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PDBsum entry 1ctp

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Top Page protein ligands Protein-protein interface(s) links
Transferase/transferase inhibitor PDB id
1ctp
Jmol
Contents
Protein chains
333 a.a. *
18 a.a. *
Ligands
MYR
Waters ×2
* Residue conservation analysis
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       08-APR-93   1CTP
TITLE     STRUCTURE OF THE MAMMALIAN CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN
TITLE    2 KINASE AND AN INHIBITOR PEPTIDE DISPLAYS AN OPEN CONFORMATION
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: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM;
COMPND   8 CHAIN: I;
COMPND   9 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   3 ORGANISM_COMMON: PIG;
SOURCE   4 ORGANISM_TAXID: 9823;
SOURCE   5 MOL_ID: 2;
SOURCE   6 SYNTHETIC: YES;
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   8 ORGANISM_COMMON: HUMAN;
SOURCE   9 ORGANISM_TAXID: 9606
KEYWDS    TRANSFERASE(PHOSPHOTRANSFERASE), TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS   2 COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.KARLSSON,J.ZHENG,N.H.XUONG,S.S.TAYLOR,J.M.SOWADSKI
REVDAT   4   18-JUL-12 1CTP    1       HEADER SITE   SOURCE VERSN
REVDAT   3   24-FEB-09 1CTP    1       VERSN
REVDAT   2   01-APR-03 1CTP    1       JRNL
REVDAT   1   31-JAN-94 1CTP    0
JRNL        AUTH   R.KARLSSON,J.ZHENG,N.XUONG,S.S.TAYLOR,J.M.SOWADSKI
JRNL        TITL   STRUCTURE OF THE MAMMALIAN CATALYTIC SUBUNIT OF
JRNL        TITL 2 CAMP-DEPENDENT PROTEIN KINASE AND AN INHIBITOR PEPTIDE
JRNL        TITL 3 DISPLAYS AN OPEN CONFORMATION.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   381 1993
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   15299513
JRNL        DOI    10.1107/S0907444993002306
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.ZHENG,D.R.KNIGHTON,N.-H.XUONG,L.F.T.EYCK,R.KARLSSON,
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 A MGATP 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,S.M.BELL,J.ZHENG,L.F.T.EYCK,N.-H.XUONG,
REMARK   1  AUTH 2 S.S.TAYLOR,J.M.SOWADSKI
REMARK   1  TITL   2.0 ANGSTROMS 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    ACTA CRYSTALLOGR.,SECT.D      V.  49   357 1993
REMARK   1  REFN                   ISSN 0907-4449
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.H.ZHENG,E.A.TRAFNY,D.R.KNIGHTON,N.-H.XUONG,S.S.TAYLOR,
REMARK   1  AUTH 2 L.F.T.EYCK,J.M.SOWADSKI
REMARK   1  TITL   2.2 ANGSTROMS REFINED CRYSTAL-STRUCTURE OF THE CATALYTIC
REMARK   1  TITL 2 SUBUNIT OF CAMP-DEPENDENT PROTEIN-KINASE COMPLEXED WITH
REMARK   1  TITL 3 MNATP AND A PEPTIDE INHIBITOR
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   362 1993
REMARK   1  REFN                   ISSN 0907-4449
REMARK   1 REFERENCE 4
REMARK   1  AUTH   D.R.KNIGHTON,J.ZHENG,L.F.T.EYCK,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 5
REMARK   1  AUTH   D.R.KNIGHTON,J.ZHENG,L.F.T.EYCK,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 6
REMARK   1  AUTH   L.W.SLICE,S.S.TAYLOR
REMARK   1  TITL   EXPRESSION OF THE CATALYTIC SUBUNIT OF CAMP-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.    2.90 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) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
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) : 0.190
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            : 2720
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 2
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) : 0.022 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 4.300 ; 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  THE TEMPERATURE FACTOR OF OH TYR E 108 IS ABOUT 30 UNITS
REMARK   3  GREATER THAN THOSE OF THE ATOMS IN THE PHENYL RING.
