HEADER TRANSFERASE/TRANSFERASE REGULATOR 08-AUG-07 2QVS
TITLE CRYSTAL STRUCTURE OF TYPE IIA HOLOENZYME OF CAMP-DEPENDENT PROTEIN
TITLE 2 KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT;
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 TYPE II-ALPHA REGULATORY
COMPND 9 SUBUNIT;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRKACA, PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: PRKAR2A;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PRSET
KEYWDS CAMP-DEPENDENT PROTEIN KINASE, TYPE IIA HOLOENZYME, ISOFORM
KEYWDS 2 DIVERSITY, ALTERNATIVE SPLICING, ATP-BINDING, CYTOPLASM,
KEYWDS 3 LIPOPROTEIN, MYRISTATE, NUCLEOTIDE-BINDING, NUCLEUS,
KEYWDS 4 PHOSPHORYLATION, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE,
KEYWDS 5 ACETYLATION, CAMP-BINDING, TRANSFERASE-TRANSFERASE REGULATOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WU,S.H.J.BROWN,S.VON DAAKE,S.S.TAYLOR
REVDAT 3 30-AUG-23 2QVS 1 LINK
REVDAT 2 24-FEB-09 2QVS 1 VERSN
REVDAT 1 23-OCT-07 2QVS 0
JRNL AUTH J.WU,S.H.J.BROWN,S.VON DAAKE,S.S.TAYLOR
JRNL TITL PKA TYPE IIALPHA HOLOENZYME REVEALS A COMBINATORIAL STRATEGY
JRNL TITL 2 FOR ISOFORM DIVERSITY.
JRNL REF SCIENCE V. 318 274 2007
JRNL REFN ISSN 0036-8075
JRNL PMID 17932298
JRNL DOI 10.1126/SCIENCE.1146447
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.50
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) (%) : 78.4
REMARK 3 NUMBER OF REFLECTIONS : 26790
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) : 0.212
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1309
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 54
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.035
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4875
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 181
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.82000
REMARK 3 B22 (A**2) : 3.65000
REMARK 3 B33 (A**2) : 0.17000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.29
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.960
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 2QVS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000044117.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
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 : NULL
REMARK 200 OPTICS : KOHZU: DOUBLE CRYSTAL SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33730
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1ATP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M SODIUM FORMATE, PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295.5K
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 43.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.45000
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: 3510 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY 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 LYS E 319
REMARK 465 GLY E 320
REMARK 465 PRO E 321
REMARK 465 GLY E 322
REMARK 465 ASP E 323
REMARK 465 THR E 324
REMARK 465 SER E 325
REMARK 465 ASN E 326
REMARK 465 PHE E 327
REMARK 465 ASP E 328
REMARK 465 ASP E 329
REMARK 465 TYR E 330
REMARK 465 GLU E 331
REMARK 465 ASN B 110
REMARK 465 ASP B 111
REMARK 465 PRO B 112
REMARK 465 ARG B 113
REMARK 465 LEU B 393
REMARK 465 ASP B 394
REMARK 465 LEU B 395
REMARK 465 MET B 396
