HEADER COMPLEX (PHOSPHOTRANSFERASE/INHIBITOR) 08-JUL-97 1FMO
TITLE CRYSTAL STRUCTURE OF A POLYHISTIDINE-TAGGED RECOMBINANT
TITLE 2 CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE
TITLE 3 COMPLEXED WITH THE PEPTIDE INHIBITOR PKI(5-24) AND
TITLE 4 ADENOSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE;
COMPND 3 CHAIN: E;
COMPND 4 FRAGMENT: CATALYTIC SUBUNIT;
COMPND 5 SYNONYM: CAPK, PKA;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HEAT STABLE RABBIT SKELETAL MUSCLE INHIBITOR
COMPND 10 PROTEIN;
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: RESIDUES 5 - 24;
COMPND 13 SYNONYM: PKI-ALPHA, PKI(5-24);
COMPND 14 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 ORGAN: SKELETAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2
KEYWDS COMPLEX (PHOSPHOTRANSFERASE/INHIBITOR), PHOSPHORYLATION,
KEYWDS 2 POLYHISTIDINE-TAG, PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.NARAYANA,S.COX,S.SHALTIEL,S.S.TAYLOR,N.-H.XUONG
REVDAT 3 24-FEB-09 1FMO 1 VERSN
REVDAT 2 01-APR-03 1FMO 1 JRNL
REVDAT 1 14-JAN-98 1FMO 0
JRNL AUTH N.NARAYANA,S.COX,S.SHALTIEL,S.S.TAYLOR,N.XUONG
JRNL TITL CRYSTAL STRUCTURE OF A POLYHISTIDINE-TAGGED
JRNL TITL 2 RECOMBINANT CATALYTIC SUBUNIT OF CAMP-DEPENDENT
JRNL TITL 3 PROTEIN KINASE COMPLEXED WITH THE PEPTIDE
JRNL TITL 4 INHIBITOR PKI(5-24) AND ADENOSINE.
JRNL REF BIOCHEMISTRY V. 36 4438 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9109651
JRNL DOI 10.1021/BI961947+
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.NARAYANA,S.COX,N.H.XUONG,L.F.TEN EYCK,S.S.TAYLOR
REMARK 1 TITL A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF
REMARK 1 TITL 2 CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE
REMARK 1 TITL 3 FURTHER DEFINES CONFORMATIONAL FLEXIBILITY
REMARK 1 REF STRUCTURE V. 5 921 1997
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.ZHENG,D.R.KNIGHTON,L.F.TEN EYCK,R.KARLSSON,
REMARK 1 AUTH 2 N.H.XUONG,S.S.TAYLOR,J.M.SOWADSKI
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF
REMARK 1 TITL 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MGATP
REMARK 1 TITL 3 AND PEPTIDE INHIBITOR
REMARK 1 REF BIOCHEMISTRY V. 32 2154 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.W.HERBERG,S.M.BELL,S.S.TAYLOR
REMARK 1 TITL EXPRESSION OF THE CATALYTIC SUBUNIT OF
REMARK 1 TITL 2 CAMP-DEPENDENT PROTEIN KINASE IN ESCHERICHIA COLI:
REMARK 1 TITL 3 MULTIPLE ISOZYMES REFLECT DIFFERENT
REMARK 1 TITL 4 PHOSPHORYLATION STATES
REMARK 1 REF PROTEIN ENG. V. 6 771 1993
REMARK 1 REFN ISSN 0269-2139
REMARK 1 REFERENCE 4
REMARK 1 AUTH D.R.KNIGHTON,J.H.ZHENG,L.F.TEN EYCK,V.A.ASHFORD,
REMARK 1 AUTH 2 N.H.XUONG,S.S.TAYLOR,J.M.SOWADSKI
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF
REMARK 1 TITL 2 CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN
REMARK 1 TITL 3 KINASE
REMARK 1 REF SCIENCE V. 253 407 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 5
REMARK 1 AUTH D.R.KNIGHTON,J.H.ZHENG,L.F.TEN EYCK,N.H.XUONG,
REMARK 1 AUTH 2 S.S.TAYLOR,J.M.SOWADSKI
REMARK 1 TITL STRUCTURE OF A PEPTIDE INHIBITOR BOUND TO THE
REMARK 1 TITL 2 CATALYTIC SUBUNIT OF CYCLIC ADENOSINE
REMARK 1 TITL 3 MONOPHOSPHATE-DEPENDENT PROTEIN KINASE
REMARK 1 REF SCIENCE V. 253 414 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT V. 5-E, X-PLOR 3.1
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)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.0
REMARK 3 NUMBER OF REFLECTIONS : 19980
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) : 0.182
