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PDBsum entry 6pad

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Hydrolase/hydrolase inhibitor PDB id
6pad
Jmol
Contents
Protein chain
212 a.a.
Ligands
0PC
Waters ×30
HEADER    HYDROLASE/HYDROLASE INHIBITOR           01-NOV-76   6PAD
TITLE     BINDING OF CHLOROMETHYL KETONE SUBSTRATE ANALOGUES TO CRYSTALLINE
TITLE    2 PAPAIN
CAVEAT     6PAD    60 ATOM PAIRS RELATED BY CRYSTALLOGRAPHIC SYMMETRY ARE IN
CAVEAT   2 6PAD     CLOSE CONTACT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PAPAIN;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.4.22.2;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CARICA PAPAYA;
SOURCE   3 ORGANISM_COMMON: PAPAYA;
SOURCE   4 ORGANISM_TAXID: 3649;
SOURCE   5 TISSUE: FRUIT LATEX
KEYWDS    SULFHYDRYL PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.DRENTH,K.H.KALK,H.M.SWEN
REVDAT  14   13-JUL-11 6PAD    1       VERSN
REVDAT  13   25-AUG-09 6PAD    1       SOURCE
REVDAT  12   24-FEB-09 6PAD    1       VERSN
REVDAT  11   17-FEB-84 6PAD    1       REMARK
REVDAT  10   30-SEP-83 6PAD    1       REVDAT
REVDAT   9   14-SEP-81 6PAD    1       REMARK
REVDAT   8   31-DEC-80 6PAD    1       REMARK
REVDAT   7   30-DEC-77 6PAD    1       REMARK
REVDAT   6   01-NOV-77 6PAD    1       COMPND SOURCE AUTHOR REMARK
REVDAT   6 2                   1       FORMUL SSBOND
REVDAT   5   27-SEP-77 6PAD    1       SEQRES
REVDAT   4   23-AUG-77 6PAD    3       ATOM
REVDAT   3   13-JUN-77 6PAD    1       REMARK
REVDAT   2   28-APR-77 6PAD    1       REMARK
REVDAT   1   12-APR-77 6PAD    0
SPRSDE     12-APR-77 6PAD      7PAP
JRNL        AUTH   J.DRENTH,K.H.KALK,H.M.SWEN
JRNL        TITL   BINDING OF CHLOROMETHYL KETONE SUBSTRATE ANALOGUES TO
JRNL        TITL 2 CRYSTALLINE PAPAIN.
JRNL        REF    BIOCHEMISTRY                  V.  15  3731 1976
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   952885
JRNL        DOI    10.1021/BI00662A014
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.DRENTH,J.N.JANSONIUS,R.KOEKOEK,B.G.WOLTHERS
REMARK   1  TITL   THE STRUCTURE OF PAPAIN
REMARK   1  REF    ADV.PROTEIN CHEM.             V.  25    79 1971
REMARK   1  REFN                   ISSN 0065-3233
REMARK   1 REFERENCE 2
REMARK   1  AUTH   J.DRENTH,J.N.JANSONIUS,R.KOEKOEK,L.A.A.SLUYTERMAN,
REMARK   1  AUTH 2 B.G.WOLTHERS
REMARK   1  TITL   THE STRUCTURE OF THE PAPAIN MOLECULE
REMARK   1  REF    PHILOS.TRANS.R.SOC.LONDON,    V. 257   231 1970
REMARK   1  REF  2 SER.B
REMARK   1  REFN                   ISSN 0080-4622
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.DRENTH,J.N.JANSONIUS,R.KOEKOEK,H.M.SWEN,B.G.WOLTHERS
REMARK   1  TITL   STRUCTURE OF PAPAIN
REMARK   1  REF    NATURE                        V. 218   929 1968
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1 REFERENCE 4
REMARK   1  EDIT   R.J.FELDMANN
REMARK   1  REF    ATLAS OF MACROMOLECULAR                276 1976
REMARK   1  REF  2 STRUCTURE ON MICROFICHE
REMARK   1  PUBL   TRACOR JITCO INC.,ROCKVILLE,MD.
REMARK   1  REFN
REMARK   1 REFERENCE 5
REMARK   1  EDIT   M.O.DAYHOFF
REMARK   1  REF    ATLAS OF PROTEIN SEQUENCE     V.   5   121 1972
REMARK   1  REF  2 AND STRUCTURE (DATA SECTION)
REMARK   1  PUBL   NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK   1  REFN
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : NULL
REMARK   3   AUTHORS     : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
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   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) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
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            : 1655
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 27
REMARK   3   SOLVENT ATOMS            : 30
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) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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  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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  THIS DATA SET WAS OBTAINED BY MERGING THE INHIBITOR
REMARK   3  COORDINATES WITH THE REFINED NATIVE PAPAIN COORDINATES
REMARK   3  OF SET 8PAP.  THE CONFORMATION OF RESIDUE CYS 25 IN THIS
REMARK   3  DERIVATIVE STRUCTURE IS NOT THE SAME AS THAT IN THE NATIVE
REMARK   3  ENZYME AND THIS FACT IS REFLECTED IN THE COORDINATES.
