE PHE
SEQRES 6 B 160 ASP ALA MET PHE PRO VAL SER PHE ILE ALA GLY GLU THR
SEQRES 7 B 160 VAL ILE GLN GLN GLY ASP GLU GLY ASP ASN PHE TYR VAL
SEQRES 8 B 160 ILE ASP GLN GLY GLU MET ASP VAL TYR VAL ASN ASN GLU
SEQRES 9 B 160 TRP ALA THR SER VAL GLY GLU GLY GLY SER PHE GLY GLU
SEQRES 10 B 160 LEU ALA LEU ILE TYR GLY THR PRO ARG ALA ALA THR VAL
SEQRES 11 B 160 LYS ALA LYS THR ASN VAL LYS LEU TRP GLY ILE ASP ARG
SEQRES 12 B 160 ASP SER TYR ARG ARG ILE LEU MET GLY SER THR LEU ARG
SEQRES 13 B 160 LYS ARG LYS MET
MODRES 3PVB SEP A 10 SER PHOSPHOSERINE
MODRES 3PVB SEP A 139 SER PHOSPHOSERINE
MODRES 3PVB TPO A 197 THR PHOSPHOTHREONINE
MODRES 3PVB SEP A 338 SER PHOSPHOSERINE
HET SEP A 10 10
HET SEP A 139 10
HET TPO A 197 11
HET SEP A 338 10
HET ANP A 400 31
HET MN A 401 1
HET MN A 402 1
HET GOL B 1 6
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MN MANGANESE (II) ION
HETNAM GOL GLYCEROL
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 SEP 3(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 ANP C10 H17 N6 O12 P3
FORMUL 4 MN 2(MN 2+)
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *15(H2 O)
HELIX 1 1 SEP A 10 GLU A 31 1 22
HELIX 2 2 LYS A 76 LEU A 82 1 7
HELIX 3 3 GLN A 84 VAL A 98 1 15
HELIX 4 4 PHE A 129 ARG A 134 1 6
HELIX 5 5 SEP A 139 SER A 159 1 21
HELIX 6 6 LYS A 168 LEU A 172 5 5
HELIX 7 7 THR A 201 LEU A 205 5 5
HELIX 8 8 ALA A 206 SER A 212 1 7
HELIX 9 9 LYS A 217 ALA A 232 1 16
HELIX 10 10 GLN A 242 GLY A 253 1 12
HELIX 11 11 SER A 262 LEU A 273 1 12
HELIX 12 12 ASP A 276 ARG A 280 5 5
HELIX 13 13 VAL A 288 ASN A 293 1 6
HELIX 14 14 HIS A 294 ALA A 298 5 5
HELIX 15 15 ASP A 301 ARG A 308 1 8
HELIX 16 16 THR B 104 ALA B 109 1 6
HELIX 17 17 ASP B 119 ILE B 130 1 12
HELIX 18 18 ASP B 140 SER B 145 1 6
HELIX 19 19 SER B 145 MET B 151 1 7
HELIX 20 20 LEU B 201 GLY B 206 1 6
HELIX 21 21 ARG B 226 ARG B 239 1 14
SHEET 1 A 2 PHE A 43 ASP A 44 0
SHEET 2 A 2 LYS A 61 HIS A 62 -1 O LYS A 61 N ASP A 44
SHEET 1 B 5 THR A 48 THR A 51 0
SHEET 2 B 5 ARG A 56 MET A 58 -1 O VAL A 57 N LEU A 49
SHEET 3 B 5 TYR A 69 ASP A 75 -1 O ILE A 73 N ARG A 56
SHEET 4 B 5 ASN A 115 GLU A 121 -1 O MET A 120 N ALA A 70
SHEET 5 B 5 LEU A 106 LYS A 111 -1 N PHE A 110 O TYR A 117
SHEET 1 C 2 CYS A 199 GLY A 200 0
SHEET 2 C 2 ILE B 98 SER B 99 -1 O ILE B 98 N GLY A 200
SHEET 1 D 4 PHE B 152 PHE B 156 0
SHEET 2 D 4 VAL B 219 ASP B 225 -1 O GLY B 223 N PHE B 152
SHEET 3 D 4 ASN B 171 GLY B 178 -1 N PHE B 172 O ILE B 224
SHEET 4 D 4 SER B 197 PHE B 198 -1 O PHE B 198 N TYR B 173
SHEET 1 E 3 TRP B 188 VAL B 192 0
SHEET 2 E 3 MET B 180 TYR B 183 -1 N VAL B 182 O THR B 190
SHEET 3 E 3 THR B 212 LYS B 214 -1 O THR B 212 N TYR B 183
LINK C GLY A 9 N SEP A 10 1555 1555 1.33
LINK C SEP A 10 N GLU A 11 1555 1555 1.33
LINK C PHE A 138 N SEP A 139 1555 1555 1.32
LINK C SEP A 139 N GLU A 140 1555 1555 1.33
LINK C TRP A 196 N TPO A 197 1555 1555 1.34
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
LINK OD1 ASN A 171 MN MN A 401 1555 1555 1.77
LINK O1G ANP A 400 MN MN A 402 1555 1555 2.02
LINK N3B ANP A 400 MN MN A 401 1555 1555 2.04
LINK O2A ANP A 400 MN MN A 401 1555 1555 2.20
LINK OD1 ASP A 184 MN MN A 402 1555 1555 2.22
LINK O2G ANP A 400 MN MN A 401 1555 1555 2.49
LINK OD2 ASP A 184 MN MN A 402 1555 1555 2.61
SITE 1 AC1 23 GLY A 50 GLY A 52 SER A 53 PHE A 54
SITE 2 AC1 23 GLY A 55 VAL A 57 ALA A 70 LYS A 72
SITE 3 AC1 23 MET A 120 GLU A 121 VAL A 123 GLU A 127
SITE 4 AC1 23 LYS A 168 GLU A 170 ASN A 171 LEU A 173
SITE 5 AC1 23 THR A 183 ASP A 184 PHE A 327 MN A 401
SITE 6 AC1 23 MN A 402 ARG B 94 ALA B 97
SITE 1 AC2 3 ASN A 171 ASP A 184 ANP A 400
SITE 1 AC3 3 ASP A 166 ASP A 184 ANP A 400
SITE 1 AC4 5 GLU B 200 PRO B 208 ARG B 209 ALA B 210
SITE 2 AC4 5 ALA B 211
CRYST1 116.667 116.667 140.103 90.00 90.00 120.00 P 32 2 1 6
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 0.008571 0.004949 0.000000 0.00000
SCALE2 0.000000 0.009897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007138 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