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 : 2949
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 90
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 24.000
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.012 ; 1.300 ; 3044
REMARK 3 BOND ANGLES (DEGREES) : 2.500 ; 2.800 ; 4088
REMARK 3 TORSION ANGLES (DEGREES) : 2.000 ; 0.000 ; 1786
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.010 ; 2.200 ; 78
REMARK 3 GENERAL PLANES (A) : 0.010 ; 10.000; 431
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; 3058
REMARK 3 NON-BONDED CONTACTS (A) : 0.040 ; 18.000; 14
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.45
REMARK 3 BSOL : 167.10
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 1FMO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-94
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
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
REMARK 200 DATA SCALING SOFTWARE : UCSD
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21679
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1APM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ORTHORHOMBIC CRYSTALS OF THE
REMARK 280 TERNARY COMPLEX, COMPRISED OF MOUSE HIS6-RC SUBUNIT, PKI (5-
REMARK 280 24) AND ADENOSINE, WERE GROWN BY THE HANGING-DROP VAPOUR
REMARK 280 DIFFUSION METHOD USING 2-METHYL-2,4-PENTANEDIOL (MPD) AS THE
REMARK 280 PRECIPITATING AGENT. THE MOTHER-LIQUOR CONTAINED PROTEIN AT A
REMARK 280 CONCENTRATION OF 0.25 MM IN 100 MM BICINE BUFFER AT PH 8.0,
REMARK 280 0.75 MM PKI(5-24), 4 MM ADENOSINE AND 4% MPD. THE RESERVOIR
REMARK 280 SOLUTION WAS MADE UP OF 20% MPD IN 100 MM BICINE BUFFER (PH
REMARK 280 8.0). X-RAY DIFFRACTION QUALITY CRYSTALS (0.2 X 0.15 X 0.8
REMARK 280 MM3) WERE GROWN AT 4 C IN APPROXIMATELY 4 - 6 WEEKS., VAPOR
REMARK 280 DIFFUSION - HANGING DROP, TEMPERATURE 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 36.54000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.24500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.22000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.24500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.54000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.22000
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: 2800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 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 0.068
REMARK 500 GLU E 17 CD GLU E 17 OE1 0.076
REMARK 500 GLU E 24 CD GLU E 24 OE2 0.083
REMARK 500 GLU E 64 CD GLU E 64 OE1 0.073
REMARK 500 GLU E 86 CD GLU E 86 OE2 0.072
REMARK 500 GLU E 155 CD GLU E 155 OE2 0.068
REMARK 500 GLU E 311 CD GLU E 311 OE2 0.100
REMARK 500 GLU E 332 CD GLU E 332 OE1 0.076
REMARK 500 GLU E 333 CD GLU E 333 OE1 0.072
REMARK 500 GLU E 334 CD GLU E 334 OE1 0.075
REMARK 500 GLU E 341 CD GLU E 341 OE2 0.073
REMARK 500 GLU E 349 CD GLU E 349 OE1 0.097
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 25 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP E 44 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP E 44 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP E 112 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG E 165 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP E 166 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP E 220 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 241 CB - CG - OD1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ASP E 241 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 264 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 264 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP E 290 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP E 301 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 301 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP E 328 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP E 328 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP I 24 CB - CG - OD2 ANGL. DEV. = -5.7 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 ASN E 36 69.49 19.43