REMARK 465 ASP B 397
REMARK 465 PRO B 398
REMARK 465 GLY B 399
REMARK 465 GLN B 400
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 GLN E 42 CG CD OE1 NE2
REMARK 470 PHE E 43 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP E 44 CG OD1 OD2
REMARK 470 ARG E 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 46 CG1 CG2 CD1
REMARK 470 LYS E 47 CG CD CE NZ
REMARK 470 THR E 48 OG1 CG2
REMARK 470 LEU E 49 CG CD1 CD2
REMARK 470 THR E 51 OG1 CG2
REMARK 470 SER E 53 OG
REMARK 470 PHE E 54 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG E 56 CG CD NE CZ NH1 NH2
REMARK 470 VAL E 57 CG1 CG2
REMARK 470 MET E 58 CG SD CE
REMARK 470 VAL E 60 CG1 CG2
REMARK 470 LYS E 61 CG CD CE NZ
REMARK 470 LYS E 63 CG CD CE NZ
REMARK 470 GLU E 64 CG CD OE1 OE2
REMARK 470 SER E 65 OG
REMARK 470 MET E 71 CG SD CE
REMARK 470 LYS E 72 CG CD CE NZ
REMARK 470 ILE E 73 CG1 CG2 CD1
REMARK 470 LEU E 74 CG CD1 CD2
REMARK 470 ASP E 75 CG OD1 OD2
REMARK 470 LYS E 76 CG CD CE NZ
REMARK 470 GLN E 77 CG CD OE1 NE2
REMARK 470 LYS E 78 CG CD CE NZ
REMARK 470 VAL E 79 CG1 CG2
REMARK 470 VAL E 80 CG1 CG2
REMARK 470 LYS E 81 CG CD CE NZ
REMARK 470 LEU E 82 CG CD1 CD2
REMARK 470 LYS E 111 CG CD CE NZ
REMARK 470 ASP E 112 CG OD1 OD2
REMARK 470 ASN E 113 CG OD1 ND2
REMARK 470 SER E 114 OG
REMARK 470 ASN E 115 CG OD1 ND2
REMARK 470 LEU E 116 CG CD1 CD2
REMARK 470 TYR E 117 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET E 118 CG SD CE
REMARK 470 VAL E 119 CG1 CG2
REMARK 470 GLU E 332 CG CD OE1 OE2
REMARK 470 GLU E 333 CG CD OE1 OE2
REMARK 470 GLU E 334 CG CD OE1 OE2
REMARK 470 ILE E 335 CG1 CG2 CD1
REMARK 470 ARG E 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 339 CG1 CG2 CD1
REMARK 470 LYS E 345 CG CD CE NZ
REMARK 470 GLU E 349 CG CD OE1 OE2
REMARK 470 SER B 308 OG
REMARK 470 LYS B 309 CG CD CE NZ
REMARK 470 THR B 310 OG1 CG2
REMARK 470 LYS B 311 CG CD CE NZ
REMARK 470 SER B 312 OG
REMARK 470 ASN B 313 CG OD1 ND2
REMARK 470 LYS B 314 CG CD CE NZ
REMARK 470 ASN B 315 CG OD1 ND2
REMARK 470 ASN B 318 CG OD1 ND2
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 E 80 CB - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 LYS E 81 N - CA - CB ANGL. DEV. = 16.4 DEGREES
REMARK 500 LYS E 81 CA - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASN E 113 CB - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500 SER E 114 CB - CA - C ANGL. DEV. = 15.3 DEGREES
REMARK 500 SER E 114 N - CA - CB ANGL. DEV. = 10.0 DEGREES
REMARK 500 SER E 114 CA - C - O ANGL. DEV. = 18.9 DEGREES
REMARK 500 SER E 114 CA - C - N ANGL. DEV. = -21.6 DEGREES
REMARK 500 ASN E 115 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 ASN E 115 N - CA - C ANGL. DEV. = 23.8 DEGREES
REMARK 500 LEU E 116 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU E 116 CA - C - O ANGL. DEV. = 23.2 DEGREES
REMARK 500 LEU E 116 CA - C - N ANGL. DEV. = -23.6 DEGREES
REMARK 500 LYS B 314 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 LYS B 314 N - CA - C ANGL. DEV. = 20.7 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 THR E 32 62.36 -164.49
REMARK 500 ASN E 36 85.65 11.41
REMARK 500 THR E 37 -75.10 -84.71
REMARK 500 ASP E 44 -111.55 -86.74
REMARK 500 ARG E 45 138.95 172.40
REMARK 500 ILE E 46 -118.91 -126.54
REMARK 500 LYS E 47 -169.69 -67.34
