HEADER TRANSFERASE 28-FEB-02 1L3R
TITLE CRYSTAL STRUCTURE OF A TRANSITION STATE MIMIC OF THE
TITLE 2 CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: E;
COMPND 5 SYNONYM: PKA C-ALPHA;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,
COMPND 10 MUSCLE/BRAIN FORM;
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: RESIDUES 5-24;
COMPND 13 SYNONYM: PKI-ALPHA;
COMPND 14 ENGINEERED: YES;
COMPND 15 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
SOURCE 10 SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN MUS MUSCULUS
SOURCE 11 (MOUSE).
KEYWDS PROTEIN KINASE, PROTEIN-ALF3 COMPLEX, TRANSITION STATE
KEYWDS 2 MIMIC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR MADHUSUDAN,P.AKAMINE,N.-H.XUONG,S.S.TAYLOR
REVDAT 4 24-FEB-09 1L3R 1 VERSN
REVDAT 3 01-APR-03 1L3R 1 JRNL
REVDAT 2 27-MAR-02 1L3R 1 JRNL
REVDAT 1 20-MAR-02 1L3R 0
JRNL AUTH MADHUSUDAN,P.AKAMINE,N.H.XUONG,S.S.TAYLOR
JRNL TITL CRYSTAL STRUCTURE OF A TRANSITION STATE MIMIC OF
JRNL TITL 2 THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN
JRNL TITL 3 KINASE.
JRNL REF NAT.STRUCT.BIOL. V. 9 273 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 11896404
JRNL DOI 10.1038/NSB780
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
REMARK 1 TITL 2 SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED
REMARK 1 TITL 3 WITH A PEPTIDE 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
REMARK 1 TITL 2 SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED
REMARK 1 TITL 3 WITH MNATP AND A 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 1 REFERENCE 3
REMARK 1 AUTH MADHUSUDAN,E.A.TRAFNY,N.H.XUONG,J.A.ADAMS,
REMARK 1 AUTH 2 L.F.TEN EYCK,S.S.TAYLOR,J.M.SOWADSKI
REMARK 1 TITL CAMP-DEPENDENT PROTEIN KINASE: CRYSTALLOGRAFIC
REMARK 1 TITL 2 INSIGHTS INTO SUBSTRATE RECOGNITION AND
REMARK 1 TITL 3 PHOSPHOTRANSFER
REMARK 1 REF PROTEIN SCI. V. 3 176 1994
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 30443
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1819
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE : 0.3170
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 : 2886
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 241
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) : 0.96800
REMARK 3 B22 (A**2) : -10.94100
REMARK 3 B33 (A**2) : 9.97300
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) : 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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.28
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : PHOSPHO_RESI.PARAM
REMARK 3 PARAMETER FILE 3 : DNA-RNA.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L3R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-02.
