HEADER TRANSFERASE(PHOSPHOTRANSFERASE) 18-JAN-93 1APM
TITLE 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF
TITLE 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND
TITLE 3 DETERGENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE;
COMPND 3 CHAIN: E;
COMPND 4 EC: 2.7.1.37;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PEPTIDE INHIBITOR PKI(5-24);
COMPND 8 CHAIN: I;
COMPND 9 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 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090
KEYWDS TRANSFERASE(PHOSPHOTRANSFERASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TENEYCK,N.-H.XUONG,S.S.TAYLOR,
AUTHOR 2 J.M.SOWADSKI
REVDAT 4 14-AUG-19 1APM 1 REMARK
REVDAT 3 17-JUL-19 1APM 1 REMARK LINK
REVDAT 2 24-FEB-09 1APM 1 VERSN
REVDAT 1 15-APR-93 1APM 0
JRNL AUTH D.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN EYCK,N.H.XUONG,
JRNL AUTH 2 S.S.TAYLOR,J.M.SOWADSKI
JRNL TITL 2.0 A REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF
JRNL TITL 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE
JRNL TITL 3 INHIBITOR AND DETERGENT.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 49 357 1993
JRNL REFN ISSN 0907-4449
JRNL PMID 15299526
JRNL DOI 10.1107/S0907444993000502
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZHENG,D.R.KNIGHTON,L.F.TENEYCK,R.KARLSSON,N.-H.XUONG,
REMARK 1 AUTH 2 S.S.TAYLOR,J.M.SOWADSKI
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT
REMARK 1 TITL 2 PROTEIN KINASE COMPLEXED WITH MG/ATP AND PEPTIDE INHIBITOR
REMARK 1 REF BIOCHEMISTRY V. 32 2154 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.R.KNIGHTON,J.ZHENG,L.F.TENEYCK,V.A.ASHFORD,N.-H.XUONG,
REMARK 1 AUTH 2 S.S.TAYLOR,J.M.SOWADSKI
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC
REMARK 1 TITL 2 ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE
REMARK 1 REF SCIENCE V. 253 407 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.R.KNIGHTON,J.ZHENG,L.F.TENEYCK,N.-H.XUONG,S.S.TAYLOR,
REMARK 1 AUTH 2 J.M.SOWADSKI
REMARK 1 TITL STRUCTURE OF A PEPTIDE INHIBITOR BOUND TO THE CATALYTIC
REMARK 1 TITL 2 SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN
REMARK 1 TITL 3 KINASE
REMARK 1 REF SCIENCE V. 253 414 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 4
REMARK 1 AUTH L.W.SLICE,S.S.TAYLOR
REMARK 1 TITL EXPRESSION OF THE CATALYTIC SUBUNIT OF C/AMP-DEPENDENT
REMARK 1 TITL 2 PROTEIN KINASE IN ESCHERICHIA COLI
REMARK 1 REF J.BIOL.CHEM. V. 264 20940 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
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 : 2846
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 207
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) : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL ; 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:
REMARK 3 RESIDUES E 51-E 55, E 319-E 322, AND I 23-I 24 HAVE WEAK
REMARK 3 BACKBONE ELECTRON DENSITY.
REMARK 4
REMARK 4 1APM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171101.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 36.92000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.50500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.50500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.92000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.88000
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: 3000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 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 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 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 CE NZ
REMARK 470 SER E 34 OG
REMARK 470 GLN E 39 CG CD OE1 NE2
REMARK 470 ASP E 41 CG OD1 OD2
REMARK 470 ARG E 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 63 CD CE NZ
REMARK 470 GLU E 64 CG CD OE1 OE2
REMARK 470 LYS E 78 CD CE NZ
REMARK 470 LYS E 83 CD CE NZ
REMARK 470 LYS E 105 CD CE NZ
REMARK 470 GLU E 121 CG CD OE1 OE2
REMARK 470 GLN E 176 CG CD OE1 NE2
REMARK 470 GLN E 177 CG CD OE1 NE2
REMARK 470 LYS E 213 CG CD CE NZ
REMARK 470 LYS E 217 CG CD CE NZ
REMARK 470 LYS E 249 CG CD CE NZ
REMARK 470 LYS E 254 CG CD CE NZ
REMARK 470 ARG E 256 CD NE CZ NH1 NH2
REMARK 470 LYS E 266 CG CD CE NZ
REMARK 470 ARG E 270 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 279 CG CD CE NZ
REMARK 470 LYS E 285 CG CD CE NZ
REMARK 470 GLU E 311 CG CD OE1 OE2
REMARK 470 LYS E 317 CG CD CE NZ
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 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 OE1 0.076
REMARK 500 GLU E 140 CD GLU E 140 OE2 0.074
REMARK 500 GLU E 230 CD GLU E 230 OE1 0.068
REMARK 500 GLU E 341 CD GLU E 341 OE2 0.067
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 44 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 VAL E 60 CA - CB - CG2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASP E 75 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP E 75 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP E 112 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG E 134 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG E 134 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP E 161 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP E 161 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP E 184 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP E 220 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP E 220 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 TYR E 247 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP E 264 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP E 267 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP E 267 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP E 290 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP E 301 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP E 323 CB - CG - OD1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP E 329 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP I 24 CB - CG - OD1 ANGL. DEV. = 5.8 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 ILE E 46 -62.66 -93.81
REMARK 500 ASN E 99 101.93 -166.19
REMARK 500 ARG E 165 -2.38 71.67
REMARK 500 LYS E 168 149.32 178.15
REMARK 500 ASP E 184 88.79 62.58
REMARK 500 ASN E 216 -162.25 -128.97
REMARK 500 LEU E 273 41.26 -85.27
REMARK 500 HIS I 23 -23.40 -147.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 INHIBITOR RESIDUE NUMBERING CORRESPONDS TO NUMBERS FROM
REMARK 600 THE SEQUENCE OF THE LARGER NATURALLY OCCURRING PKI PROTEIN
REMARK 600 OF WHICH THE INHIBITOR IS A SYNTHETIC FRAGMENT.