REMARK 500 ALA E 38 -162.98 -175.54
REMARK 500 LEU E 40 -39.21 -36.72
REMARK 500 ILE E 46 -82.98 -104.43
REMARK 500 LYS E 63 -60.39 -27.34
REMARK 500 ASN E 99 101.97 -169.25
REMARK 500 PHE E 110 163.23 176.10
REMARK 500 ALA E 148 -41.29 -29.44
REMARK 500 ARG E 165 -3.64 74.44
REMARK 500 ASP E 166 35.05 -142.32
REMARK 500 LYS E 168 144.14 -172.21
REMARK 500 ASP E 184 101.15 67.95
REMARK 500 LEU E 205 134.32 -39.48
REMARK 500 ASN E 216 -159.23 -124.35
REMARK 500 ALA E 240 -174.07 -170.24
REMARK 500 LEU E 273 32.74 -95.46
REMARK 500 LYS E 279 -14.13 -141.10
REMARK 500 ASN E 289 -9.96 -48.08
REMARK 500 GLU E 311 95.21 -69.56
REMARK 500 ARG I 15 57.95 -112.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 417 DISTANCE = 7.85 ANGSTROMS
REMARK 525 HOH E 429 DISTANCE = 5.73 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN E 351
DBREF 1FMO E 1 350 UNP P05132 KAPCA_MOUSE 1 350
DBREF 1FMO I 5 24 UNP P61926 IPKA_RABIT 5 24
SEQADV 1FMO TPO E 197 UNP P05132 THR 197 MODIFIED RESIDUE
SEQADV 1FMO SEP E 338 UNP P05132 SER 338 MODIFIED RESIDUE
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 1FMO TPO E 197 THR PHOSPHOTHREONINE
MODRES 1FMO SEP E 338 SER PHOSPHOSERINE
HET TPO E 197 11
HET SEP E 338 10
HET ADN E 351 19
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM ADN ADENOSINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 ADN C10 H13 N5 O4
FORMUL 4 HOH *90(H2 O)
HELIX 1 1 SER E 14 GLU E 31 1 18
HELIX 2 2 LEU E 40 GLN E 42 5 3
HELIX 3 3 LYS E 76 LYS E 81 1 6
HELIX 4 4 ILE E 85 ALA E 97 1 13
HELIX 5 5 MET E 128 ILE E 135 1 8
HELIX 6 6 GLU E 140 LEU E 160 1 21
HELIX 7 7 PRO E 169 ASN E 171 5 3
HELIX 8 8 PRO E 207 ILE E 210 1 4
HELIX 9 9 LYS E 217 ALA E 233 5 17
HELIX 10 10 PRO E 243 SER E 252 1 10
HELIX 11 11 SER E 263 LEU E 272 1 10
HELIX 12 12 GLY E 287 LYS E 292 5 6
HELIX 13 13 LYS E 295 PHE E 297 5 3
HELIX 14 14 TRP E 302 GLN E 307 1 6
HELIX 15 15 THR I 6 ALA I 12 1 7
SHEET 1 A 5 PHE E 43 ARG E 45 0
SHEET 2 A 5 GLY E 55 HIS E 62 -1 N LYS E 61 O ASP E 44
SHEET 3 A 5 ASN E 67 ASP E 75 -1 N ILE E 73 O ARG E 56
SHEET 4 A 5 ASN E 115 GLU E 121 -1 N MET E 120 O ALA E 70
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 172 ILE E 174 0
SHEET 2 B 2 ILE E 180 VAL E 182 -1 N GLN E 181 O LEU E 173
SHEET 1 C 2 THR E 48 THR E 51 0
SHEET 2 C 2 ARG E 56 MET E 58 -1 N VAL E 57 O LEU E 49
LINK N TPO E 197 C TRP E 196 1555 1555 1.31
LINK C TPO E 197 N LEU E 198 1555 1555 1.31
LINK N SEP E 338 C VAL E 337 1555 1555 1.32
LINK C SEP E 338 N ILE E 339 1555 1555 1.31
SITE 1 AC1 13 LEU E 49 VAL E 57 ALA E 70 GLU E 121
SITE 2 AC1 13 VAL E 123 GLU E 127 GLU E 170 ASN E 171
SITE 3 AC1 13 LEU E 173 THR E 183 PHE E 327 HOH E 375
SITE 4 AC1 13 ARG I 18
CRYST1 73.080 78.440 80.490 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 0.013684 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012749 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012424 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
