HEADER TRANSFERASE(PHOSPHOTRANSFERASE) 08-JAN-93 1ATP
TITLE 2.2 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF
TITLE 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A PEPTIDE
TITLE 3 INHIBITOR
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 J.ZHENG,E.A.TRAFNY,D.R.KNIGHTON,N.-H.XUONG,S.S.TAYLOR,L.F.TENEYCK,
AUTHOR 2 J.M.SOWADSKI
REVDAT 4 14-AUG-19 1ATP 1 REMARK
REVDAT 3 17-JUL-19 1ATP 1 REMARK LINK
REVDAT 2 24-FEB-09 1ATP 1 VERSN
REVDAT 1 15-APR-93 1ATP 0
JRNL AUTH J.ZHENG,E.A.TRAFNY,D.R.KNIGHTON,N.H.XUONG,S.S.TAYLOR,
JRNL AUTH 2 L.F.TEN EYCK,J.M.SOWADSKI
JRNL TITL 2.2 A REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF
JRNL TITL 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A
JRNL TITL 3 PEPTIDE INHIBITOR.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 49 362 1993
JRNL REFN ISSN 0907-4449
JRNL PMID 15299527
JRNL DOI 10.1107/S0907444993000423
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TENEYCK,N.-H.XUONG,
REMARK 1 AUTH 2 S.S.TAYLOR,J.M.SOWADSKI
REMARK 1 TITL 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC
REMARK 1 TITL 2 SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A
REMARK 1 TITL 3 PEPTIDE INHIBITOR AND DETERGENT
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
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 3
REMARK 1 AUTH D.R.KNIGHTON,J.ZHENG,L.F.TENEYCK,V.A.XUONG,N.-H.ASHFORD,
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 4
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 5
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. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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) : 0.177
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 : 2934
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 103
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: NULL
REMARK 4
REMARK 4 1ATP 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_1000171245.
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 (%): 53.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
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 36.79000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.29000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.14000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.29000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.79000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.14000
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: 3770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 465 SER E 10
REMARK 465 GLU E 11
REMARK 465 GLN E 12
REMARK 465 GLU E 13
REMARK 465 SER E 14
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 TYR E 164 O HOH E 424 1.14
REMARK 500 O ARG E 165 N ASP E 166 1.78
REMARK 500 ND2 ASN E 326 O HOH E 605 1.95
REMARK 500 C TYR E 164 O HOH E 424 2.10
REMARK 500
REMARK 500 REMARK: NULL
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 17 CD GLU E 17 OE2 0.073
REMARK 500 GLU E 24 CD GLU E 24 OE2 0.068
REMARK 500 GLU E 31 CD GLU E 31 OE1 0.067
REMARK 500 GLU E 64 CD GLU E 64 OE2 0.069
REMARK 500 GLU E 91 CD GLU E 91 OE2 -0.068
REMARK 500 GLU E 140 CD GLU E 140 OE2 0.067
REMARK 500 ARG E 165 C ASP E 166 N -0.199
REMARK 500 GLU E 170 CD GLU E 170 OE2 0.085
REMARK 500 GLU E 203 CD GLU E 203 OE2 0.082
REMARK 500 GLU E 248 CD GLU E 248 OE1 0.071
REMARK 500 GLU E 331 CD GLU E 331 OE2 0.072
REMARK 500 GLU E 333 CD GLU E 333 OE2 0.075
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 - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP E 44 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG E 56 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP E 75 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP E 112 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG E 137 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP E 161 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP E 161 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG E 165 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG E 165 CA - C - N ANGL. DEV. = 23.8 DEGREES
REMARK 500 ARG E 165 O - C - N ANGL. DEV. = -25.8 DEGREES
REMARK 500 ASP E 166 CA - C - N ANGL. DEV. = -13.9 DEGREES