REMARK 500 THR E 48 61.16 -150.31
REMARK 500 THR E 51 -109.64 -99.09
REMARK 500 SER E 53 11.86 -161.92
REMARK 500 LYS E 63 -97.16 -78.02
REMARK 500 VAL E 79 -159.77 -61.92
REMARK 500 VAL E 80 -28.07 71.61
REMARK 500 LYS E 81 -133.27 -95.65
REMARK 500 LEU E 82 -139.73 53.26
REMARK 500 HIS E 87 1.50 -57.12
REMARK 500 ASP E 112 107.95 160.60
REMARK 500 ASN E 113 -27.78 53.29
REMARK 500 ASN E 115 109.86 37.98
REMARK 500 LEU E 116 89.98 87.83
REMARK 500 ASP E 166 33.61 -150.39
REMARK 500 LYS E 168 150.15 176.81
REMARK 500 ASP E 184 91.61 66.05
REMARK 500 PHE E 185 33.08 -98.74
REMARK 500 ASN E 216 -121.38 -153.13
REMARK 500 LEU E 273 53.75 -93.70
REMARK 500 GLU E 333 -162.89 -162.36
REMARK 500 VAL E 337 -160.59 -64.50
REMARK 500 ILE E 339 10.16 59.09
REMARK 500 LYS E 342 -105.31 -95.34
REMARK 500 CYS E 343 19.54 -52.05
REMARK 500 GLU E 346 -37.82 -166.41
REMARK 500 GLU B 107 102.40 164.93
REMARK 500 GLU B 108 110.02 -12.85
REMARK 500 LYS B 137 -49.59 -28.79
REMARK 500 ASP B 159 -4.51 83.58
REMARK 500 ASP B 187 -138.81 63.35
REMARK 500 ASP B 280 132.24 -35.74
REMARK 500 SER B 299 143.26 -174.62
REMARK 500 SER B 308 77.04 -55.40
REMARK 500 LYS B 309 -43.77 -130.09
REMARK 500 THR B 310 50.57 -69.57
REMARK 500 SER B 312 -85.90 157.53
REMARK 500 ASN B 313 81.89 -176.65
REMARK 500 LYS B 314 74.29 69.36
REMARK 500 ASN B 315 179.13 135.19
REMARK 500 GLN B 319 -123.79 -157.86
REMARK 500 ASN B 340 56.05 -141.81
REMARK 500 SER B 391 -79.69 -46.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U7E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIA(91-244):C COMPLEX OF CAMP-DEPENDENT
REMARK 900 PROTEIN KINASE
REMARK 900 RELATED ID: 1CX4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TYPE II BETA REGULATORY SUBUNIT OF CAMP-
REMARK 900 DEPENDENT PROTEIN KINASE
REMARK 900 RELATED ID: 1RGS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TYPE IA REGULATORY SUBUNIT OF CAMP-
REMARK 900 DEPENDENT PROTEIN KINASE
DBREF 2QVS E 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 2QVS B 91 400 UNP P12367 KAP2_MOUSE 92 401
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 B 310 THR ARG ARG VAL SER VAL CYS ALA GLU THR PHE ASN PRO
SEQRES 2 B 310 ASP GLU GLU GLU GLU ASP ASN ASP PRO ARG VAL VAL HIS
SEQRES 3 B 310 PRO LYS THR ASP GLU GLN ARG CYS ARG LEU GLN GLU ALA
SEQRES 4 B 310 CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU ASP GLN GLU
SEQRES 5 B 310 GLN LEU SER GLN VAL LEU ASP ALA MET PHE GLU LYS ILE
SEQRES 6 B 310 VAL LYS THR ASP GLU HIS VAL ILE ASP GLN GLY ASP ASP
SEQRES 7 B 310 GLY ASP ASN PHE TYR VAL ILE GLU ARG GLY THR TYR ASP
SEQRES 8 B 310 ILE LEU VAL THR LYS ASP ASN GLN THR ARG SER VAL GLY
SEQRES 9 B 310 GLN TYR ASP ASN ARG GLY SER PHE GLY GLU LEU ALA LEU
SEQRES 10 B 310 MET TYR ASN THR PRO ARG ALA ALA THR ILE ILE ALA THR
SEQRES 11 B 310 SER GLU GLY SER LEU TRP GLY LEU ASP ARG VAL THR PHE
SEQRES 12 B 310 ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS LYS ARG LYS
SEQRES 13 B 310 MET PHE GLU SER PHE ILE GLU SER VAL PRO LEU PHE LYS
SEQRES 14 B 310 SER LEU GLU MET SER GLU ARG MET LYS ILE VAL ASP VAL
SEQRES 15 B 310 ILE GLY GLU LYS ILE TYR LYS ASP GLY GLU ARG ILE ILE
SEQRES 16 B 310 ALA GLN GLY GLU LYS ALA ASP SER PHE TYR ILE ILE GLU
SEQRES 17 B 310 SER GLY GLU VAL SER ILE LEU ILE ARG SER LYS THR LYS