REMARK   4
REMARK   4 1CTP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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        : 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   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   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 74.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2
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       5555   Z,X,Y
REMARK 290       6555   Z+1/2,-X+1/2,-Y
REMARK 290       7555   -Z+1/2,-X,Y+1/2
REMARK 290       8555   -Z,X+1/2,-Y+1/2
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z+1/2,-X+1/2
REMARK 290      11555   Y+1/2,-Z+1/2,-X
REMARK 290      12555   -Y+1/2,-Z,X+1/2
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4
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       85.75000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.75000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       85.75000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.75000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       85.75000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       85.75000
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       85.75000
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       85.75000
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       85.75000
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       85.75000
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       85.75000
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       85.75000
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       85.75000
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000      128.62500
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       42.87500
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       42.87500
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000      128.62500
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000      128.62500
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      128.62500
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       42.87500
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       42.87500
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      128.62500
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       42.87500
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000      128.62500
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       42.87500
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000      128.62500
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       42.87500
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       42.87500
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       42.87500
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000      128.62500
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       42.87500
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000      128.62500
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000      128.62500
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000      128.62500
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       42.87500
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       42.87500
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000      128.62500
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000      128.62500
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       42.87500
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       42.87500
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       42.87500
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       42.87500
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000      128.62500
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       42.87500
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000      128.62500
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       42.87500
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000      128.62500
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000      128.62500
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000      128.62500
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: TETRAMERIC
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 350   BIOMT1   2 -1.000000  0.000000  0.000000       42.87500
REMARK 350   BIOMT2   2  0.000000  0.000000  1.000000      -42.87500
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000       42.87500
REMARK 400
REMARK 400 COMPOUND
REMARK 400 N-TERMINAL IS MYRISTOYLATED BUT ONLY THE LAST 10 ATOMS OF
REMARK 400 THE ALKANE CHAIN WERE LOCATED.  THE MYRISTOYLATE GROUP IS