REMARK   3  THE COORDINATES OF THE INHIBITOR WERE NOT REFINED.
REMARK   4
REMARK   4 6PAD 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) : 2.800
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   (%): 50.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 285
REMARK 285 THE AXIAL SYSTEM OF THIS COORDINATE SET IS RELATED TO THE
REMARK 285 CRYSTALLOGRAPHIC AXES BY THE FOLLOWING -
REMARK 285      (I) ITS ORIGIN IS DISPLACED BY THE VECTOR
REMARK 285          (11.6,-101.2,-38.55) IN ANGSTROMS.
REMARK 285      (II) ROTATION OF THE OLD AXES BY +178.785 DEGREES
REMARK 285           ABOUT X.
REMARK 285 A PRECISE STATEMENT OF THIS TRANSFORMATION IS CONTAINED
REMARK 285 IN THE SCALE RECORDS BELOW WHICH CAN BE USED TO PRODUCE
REMARK 285 FRACTIONAL CRYSTALLOGRAPHIC COORDINATES FROM THOSE
REMARK 285 STORED HERE.
REMARK 285 THE ENTRY COORDINATES
REMARK 285 ARE NOT PRESENTED IN THE STANDARD CRYSTAL FRAME.
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       22.50023
REMARK 290   SMTRY2   2  0.000000 -0.999085  0.042193       -0.53599
REMARK 290   SMTRY3   2  0.000000  0.043374  0.999085      -25.39487
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  0.999085 -0.042193      -51.24843
REMARK 290   SMTRY3   3  0.000000 -0.043374 -0.999085      -24.29456
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.50023
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      -50.71244
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        1.10032
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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   OH   TYR A   203     O    HOH A   237              1.11
REMARK 500   O    GLN A    19     OH   TYR A    88              1.75
REMARK 500   CZ   TYR A   203     O    HOH A   237              1.91
REMARK 500   O    ALA A    30     OG1  THR A    33              1.93
REMARK 500   OE1  GLN A   135     N    GLY A   154              1.93
REMARK 500   O    GLY A    11     O    HOH A   218              2.02
REMARK 500   CB   GLN A   112     CE2  PHE A   207              2.15
REMARK 500   O    ALA A   136     N    GLY A   138              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   NH2  ARG A    58     C    GLY A   180     4466     0.67
REMARK 500   NH2  ARG A    58     N    TRP A   181     4466     0.79
REMARK 500   CE1  TYR A    94     CD   ARG A   145     4466     0.80
REMARK 500   CZ   TYR A    94     NE   ARG A   145     4466     0.84
REMARK 500   CG   TYR A    94     CB   ARG A   145     4466     1.09
REMARK 500   CA   GLY A   178     O    HOH A   214     4566     1.15
REMARK 500   NE2  GLN A    92     CG2  THR A   179     4466     1.18
REMARK 500   CG   GLN A    92     OG1  THR A   179     4466     1.18
REMARK 500   CZ   TYR A    94     CD   ARG A   145     4466     1.19
REMARK 500   CB   GLN A    92     OG1  THR A   179     4466     1.24
REMARK 500   CE1  TYR A    94     CG   ARG A   145     4466     1.32
REMARK 500   OH   TYR A    94     NE   ARG A   145     4466     1.32
REMARK 500   NE2  GLN A    92     CB   THR A   179     4466     1.37
REMARK 500   CD1  TYR A    94     CB   ARG A   145     4466     1.40
REMARK 500   CD   GLN A    92     OG1  THR A   179     4466     1.40
REMARK 500   CD2  TYR A    94     CB   ARG A   145     4466     1.47
REMARK 500   CD   GLN A    92     N    THR A   179     4466     1.48
REMARK 500   OH   TYR A    94     CZ   ARG A   145     4466     1.50
REMARK 500   CZ   ARG A    58     C    GLY A   180     4466     1.51
REMARK 500   NH2  ARG A    58     O    GLY A   180     4466     1.52
REMARK 500   CG   ARG A    93     OD1  ASN A   184     4466     1.53
REMARK 500   CD   ARG A    98     NH2  ARG A   145     4466     1.57
REMARK 500   NH1  ARG A    58     O    GLY A   178     4466     1.62
REMARK 500   OE1  GLN A    92     N    THR A   179     4466     1.63
REMARK 500   ND2  ASN A    44     NH2  ARG A   111     4565     1.64
REMARK 500   CZ   ARG A    58     N    TRP A   181     4466     1.65
REMARK 500   CD   GLN A    92     CB   THR A   179     4466     1.66
REMARK 500   CD   GLN A    92     CA   THR A   179     4466     1.69
REMARK 500   ND2  ASN A    18     O    ARG A    58     4566     1.69
REMARK 500   OH   TYR A    94     CD   ARG A   145     4466     1.71
REMARK 500   CZ   TYR A    94     CG   ARG A   145     4466     1.72
REMARK 500   CG   GLN A    92     CB   THR A   179     4466     1.74
REMARK 500   CE2  TYR A    94     NE   ARG A   145     4466     1.74