SEQRES 18 B 310 SER ASN LYS ASN GLY GLY ASN GLN GLU VAL GLU ILE ALA
SEQRES 19 B 310 HIS CYS HIS LYS GLY GLN TYR PHE GLY GLU LEU ALA LEU
SEQRES 20 B 310 VAL THR ASN LYS PRO ARG ALA ALA SER ALA TYR GLY VAL
SEQRES 21 B 310 GLY ASP VAL LYS CYS LEU VAL MET ASP VAL GLN ALA PHE
SEQRES 22 B 310 GLU ARG LEU LEU GLY PRO CYS MET ASP ILE MET LYS ARG
SEQRES 23 B 310 ASN ILE SER HIS TYR GLU GLU GLN LEU VAL LYS MET PHE
SEQRES 24 B 310 GLY SER ASN LEU ASP LEU MET ASP PRO GLY GLN
MODRES 2QVS TPO E 197 THR PHOSPHOTHREONINE
MODRES 2QVS SEP E 338 SER PHOSPHOSERINE
HET TPO E 197 11
HET SEP E 338 10
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 HOH *181(H2 O)
HELIX 1 1 GLU E 13 GLU E 31 1 19
HELIX 2 2 GLN E 39 PHE E 43 5 5
HELIX 3 3 ILE E 85 VAL E 98 1 14
HELIX 4 4 MET E 128 GLY E 136 1 9
HELIX 5 5 SER E 139 LEU E 160 1 22
HELIX 6 6 LYS E 168 GLU E 170 5 3
HELIX 7 7 THR E 201 LEU E 205 5 5
HELIX 8 8 ALA E 206 LEU E 211 1 6
HELIX 9 9 LYS E 217 GLY E 234 1 18
HELIX 10 10 GLN E 242 GLY E 253 1 12
HELIX 11 11 SER E 262 LEU E 273 1 12
HELIX 12 12 VAL E 288 ASN E 293 1 6
HELIX 13 13 HIS E 294 ALA E 298 5 5
HELIX 14 14 ASP E 301 GLN E 307 1 7
HELIX 15 15 LYS E 342 GLU E 346 5 5
HELIX 16 16 THR B 119 LYS B 131 1 13
HELIX 17 17 ILE B 133 ASN B 138 1 6
HELIX 18 18 ASP B 140 MET B 151 1 12
HELIX 19 19 GLY B 203 MET B 208 5 6
HELIX 20 20 ARG B 230 SER B 254 1 25
HELIX 21 21 VAL B 255 LYS B 259 5 5
HELIX 22 22 GLU B 262 ILE B 273 1 12
HELIX 23 23 GLY B 333 VAL B 338 5 6
HELIX 24 24 VAL B 360 GLY B 368 1 9
HELIX 25 25 PRO B 369 ASN B 377 1 9
HELIX 26 26 HIS B 380 GLY B 390 1 11
SHEET 1 A 4 ARG E 56 LYS E 61 0
SHEET 2 A 4 HIS E 68 ILE E 73 -1 O TYR E 69 N VAL E 60
SHEET 3 A 4 TYR E 117 GLU E 121 -1 O MET E 120 N ALA E 70
SHEET 4 A 4 LEU E 106 PHE E 110 -1 N PHE E 108 O VAL E 119
SHEET 1 B 3 GLY E 126 GLU E 127 0
SHEET 2 B 3 LEU E 172 ILE E 174 -1 O ILE E 174 N GLY E 126
SHEET 3 B 3 ILE E 180 VAL E 182 -1 O GLN E 181 N LEU E 173
SHEET 1 C 2 LEU E 162 ILE E 163 0
SHEET 2 C 2 LYS E 189 ARG E 190 -1 O LYS E 189 N ILE E 163
SHEET 1 D 2 CYS E 199 GLY E 200 0
SHEET 2 D 2 VAL B 96 CYS B 97 -1 O VAL B 96 N GLY E 200
SHEET 1 E 4 PHE B 152 VAL B 156 0
SHEET 2 E 4 GLY B 223 ASP B 229 -1 O GLY B 227 N PHE B 152
SHEET 3 E 4 ASN B 171 ARG B 177 -1 N VAL B 174 O TRP B 226
SHEET 4 E 4 SER B 201 PHE B 202 -1 O PHE B 202 N TYR B 173
SHEET 1 F 4 HIS B 161 ILE B 163 0
SHEET 2 F 4 THR B 216 ALA B 219 -1 O ILE B 217 N VAL B 162
SHEET 3 F 4 THR B 179 LYS B 186 -1 N LEU B 183 O THR B 216
SHEET 4 F 4 GLN B 189 ASP B 197 -1 O GLY B 194 N ILE B 182
SHEET 1 G 4 GLY B 274 TYR B 278 0
SHEET 2 G 4 SER B 346 ASP B 359 -1 O VAL B 353 N TYR B 278
SHEET 3 G 4 SER B 293 ILE B 306 -1 N GLU B 301 O VAL B 350
SHEET 4 G 4 VAL B 321 HIS B 327 -1 O VAL B 321 N ILE B 306
SHEET 1 H 4 ARG B 283 ILE B 285 0
SHEET 2 H 4 SER B 346 ASP B 359 -1 O ALA B 347 N ILE B 284
SHEET 3 H 4 SER B 293 ILE B 306 -1 N GLU B 301 O VAL B 350
SHEET 4 H 4 TYR B 331 PHE B 332 -1 O PHE B 332 N TYR B 295
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
CRYST1 87.900 92.900 118.000 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 0.011377 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008475 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