REMARK 600
REMARK 600 THE MODEL HAS AN N-OCTANE RESIDUE (OCT) THAT IS USED TO
REMARK 600 MODEL THE THE ORDERED PART OF A MEGA-8 (OCTANOYL-N-
REMARK 600 METHYLGLUCAMIDE) DETERGENT MOLECULE OBSERVED NEAR THE
REMARK 600 N-TERMINAL HELIX.
DBREF 1APM E 1 350 UNP P05132 KAPCA_MOUSE 1 350
DBREF 1APM I 5 24 UNP P63248 IPKA_MOUSE 5 24
SEQADV 1APM ALA E 139 UNP P05132 SER 139 ENGINEERED
SEQRES 1 E 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP 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 ALA 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 ASN ALA ILE HIS ASP
MODRES 1APM SEP E 10 SER PHOSPHOSERINE
MODRES 1APM TPO E 197 THR PHOSPHOTHREONINE
MODRES 1APM SEP E 338 SER PHOSPHOSERINE
HET SEP E 10 10
HET TPO E 197 11
HET SEP E 338 10
HET OCT E 354 8
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM OCT N-OCTANE
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 OCT C8 H18
FORMUL 4 HOH *207(H2 O)
HELIX 1 A GLU E 11 GLU E 31 1 21
HELIX 2 AB LEU E 40 GLN E 42 5NOT NOTED IN REF 2 3
HELIX 3 B LYS E 76 LYS E 81 1 6
HELIX 4 C ILE E 85 ALA E 97 1 13
HELIX 5 D MET E 128 ILE E 135 1 8
HELIX 6 E GLU E 140 SER E 159 1 20
HELIX 7 EF0 PRO E 169 ASN E 171 5NOT NOTED IN REF 2 3
HELIX 8 EF1 PRO E 202 TYR E 204 5NOT NOTED IN REF 2 3
HELIX 9 EF2 PRO E 207 ILE E 210 1NOT NOTED IN REF 2 4
HELIX 10 F ALA E 218 ALA E 233 1 16
HELIX 11 G PRO E 243 SER E 252 1 10
HELIX 12 H SER E 263 LEU E 272 1 10
HELIX 13 I ASN E 289 LYS E 292 1 4
HELIX 14 IJ LYS E 295 PHE E 297 5NOT NOTED IN REF 2 3
HELIX 15 J TRP E 302 GLN E 307 1 6
HELIX 16 IA THR I 6 ALA I 12 1INHIBITOR N-TERMINAL HELIX 7
SHEET 1 A 5 PHE E 43 THR E 51 0
SHEET 2 A 5 GLY E 55 HIS E 62 -1
SHEET 3 A 5 HIS E 68 ASP E 75 -1
SHEET 4 A 5 ASN E 115 GLU E 121 -1
SHEET 5 A 5 LEU E 106 LYS E 111 -1
SHEET 1 B 2 LEU E 162 ILE E 163 0
SHEET 2 B 2 LEU E 172 ILE E 174 -1
SHEET 1 C 2 ILE E 180 VAL E 182 0
SHEET 2 C 2 LYS E 189 ARG E 190 -1
LINK C SEP E 10 N GLU E 11 1555 1555 1.34
LINK C TRP E 196 N TPO E 197 1555 1555 1.31
LINK C TPO E 197 N LEU E 198 1555 1555 1.32
LINK C VAL E 337 N SEP E 338 1555 1555 1.33
LINK C SEP E 338 N ILE E 339 1555 1555 1.34
CRYST1 73.840 75.760 81.010 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 0.013543 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013200 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012344 0.00000
HETATM 1 N SEP E 10 -7.153 -20.816 -14.915 1.00 36.59 N
HETATM 2 CA SEP E 10 -8.344 -20.050 -14.482 1.00 34.88 C
HETATM 3 CB SEP E 10 -9.516 -20.906 -13.949 1.00100.00 C
HETATM 4 OG SEP E 10 -10.760 -20.216 -14.040 1.00100.00 O
HETATM 5 C SEP E 10 -7.992 -18.823 -13.599 1.00 43.48 C
HETATM 6 O SEP E 10 -8.385 -17.670 -13.880 1.00 46.16 O
HETATM 7 P SEP E 10 -12.192 -20.937 -13.799 1.00100.00 P
HETATM 8 O1P SEP E 10 -12.854 -20.167 -12.708 1.00100.00 O
HETATM 9 O2P SEP E 10 -12.444 -21.872 -14.958 1.00 51.82 O
HETATM 10 O3P SEP E 10 -12.129 -21.747 -12.565 1.00100.00 O
(ATOM LINES ARE NOT SHOWN.)
END