REMARK 400 PRESENTED ON *HETATM* RECORDS AT THE END OF THE CHAIN.
REMARK 400
REMARK 400 THERE ARE NINE MUTATIONS BETWEEN THE MOUSE RECOMBINANT FORM
REMARK 400 OF THE ENZYME (PDB ENTRY 2CPK) AND THE PORCINE ENZYME GIVEN
REMARK 400 IN THIS ENTRY.  THE MUTATIONS ARE:
REMARK 400
REMARK 400      PORCINE ENZYME    -    MOUSE RECOMBINANT ENZYME
REMARK 400
REMARK 400      ASN  32                THR  32
REMARK 400      ALA  34                SER  34
REMARK 400      HIS  39                GLN  39
REMARK 400      GLU  44                ASP  44
REMARK 400      THR  65                SER  65
REMARK 400      PHE  69                TYR  69
REMARK 400      TYR 108                PHE 108
REMARK 400      PRO 124                ALA 124
REMARK 400      SER 348                THR 348
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     PHE E   318
REMARK 465     LYS E   319
REMARK 465     GLY E   320
REMARK 465     PRO E   321
REMARK 465     GLY E   322
REMARK 465     ASP E   323
REMARK 465     THR E   324
REMARK 465     SER E   325
REMARK 465     ASN E   326
REMARK 465     ILE E   339
REMARK 465     ASN E   340
REMARK 465     HIS I    23
REMARK 465     ASP I    24
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     LYS E   7    CG   CD   CE   NZ
REMARK 470     LYS E   8    CG   CD   CE   NZ
REMARK 470     GLU E  11    CG   CD   OE1  OE2
REMARK 470     GLN E  12    CG   CD   OE1  NE2
REMARK 470     GLU E  13    CG   CD   OE1  OE2
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     ASN E  32    CG   OD1  ND2
REMARK 470     ASN E  36    CG   OD1  ND2
REMARK 470     HIS E  39    CG   ND1  CD2  CE1  NE2
REMARK 470     ASP E  41    CG   OD1  OD2
REMARK 470     GLU E  44    CG   CD   OE1  OE2
REMARK 470     ARG E  45    CG   CD   NE   CZ   NH1  NH2
REMARK 470     PHE E  54    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU E  64    CG   CD   OE1  OE2
REMARK 470     LYS E  78    CG   CD   CE   NZ
REMARK 470     LYS E  81    CG   CD   CE   NZ
REMARK 470     LYS E  83    CG   CD   CE   NZ
REMARK 470     LYS E 105    CG   CD   CE   NZ
REMARK 470     LYS E 192    CG   CD   CE   NZ
REMARK 470     LYS E 213    CG   CD   CE   NZ
REMARK 470     LYS E 217    CG   CD   CE   NZ
REMARK 470     ASP E 241    CG   OD1  OD2
REMARK 470     GLN E 242    CG   CD   OE1  NE2
REMARK 470     ILE E 244    CG1  CG2  CD1
REMARK 470     GLU E 248    CG   CD   OE1  OE2
REMARK 470     LYS E 254    CG   CD   CE   NZ
REMARK 470     ARG E 256    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     LYS E 295    CG   CD   CE   NZ
REMARK 470     ASP E 329    CG   OD1  OD2
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     ILE E 335    CG1  CG2  CD1
REMARK 470     ARG E 336    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL E 337    CG1  CG2
REMARK 470     SER E 338    CB   OG
REMARK 470     LYS E 342    CG   CD   CE   NZ
REMARK 470     LYS E 345    CG   CD   CE   NZ
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   OE2  GLU E   140     OG   SER E   262              1.95
REMARK 500   NE1  TRP E   222     O    HOH E   402              2.00
REMARK 500   NH2  ARG E   194     O    LYS E   213              2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   OE2  GLU E    86     CZ3  TRP E   196    24555     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  86   CD    GLU E  86   OE2     0.150
REMARK 500    GLU E  91   CD    GLU E  91   OE2     0.087
REMARK 500    GLU E 121   CD    GLU E 121   OE1     0.107
REMARK 500    GLU E 127   CD    GLU E 127   OE2     0.109
REMARK 500    GLU E 140   CD    GLU E 140   OE1     0.077
REMARK 500    GLU E 311   CD    GLU E 311   OE1     0.100
REMARK 500    GLU E 332   CD    GLU E 332   OE2     0.076
REMARK 500    GLU E 349   CD    GLU E 349   OE2     0.138
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    VAL E  15   CA  -  CB  -  CG2 ANGL. DEV. = -18.2 DEGREES
REMARK 500    ASN E  32   CB  -  CA  -  C   ANGL. DEV. =  15.7 DEGREES
REMARK 500    ALA E  34   CB  -  CA  -  C   ANGL. DEV. =  12.8 DEGREES
REMARK 500    THR E  37   CA  -  CB  -  CG2 ANGL. DEV. = -16.3 DEGREES
REMARK 500    ASP E  41   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES
REMARK 500    ARG E  56   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    MET E  58   CA  -  CB  -  CG  ANGL. DEV. = -11.0 DEGREES
REMARK 500    MET E  58   CG  -  SD  -  CE  ANGL. DEV. = -10.1 DEGREES
REMARK 500    LYS E  63   O   -  C   -  N   ANGL. DEV. =  -9.7 DEGREES
REMARK 500    ASN E  67   CA  -  CB  -  CG  ANGL. DEV. = -16.7 DEGREES
REMARK 500    LEU E  89   CB  -  CG  -  CD1 ANGL. DEV. = -11.9 DEGREES
