HEADER TRANSFERASE/TRANSFERASE INHIBITOR 16-JUL-01 1JLU
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN
TITLE 2 KINASE COMPLEXED WITH A PHOSPHORYLATED SUBSTRATE PEPTIDE AND
TITLE 3 DETERGENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.1.37;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, MUSCLE/BRAIN FORM;
COMPND 9 CHAIN: S;
COMPND 10 FRAGMENT: RESIDUES 5-24;
COMPND 11 SYNONYM: PKI-ALPHA;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 10 OF THE PEPTIDE IS NATURALLY FOUND IN MUS MUSCULUS (MOUSE).
KEYWDS PROTEIN KINASE-PHOSPHORYLATED SUBSTRATE COMPLEX, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR MADHUSUDAN,E.A.TRAFNY,N.-H.XUONG,J.A.ADAMS,L.F.TEN EYCK,S.S.TAYLOR,
AUTHOR 2 J.M.SOWADSKI
REVDAT 5 04-OCT-17 1JLU 1 REMARK
REVDAT 4 13-JUL-11 1JLU 1 VERSN
REVDAT 3 24-FEB-09 1JLU 1 VERSN
REVDAT 2 01-APR-03 1JLU 1 JRNL
REVDAT 1 01-AUG-01 1JLU 0
JRNL AUTH MADHUSUDAN,E.A.TRAFNY,N.H.XUONG,J.A.ADAMS,L.F.TEN EYCK,
JRNL AUTH 2 S.S.TAYLOR,J.M.SOWADSKI
JRNL TITL CAMP-DEPENDENT PROTEIN KINASE: CRYSTALLOGRAPHIC INSIGHTS
JRNL TITL 2 INTO SUBSTRATE RECOGNITION AND PHOSPHOTRANSFER.
JRNL REF PROTEIN SCI. V. 3 176 1994
JRNL REFN ISSN 0961-8368
JRNL PMID 8003955
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN EYCK,N.XUONG,
REMARK 1 AUTH 2 S.S.TAYLOR,J.M.SOWADSKI
REMARK 1 TITL 2.0 A REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF
REMARK 1 TITL 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE
REMARK 1 TITL 3 INHIBITOR AND DETERGENT
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 49 357 1993
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444993000502
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.ZHENG,E.A.TRAFNY,D.R.KNIGHTON,N.XUONG,S.S.TAYLOR,
REMARK 1 AUTH 2 L.F.TEN EYCK,J.M.SOWADSKI
REMARK 1 TITL 2.2 A REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF
REMARK 1 TITL 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A
REMARK 1 TITL 3 PEPTIDE INHIBITOR
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 49 362 1993
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444993000423
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 19924
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2838
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.017 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.400 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JLU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013920.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-92
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : UCSD-SYSTEM
REMARK 200 DATA SCALING SOFTWARE : UCSD-SYSTEM
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19924
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04300
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) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1ATP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP, PH
REMARK 280 8.0,277K, 10MM DITHIOTHREITOL, 8% DOW POLYETHYLENE GLYCOL 400,
REMARK 280 METHANOL, BICINE, VAPOR DIFFUSION, HANGING DROP
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 36.93500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.35000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.79000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.35000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.93500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.79000
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: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, S
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 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 12 CG CD OE1 NE2
REMARK 470 SER E 14 OG
REMARK 470 LYS E 16 CG CD CE NZ
REMARK 470 GLU E 17 CG CD OE1 OE2
REMARK 470 LYS E 21 CG CD CE NZ
REMARK 470 GLU E 24 CG CD OE1 OE2
REMARK 470 ASP E 25 CG OD1 OD2
REMARK 470 LYS E 28 CG CD CE NZ
REMARK 470 GLU E 31 CG CD OE1 OE2
REMARK 470 ARG E 45 CG CD NE CZ NH1 NH2
REMARK 470 SER E 53 OG
REMARK 470 GLU E 64 CG CD OE1 OE2
REMARK 470 LYS E 83 CG CD CE NZ
REMARK 470 GLU E 86 CG CD OE1 OE2
REMARK 470 GLN E 242 CG CD OE1 NE2
REMARK 470 ARG E 256 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 270 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 276 CG OD1 OD2
REMARK 470 THR E 278 OG1 CG2
REMARK 470 LYS E 279 CG CD CE NZ
REMARK 470 GLU E 311 CG CD OE1 OE2
REMARK 470 LYS E 317 CG CD CE NZ
REMARK 470 PHE E 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS E 319 CG CD CE NZ
REMARK 470 GLU E 331 CG CD OE1 OE2
REMARK 470 GLU E 333 CG CD OE1 OE2
REMARK 470 GLU E 334 CG CD OE1 OE2
REMARK 470 ARG E 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 339 CG1 CG2 CD1
REMARK 470 ASN E 340 CG OD1 ND2
REMARK 470 LYS E 345 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU E 13 CD GLU E 13 OE2 0.094
REMARK 500 GLU E 127 CD GLU E 127 OE2 0.076
REMARK 500 GLU E 140 CD GLU E 140 OE2 0.070
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 ASP E 41 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP E 44 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG E 93 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG E 93 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP E 112 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP E 112 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ARG E 137 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP E 161 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP E 175 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP E 184 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP E 184 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 PHE E 187 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP E 220 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP E 220 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TYR E 229 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP E 241 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 241 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP E 267 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP E 290 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP E 290 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG E 308 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG S 374 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG S 375 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG S 375 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP S 380 CB - CG - OD1 ANGL. DEV. = 5.5 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 ASN E 36 75.47 40.58