REMARK 100 THE RCSB ID CODE IS RCSB015617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : 58 CM LONG, PT-COATED, FUSED
REMARK 200 SILICA, VERTICAL FOCUSMIRROR,
REMARK 200 CYCLINDRICALLY BENT TRIANGULAR
REMARK 200 SI(111) ASYMMETRIC CUT,
REMARK 200 HORIZONTAL FOCUS MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30443
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
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) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1JBP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, BICINE, METHANOL, AMMONIUM
REMARK 280 ACETATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
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 36.34000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.27500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.27500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.34000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.85000
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: 3920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 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 SEP E 10
REMARK 465 GLU E 11
REMARK 465 GLN E 12
REMARK 465 GLU E 13
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 ASN E 2 CG OD1 ND2
REMARK 470 SER E 14 OG
REMARK 470 VAL E 15 CG1 CG2
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 LYS E 28 CG CD CE NZ
REMARK 470 GLU E 64 CG CD OE1 OE2
REMARK 470 LYS E 105 CG CD CE NZ
REMARK 470 LYS E 285 CG CD CE NZ
REMARK 470 ASN E 286 CG OD1 ND2
REMARK 470 LYS E 309 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 334 CG CD OE1 OE2
REMARK 470 ILE E 339 CG1 CG2 CD1
REMARK 470 LYS E 345 CG CD CE NZ
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 ASP E 41 3.94 -68.91
REMARK 500 ILE E 46 -60.36 -102.22
REMARK 500 ASP E 166 44.24 -148.51
REMARK 500 ASP E 184 81.19 57.18
REMARK 500 LEU E 273 48.28 -86.11
REMARK 500 LYS E 319 33.72 -72.39
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 MG E 392 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP E 381 O2A
REMARK 620 2 HOH E 578 O 88.2
REMARK 620 3 ADP E 381 O3B 81.4 93.2
REMARK 620 4 AF3 E 400 AL 131.6 98.0 50.4
REMARK 620 5 AF3 E 400 F1 167.8 89.7 86.7 37.1
REMARK 620 6 ASP E 184 OD2 87.2 174.0 82.4 82.3 94.1
REMARK 620 7 ASN E 171 OD1 95.2 90.5 175.0 132.4 96.8 93.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 391 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 184 OD2
REMARK 620 2 ADP E 381 O2B 77.3
REMARK 620 3 HOH E 576 O 160.4 96.2
REMARK 620 4 AF3 E 400 F2 96.1 96.7 103.0
REMARK 620 5 HOH E 577 O 93.7 171.0 92.6 83.4
REMARK 620 6 ASP E 184 OD1 57.9 86.5 103.6 152.6 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 E 400 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 166 OD1
REMARK 620 2 SER I 21 OG 42.9
REMARK 620 3 MG E 391 MG 68.7 102.4
REMARK 620 4 ADP E 381 O3B 119.9 162.6 66.5
REMARK 620 5 ASP E 184 OD2 67.6 110.4 40.4 52.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 391
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 392
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 381
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 E 400
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 382
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1APM RELATED DB: PDB
REMARK 900 1APM CONTAINS THE SAME PROTEIN COMPLEX WITH PEPTIDE
REMARK 900 INHIBITOR AND DETERGENT
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 1ATP CONTAINS THE SAME PROTEIN COMPLEXED WITH MNATP AND
REMARK 900 PEPTIDE INHIBITOR
REMARK 900 RELATED ID: 1JBP RELATED DB: PDB
REMARK 900 1JBP CONTAINS THE SAME PROTEIN COMPLEXED WITH ADP AND THE
REMARK 900 SAME PEPTIDE SUBSTRATE