REMARK 500    ARG E  93   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    VAL E  98   CA  -  CB  -  CG2 ANGL. DEV. = -14.2 DEGREES
REMARK 500    VAL E 104   CA  -  CB  -  CG1 ANGL. DEV. = -11.5 DEGREES
REMARK 500    LEU E 103   O   -  C   -  N   ANGL. DEV. = -16.8 DEGREES
REMARK 500    TYR E 108   CB  -  CG  -  CD2 ANGL. DEV. =   7.8 DEGREES
REMARK 500    TYR E 108   CB  -  CG  -  CD1 ANGL. DEV. =  -9.0 DEGREES
REMARK 500    SER E 109   N   -  CA  -  CB  ANGL. DEV. = -11.9 DEGREES
REMARK 500    MET E 128   CG  -  SD  -  CE  ANGL. DEV. = -12.3 DEGREES
REMARK 500    ARG E 133   CG  -  CD  -  NE  ANGL. DEV. = -15.4 DEGREES
REMARK 500    ARG E 133   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG E 134   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG E 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG E 137   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ARG E 137   NE  -  CZ  -  NH2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ILE E 163   CA  -  CB  -  CG1 ANGL. DEV. =  12.6 DEGREES
REMARK 500    TYR E 164   O   -  C   -  N   ANGL. DEV. = -11.1 DEGREES
REMARK 500    ARG E 165   C   -  N   -  CA  ANGL. DEV. = -18.9 DEGREES
REMARK 500    ASP E 166   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP E 166   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ASP E 175   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES
REMARK 500    GLN E 177   N   -  CA  -  CB  ANGL. DEV. = -15.2 DEGREES
REMARK 500    ASP E 184   N   -  CA  -  CB  ANGL. DEV. = -17.5 DEGREES
REMARK 500    ASP E 184   CB  -  CG  -  OD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500    ARG E 194   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ARG E 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.7 DEGREES
REMARK 500    ILE E 209   O   -  C   -  N   ANGL. DEV. = -10.6 DEGREES
REMARK 500    LYS E 213   N   -  CA  -  CB  ANGL. DEV. = -13.9 DEGREES
REMARK 500    VAL E 219   CA  -  CB  -  CG2 ANGL. DEV. =   9.1 DEGREES
REMARK 500    PHE E 238   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    PRO E 237   O   -  C   -  N   ANGL. DEV. = -10.6 DEGREES
REMARK 500    TYR E 247   CB  -  CG  -  CD2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    TYR E 247   CB  -  CG  -  CD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    SER E 252   CB  -  CA  -  C   ANGL. DEV. = -22.5 DEGREES
REMARK 500    SER E 262   CB  -  CA  -  C   ANGL. DEV. = -16.5 DEGREES
REMARK 500    SER E 262   N   -  CA  -  CB  ANGL. DEV. = -10.4 DEGREES
REMARK 500    SER E 262   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES
REMARK 500    SER E 262   CA  -  C   -  O   ANGL. DEV. = -12.8 DEGREES
REMARK 500    PHE E 261   O   -  C   -  N   ANGL. DEV. = -13.5 DEGREES
REMARK 500    SER E 263   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      75 ANGLE DEVIATIONS.
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    LYS E   8      -76.28    -15.61
REMARK 500    PRO E  33     -150.35    -57.28
REMARK 500    GLN E  35      -94.02   -105.31
REMARK 500    ALA E  38     -156.65   -111.87
REMARK 500    LEU E  40      -80.14    -34.17
REMARK 500    ASP E  41      -20.20    -28.31
REMARK 500    THR E  51     -153.90   -150.20
REMARK 500    SER E  53     -179.76    -58.67
REMARK 500    PHE E  54      -55.34     68.63
REMARK 500    THR E  65      -33.30    115.22
REMARK 500    LYS E  83       70.04     45.64
REMARK 500    PRO E 101      -32.67    -39.14
REMARK 500    ASP E 161       17.84     53.07
REMARK 500    ASP E 166       63.69   -158.49
REMARK 500    ASP E 184      106.10     58.20
REMARK 500    ASN E 216     -169.74   -164.23
REMARK 500    GLN E 242       94.76    116.53
REMARK 500    ILE E 244      -60.37    -29.31
REMARK 500    PHE E 261     -175.32    -58.14
REMARK 500    SER E 262     -169.70   -104.12
REMARK 500    SER E 263      -71.84    -90.10
REMARK 500    ASP E 264      -43.44    -26.92
REMARK 500    LEU E 273       34.96    -84.86
REMARK 500    LEU E 277      -38.63    -25.23
REMARK 500    ASN E 286      -25.56    138.51
REMARK 500    ARG E 308       27.07     46.64
REMARK 500    ASP E 329     -163.96    -79.54
REMARK 500    GLU E 332     -175.74    -37.22
REMARK 500    GLU E 333     -145.73   -170.68
REMARK 500    VAL E 337       83.15     23.55
REMARK 500    LYS E 342      101.41    157.12
REMARK 500    THR I   6      149.70    173.28
REMARK 500    ARG I  15       36.88    -77.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    SER E  14        23.7      L          L   OUTSIDE RANGE
REMARK 500    ASP E  25        21.6      L          L   OUTSIDE RANGE
REMARK 500    LYS E  28        19.3      L          L   OUTSIDE RANGE