REMARK 500 GLN E 42 0.31 -67.90
REMARK 500 ASN E 99 105.28 -170.98
REMARK 500 ARG E 165 -0.29 73.92
REMARK 500 ASP E 184 85.22 62.47
REMARK 500 PRO E 202 -64.85 -23.05
REMARK 500 ASN E 216 -158.75 -121.10
REMARK 500 LEU E 273 47.16 -85.62
REMARK 500 ASN E 286 -15.51 111.83
REMARK 500 CYS E 343 66.08 34.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OCT E 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN S OF CAMP-DEPENDENT
REMARK 800 PROTEIN KINASE INHIBITOR, MUSCLE/BRAIN FORM
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1APM RELATED DB: PDB
REMARK 900 1APM CONTAINS THE SAME PROTEIN COMPLEXED WITH PEPTIDE INHIBITOR AND
REMARK 900 DETERGENT
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 1ATP CONTAINS THE SAME PROTEIN COMPLEXED WITH MNATP AND PEPTIDE
REMARK 900 INHIBITOR
DBREF 1JLU E 1 350 UNP P05132 KAPCA_MOUSE 1 350
DBREF 1JLU S 361 380 UNP P27776 IPKA_MOUSE 5 24
SEQADV 1JLU ALA S 376 UNP P27776 ASN 20 ENGINEERED MUTATION
SEQADV 1JLU SEP S 377 UNP P27776 ALA 21 ENGINEERED MUTATION
SEQRES 1 E 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 E 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 E 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 E 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 E 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 E 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 E 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 E 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 E 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 E 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 E 350 HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA
SEQRES 12 E 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 E 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 E 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 E 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 E 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 E 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 E 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 E 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 E 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 E 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 E 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 E 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 E 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 E 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 E 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 E 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 S 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 S 20 ARG ARG ALA SEP ILE HIS ASP
MODRES 1JLU TPO E 197 THR PHOSPHOTHREONINE
MODRES 1JLU SEP E 338 SER PHOSPHOSERINE
MODRES 1JLU SEP S 377 SER PHOSPHOSERINE
HET TPO E 197 11
HET SEP E 338 10
HET SEP S 377 10
HET OCT E 381 8
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM OCT N-OCTANE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 OCT C8 H18
FORMUL 4 HOH *116(H2 O)
HELIX 1 1 GLN E 12 THR E 32 1 21
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 VAL E 98 1 15
HELIX 5 5 GLU E 127 GLY E 136 1 10
HELIX 6 6 SER E 139 LEU E 160 1 22
HELIX 7 7 LYS E 168 GLU E 170 5 3
HELIX 8 8 THR E 201 LEU E 205 5 5
HELIX 9 9 ALA E 206 LEU E 211 1 6
HELIX 10 10 LYS E 217 GLY E 234 1 18
HELIX 11 11 GLN E 242 GLY E 253 1 12
HELIX 12 12 SER E 262 LEU E 273 1 12
HELIX 13 13 GLY E 287 ASN E 293 1 7
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 GLY E 344 THR E 348 5 5
HELIX 17 17 THR S 361 ALA S 368 1 8
SHEET 1 A 5 PHE E 43 THR E 51 0
SHEET 2 A 5 GLY E 55 HIS E 62 -1 O VAL E 57 N LEU E 49
SHEET 3 A 5 ASN E 67 ASP E 75 -1 O ASN E 67 N HIS E 62
SHEET 4 A 5 ASN E 115 GLU E 121 -1 O LEU E 116 N LEU E 74
SHEET 5 A 5 LEU E 106 LYS E 111 -1 N GLU E 107 O VAL E 119
SHEET 1 B 2 LEU E 162 ILE E 163 0
SHEET 2 B 2 LYS E 189 ARG E 190 -1 O LYS E 189 N ILE E 163
SHEET 1 C 2 LEU E 172 ILE E 174 0
SHEET 2 C 2 ILE E 180 VAL E 182 -1 O GLN E 181 N LEU E 173
LINK C TRP E 196 N TPO E 197 1555 1555 1.32
LINK C TPO E 197 N LEU E 198 1555 1555 1.29
LINK C VAL E 337 N SEP E 338 1555 1555 1.34
LINK C SEP E 338 N ILE E 339 1555 1555 1.36
LINK C ALA S 376 N SEP S 377 1555 1555 1.33
LINK C SEP S 377 N ILE S 378 1555 1555 1.34
SITE 1 AC1 2 PHE E 18 GLU E 155
SITE 1 AC2 36 GLN E 84 ARG E 93 GLU E 127 PHE E 129
SITE 2 AC2 36 ARG E 133 ASP E 166 LYS E 168 GLU E 170
SITE 3 AC2 36 ASP E 184 PHE E 187 ARG E 190 VAL E 191
SITE 4 AC2 36 LYS E 192 LEU E 198 CYS E 199 GLY E 200
SITE 5 AC2 36 THR E 201 GLU E 203 GLU E 230 TYR E 235
SITE 6 AC2 36 PHE E 239 ALA E 240 ASP E 241 TYR E 330
SITE 7 AC2 36 GLU E 349 HOH E 407 HOH E 419 HOH S 401
SITE 8 AC2 36 HOH S 422 HOH S 425 HOH S 429 HOH S 442
SITE 9 AC2 36 HOH S 450 HOH S 455 HOH S 485 HOH S 497
CRYST1 73.870 75.580 80.700 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 0.013537 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013231 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012392 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