DBREF 1L3R E 1 350 UNP P05132 KAPCA_MOUSE 1 350
DBREF 1L3R I 5 24 UNP P27776 IPKA_MOUSE 5 24
SEQADV 1L3R SEP E 10 UNP P05132 SER 10 MODIFIED RESIDUE
SEQADV 1L3R SEP E 139 UNP P05132 SER 139 MODIFIED RESIDUE
SEQADV 1L3R TPO E 197 UNP P05132 THR 197 MODIFIED RESIDUE
SEQADV 1L3R SEP E 338 UNP P05132 SER 338 MODIFIED RESIDUE
SEQADV 1L3R ALA I 20 UNP P27776 ASN 20 ENGINEERED
SEQADV 1L3R SER I 21 UNP P27776 ALA 21 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 SEP 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 ALA SER ILE HIS ASP
MODRES 1L3R SEP E 139 SER PHOSPHOSERINE
MODRES 1L3R TPO E 197 THR PHOSPHOTHREONINE
MODRES 1L3R SEP E 338 SER PHOSPHOSERINE
HET SEP E 139 10
HET TPO E 197 11
HET SEP E 338 10
HET MG E 391 1
HET MG E 392 1
HET ADP E 381 27
HET AF3 E 400 4
HET MPD E 382 8
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM AF3 ALUMINUM FLUORIDE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
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 MG 2(MG 2+)
FORMUL 5 ADP C10 H15 N5 O10 P2
FORMUL 6 AF3 AL F3
FORMUL 7 MPD C6 H14 O2
FORMUL 8 HOH *233(H2 O)
HELIX 1 1 SER E 14 THR E 32 1 19
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 GLN E 96 1 13
HELIX 5 5 GLU E 127 GLY E 136 1 10
HELIX 6 6 SEP 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 VAL E 288 ASN E 293 1 6
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 THR I 5 SER I 13 1 9
SHEET 1 A 5 PHE E 43 THR E 51 0
SHEET 2 A 5 ARG E 56 HIS E 62 -1 O LEU E 59 N LYS E 47
SHEET 3 A 5 HIS E 68 ASP E 75 -1 O MET E 71 N MET E 58
SHEET 4 A 5 ASN E 115 GLU E 121 -1 O MET E 118 N LYS E 72
SHEET 5 A 5 LEU E 106 LYS E 111 -1 N PHE E 110 O TYR E 117
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 PHE E 138 N SEP E 139 1555 1555 1.33
LINK C SEP E 139 N GLU E 140 1555 1555 1.33
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
LINK O2A ADP E 381 MG MG E 392 1555 1555 1.88
LINK MG MG E 391 OD2 ASP E 184 1555 1555 2.32
LINK MG MG E 391 O2B ADP E 381 1555 1555 2.13
LINK MG MG E 391 O HOH E 576 1555 1555 2.12
LINK MG MG E 391 F2 AF3 E 400 1555 1555 1.97
LINK MG MG E 391 O HOH E 577 1555 1555 2.36
LINK MG MG E 391 OD1 ASP E 184 1555 1555 2.21
LINK MG MG E 392 O HOH E 578 1555 1555 2.18
LINK MG MG E 392 O3B ADP E 381 1555 1555 2.06
LINK MG MG E 392 AL AF3 E 400 1555 1555 2.99
LINK MG MG E 392 F1 AF3 E 400 1555 1555 1.97
LINK MG MG E 392 OD2 ASP E 184 1555 1555 2.00
LINK MG MG E 392 OD1 ASN E 171 1555 1555 2.11
LINK AL AF3 E 400 OD1 ASP E 166 1555 1555 3.61
LINK AL AF3 E 400 OG SER I 21 1555 1555 2.27
LINK AL AF3 E 400 MG MG E 391 1555 1555 3.35
LINK AL AF3 E 400 O3B ADP E 381 1555 1555 2.31
LINK AL AF3 E 400 OD2 ASP E 184 1555 1555 3.37
SITE 1 AC1 5 ASP E 184 ADP E 381 AF3 E 400 HOH E 576
SITE 2 AC1 5 HOH E 577
SITE 1 AC2 5 ASN E 171 ASP E 184 ADP E 381 AF3 E 400
SITE 2 AC2 5 HOH E 578
SITE 1 AC3 25 GLY E 50 GLY E 52 SER E 53 PHE E 54
SITE 2 AC3 25 GLY E 55 VAL E 57 ALA E 70 LYS E 72
SITE 3 AC3 25 VAL E 104 MET E 120 GLU E 121 VAL E 123
SITE 4 AC3 25 GLU E 127 GLU E 170 ASN E 171 LEU E 173
SITE 5 AC3 25 THR E 183 ASP E 184 PHE E 327 MG E 391
SITE 6 AC3 25 MG E 392 AF3 E 400 HOH E 414 HOH E 578
SITE 7 AC3 25 ARG I 18
SITE 1 AC4 13 GLY E 52 SER E 53 PHE E 54 ASP E 166
SITE 2 AC4 13 LYS E 168 ASN E 171 ASP E 184 ADP E 381
SITE 3 AC4 13 MG E 391 MG E 392 HOH E 577 HOH E 578
SITE 4 AC4 13 SER I 21
SITE 1 AC5 5 PHE E 18 LEU E 152 GLU E 155 TYR E 306
SITE 2 AC5 5 HOH E 609
CRYST1 72.680 75.700 80.550 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 0.013759 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013210 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012415 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