REMARK 500    PRO E  33        21.7      L          L   OUTSIDE RANGE
REMARK 500    ASN E  36        23.0      L          L   OUTSIDE RANGE
REMARK 500    LYS E  76        23.0      L          L   OUTSIDE RANGE
REMARK 500    LYS E  78        23.1      L          L   OUTSIDE RANGE
REMARK 500    VAL E  79        20.6      L          L   OUTSIDE RANGE
REMARK 500    LYS E  81        24.5      L          L   OUTSIDE RANGE
REMARK 500    GLU E  86        23.4      L          L   OUTSIDE RANGE
REMARK 500    ASN E 113        19.9      L          L   OUTSIDE RANGE
REMARK 500    ASP E 175        21.0      L          L   OUTSIDE RANGE
REMARK 500    GLN E 176        21.9      L          L   OUTSIDE RANGE
REMARK 500    ILE E 180        22.9      L          L   OUTSIDE RANGE
REMARK 500    SER E 212        23.1      L          L   OUTSIDE RANGE
REMARK 500    ALA E 218        21.8      L          L   OUTSIDE RANGE
REMARK 500    SER E 262        48.2      L          L   OUTSIDE RANGE
REMARK 500    SER E 263        46.9      L          L   OUTSIDE RANGE
REMARK 500    ARG E 270        18.2      L          L   OUTSIDE RANGE
REMARK 500    PHE E 327        17.8      L          L   OUTSIDE RANGE
REMARK 500    GLU E 332        23.2      L          L   OUTSIDE RANGE
REMARK 500    LYS E 342        15.7      L          L   OUTSIDE RANGE
REMARK 500    ARG I  15        19.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     MYR E    0
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR E 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT
REMARK 800  PROTEIN KINASE INHIBITOR, ALPHA FORM
DBREF  1CTP E    1   350  UNP    P36887   KAPCA_PIG        1    350
DBREF  1CTP I    5    24  UNP    P61925   IPKA_HUMAN       6     25
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 ASN PRO ALA GLN ASN THR ALA HIS
SEQRES   4 E  350  LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR GLY
SEQRES   5 E  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU THR
SEQRES   6 E  350  GLY ASN HIS PHE 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 TYR SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES  10 E  350  MET VAL MET GLU TYR VAL PRO 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 SER
SEQRES  27 E  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE
SEQRES   1 I   20  THR THR TYI ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES   2 I   20  ARG ARG ASN ALA ILE HIS ASP
MODRES 1CTP TPO E  197  THR  PHOSPHOTHREONINE
MODRES 1CTP TYI I    7  TYR  3,5-DIIODOTYROSINE
HET    TPO  E 197      11
HET    TYI  I   7      14
HET    MYR  E   0      10
HETNAM     TPO PHOSPHOTHREONINE
HETNAM     TYI 3,5-DIIODOTYROSINE
HETNAM     MYR MYRISTIC ACID
HETSYN     TPO PHOSPHONOTHREONINE
FORMUL   1  TPO    C4 H10 N O6 P
FORMUL   2  TYI    C9 H9 I2 N O3
FORMUL   3  MYR    C14 H28 O2
FORMUL   4  HOH   *2(H2 O)
HELIX    1   A GLU E   11  GLU E   31  1                                  21
HELIX    2   B LYS E   76  LYS E   81  1                                   6
HELIX    3   C ILE E   85  ALA E   97  1                                  13
HELIX    4   D MET E  128  ILE E  135  1                                   8
HELIX    5   E GLU E  140  SER E  159  1                                  20
HELIX    6   F ALA E  218  ALA E  233  1                                  16
HELIX    7   G PRO E  243  SER E  252  1                                  10
HELIX    8   H SER E  263  LEU E  272  1                                  10
HELIX    9   I ASN E  289  LYS E  292  1                                   4
HELIX   10  IJ LYS E  295  THR E  299  1                                   5
HELIX   11   J TRP E  302  GLN E  307  1                                   6
HELIX   12  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   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   THR I   6                 N   TYI I   7     1555   1555  1.33
LINK         C   TYI I   7                 N   ALA I   8     1555   1555  1.35
SITE     1 AC1  1 GLU E 155
SITE     1 AC2 20 THR E  51  GLU E 127  PHE E 129  ARG E 133
SITE     2 AC2 20 LYS E 168  PRO E 169  GLU E 170  PHE E 187
SITE     3 AC2 20 GLY E 200  THR E 201  GLU E 203  GLU E 230
SITE     4 AC2 20 TYR E 235  PHE E 239  ALA E 240  ASP E 241
SITE     5 AC2 20 ARG E 256  PHE E 327  ASP E 328  TYR E 330
CRYST1  171.500  171.500  171.500  90.00  90.00  90.00 P 41 3 2     24
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      0.005831  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005831  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005831        0.00000
      
PROCHECK
Go to PROCHECK summary
 References