REMARK 500 ARG E 194 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP E 241 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP E 267 CB - CG - OD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ASP E 290 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 LYS E 317 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG I 18 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP I 24 CB - CG - OD1 ANGL. DEV. = -5.9 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 75.09 29.48
REMARK 500 ILE E 46 -86.36 -107.73
REMARK 500 ARG E 165 19.16 51.81
REMARK 500 ASP E 166 76.02 -157.62
REMARK 500 THR E 183 -165.60 -105.27
REMARK 500 ASP E 184 87.06 48.73
REMARK 500 PRO E 202 -60.76 -24.26
REMARK 500 LEU E 273 45.13 -94.84
REMARK 500 LEU E 277 -2.74 -55.75
REMARK 500 GLU E 311 99.60 -64.65
REMARK 500 LYS E 342 -60.79 -90.98
REMARK 500 HIS I 23 -136.73 -144.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG E 165 -10.44
REMARK 500 ASP E 166 -23.89
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 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 E 351 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP E 355 O1B
REMARK 620 2 HOH E 447 O 170.9
REMARK 620 3 ATP E 355 O3G 91.2 95.1
REMARK 620 4 HOH E 477 O 90.4 92.6 116.2
REMARK 620 5 ASP E 184 OD2 80.7 92.7 89.9 152.7
REMARK 620 6 ASP E 184 OD1 80.5 90.8 149.1 93.7 59.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E 352 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP E 355 O2G
REMARK 620 2 HOH E 635 O 84.9
REMARK 620 3 ATP E 355 O2A 127.3 88.4
REMARK 620 4 ASP E 184 OD2 87.1 167.9 89.3
REMARK 620 5 ASN E 171 OD1 116.5 96.1 116.2 95.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: NULL
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: NULL
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 355
DBREF 1ATP E 1 350 UNP P05132 KAPCA_MOUSE 1 350
DBREF 1ATP I 5 24 UNP P63248 IPKA_MOUSE 5 24
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 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 1ATP TPO E 197 THR PHOSPHOTHREONINE
MODRES 1ATP SEP E 338 SER PHOSPHOSERINE
HET TPO E 197 11
HET SEP E 338 10
HET MN E 351 1
HET MN E 352 1
HET ATP E 355 31
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM MN MANGANESE (II) ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 MN 2(MN 2+)
FORMUL 5 ATP C10 H16 N5 O13 P3
FORMUL 6 HOH *103(H2 O)
HELIX 1 A LYS E 16 GLU E 31 1 16
HELIX 2 AB LEU E 40 GLN E 42 5NOT NOTED IN REF 3 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 3 3
HELIX 8 EF1 PRO E 202 TYR E 204 5NOT NOTED IN REF 3 3
HELIX 9 EF2 PRO E 207 ILE E 210 1NOT NOTED IN REF 3 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 3 3
HELIX 15 J TRP E 302 TYR E 306 1 5
HELIX 16 IA THR I 6 ILE I 11 1INHIBITOR N-TERMINAL HELIX 6
SHEET 1 A 5 PHE E 43 THR E 51 0
SHEET 2 A 5 ARG E 56 HIS E 62 -1
SHEET 3 A 5 ASN E 67 ASP E 75 -1
SHEET 4 A 5 ASN E 115 MET E 120 -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 MN MN E 351 O1B ATP E 355 1555 1555 2.18
LINK MN MN E 351 O HOH E 447 1555 1555 2.15
LINK MN MN E 351 O3G ATP E 355 1555 1555 2.05
LINK MN MN E 351 O HOH E 477 1555 1555 1.85
LINK MN MN E 351 OD2 ASP E 184 1555 1555 2.19
LINK MN MN E 351 OD1 ASP E 184 1555 1555 2.35
LINK MN MN E 352 O2G ATP E 355 1555 1555 2.21
LINK MN MN E 352 O HOH E 635 1555 1555 2.08
LINK MN MN E 352 O2A ATP E 355 1555 1555 1.99
LINK MN MN E 352 OD2 ASP E 184 1555 1555 2.14
LINK MN MN E 352 OD1 ASN E 171 1555 1555 2.09
LINK C TRP E 196 N TPO E 197 1555 1555 1.32
LINK C TPO E 197 N LEU E 198 1555 1555 1.30
LINK C VAL E 337 N SEP E 338 1555 1555 1.32
LINK C SEP E 338 N ILE E 339 1555 1555 1.33
SITE 1 AC4 5 HIS E 87 ARG E 165 LYS E 189 THR E 195
SITE 2 AC4 5 HOH E 450
SITE 1 AC5 2 ASN E 340 HOH E 588
SITE 1 AC1 4 ASP E 184 ATP E 355 HOH E 447 HOH E 477
SITE 1 AC2 4 ASN E 171 ASP E 184 ATP E 355 HOH E 635
SITE 1 AC3 26 THR E 51 GLY E 52 SER E 53 PHE E 54
SITE 2 AC3 26 GLY E 55 VAL E 57 ALA E 70 LYS E 72
SITE 3 AC3 26 VAL E 104 GLU E 121 VAL E 123 GLU E 127
SITE 4 AC3 26 LYS E 168 GLU E 170 ASN E 171 LEU E 173
SITE 5 AC3 26 THR E 183 ASP E 184 PHE E 327 MN E 351
SITE 6 AC3 26 MN E 352 HOH E 447 HOH E 477 HOH E 635
SITE 7 AC3 26 ARG I 18 ALA I 21
CRYST1 73.580 76.280 80.580 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 0.013591 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013110 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012410 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