REMARK 500   CG   GLN A    92     C    THR A   179     4466     1.75
REMARK 500   CE1  TYR A    94     NE   ARG A   145     4466     1.78
REMARK 500   N    ARG A    93     O    THR A   179     4466     1.83
REMARK 500   NZ   LYS A   139     O    GLY A   192     2665     1.83
REMARK 500   NE2  GLN A    92     N    THR A   179     4466     1.83
REMARK 500   OH   TYR A    94     NH1  ARG A   145     4466     1.85
REMARK 500   NE2  GLN A    92     OG1  THR A   179     4466     1.85
REMARK 500   NH2  ARG A    58     CA   TRP A   181     4466     1.85
REMARK 500   CD1  TYR A    94     CG   ARG A   145     4466     1.88
REMARK 500   CG   TYR A    94     CA   ARG A   145     4466     1.89
REMARK 500   CG   GLN A    92     CA   THR A   179     4466     1.90
REMARK 500   NE2  GLN A    92     CA   THR A   179     4466     1.95
REMARK 500   CE1  TYR A    94     CB   ARG A   145     4466     1.96
REMARK 500   CE2  TYR A    94     CB   ARG A   145     4466     1.97
REMARK 500   N    GLY A   178     O    HOH A   214     4566     1.97
REMARK 500   O    ASP A    55     O    GLY A   180     4466     1.97
REMARK 500   O    CYS A    95     NE   ARG A   145     4466     2.04
REMARK 500
REMARK 500 THIS ENTRY HAS      60 SYMMETRY CONTACTS
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    TRP A   7   NE1   TRP A   7   CE2    -0.096
REMARK 500    ASN A  18   CG    ASN A  18   OD1     0.155
REMARK 500    TRP A  26   NE1   TRP A  26   CE2    -0.096
REMARK 500    ASN A  44   CG    ASN A  44   OD1     0.155
REMARK 500    ASN A  46   CG    ASN A  46   OD1     0.155
REMARK 500    ASN A  64   CG    ASN A  64   OD1     0.155
REMARK 500    TRP A  69   NE1   TRP A  69   CE2    -0.096
REMARK 500    SER A  70   N     SER A  70   CA      0.225
REMARK 500    ASN A  84   CG    ASN A  84   OD1     0.155
REMARK 500    ASN A 117   CG    ASN A 117   OD1     0.155
REMARK 500    ASN A 127   CG    ASN A 127   OD1     0.154
REMARK 500    PRO A 152   CD    PRO A 152   N      -0.159
REMARK 500    ASN A 155   CG    ASN A 155   OD1     0.157
REMARK 500    ASN A 169   CG    ASN A 169   OD1     0.156
REMARK 500    ASN A 175   CG    ASN A 175   OD1     0.156
REMARK 500    TRP A 177   NE1   TRP A 177   CE2    -0.093
REMARK 500    TRP A 181   NE1   TRP A 181   CE2    -0.092
REMARK 500    ASN A 184   CG    ASN A 184   OD1     0.156
REMARK 500    ASN A 195   CG    ASN A 195   OD1     0.156
REMARK 500    ASN A 212   CG    ASN A 212   OD1     0.156
REMARK 500    ASN A 212   C     ASN A 212   OXT     0.150
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    ILE A   1   N   -  CA  -  C   ANGL. DEV. = -20.8 DEGREES
REMARK 500    ASP A   6   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    CYS A  25   CB  -  CA  -  C   ANGL. DEV. =  17.0 DEGREES
REMARK 500    CYS A  25   CA  -  C   -  O   ANGL. DEV. =  12.8 DEGREES
REMARK 500    ASP A  55   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ASP A  57   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 108   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ASP A 140   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 158   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASN A 169   N   -  CA  -  C   ANGL. DEV. =  17.0 DEGREES
REMARK 500    PHE A 207   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES
REMARK 500    PHE A 207   N   -  CA  -  C   ANGL. DEV. =  22.4 DEGREES
REMARK 500    TYR A 208   N   -  CA  -  C   ANGL. DEV. =  17.3 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    PRO A   2      163.69    -46.63
REMARK 500    PRO A  15      165.40    -46.62
REMARK 500    SER A  21       32.96    -75.32
REMARK 500    CYS A  25      -66.67     -0.01
REMARK 500    TYR A  61       50.44   -109.84
REMARK 500    CYS A  63       57.73    -65.42
REMARK 500    ASN A  64       67.34    139.01
REMARK 500    TYR A  78      -82.79   -100.01
REMARK 500    TYR A  86       42.85   -176.22
REMARK 500    PRO A  87      158.68    -46.62
REMARK 500    SER A  97      -75.46    -30.77
REMARK 500    GLN A 114      109.40    -53.81
REMARK 500    PRO A 115      162.79    -46.59
REMARK 500    ASN A 117      104.16   -163.88
REMARK 500    GLN A 128      142.48    166.57
REMARK 500    PRO A 129      166.42    -46.60
REMARK 500    LEU A 134     -179.01    170.51
REMARK 500    ALA A 137       -4.41    -47.73
REMARK 500    ASP A 158       15.09   -169.91
REMARK 500    VAL A 161     -158.43   -142.01
REMARK 500    GLU A 183       71.95   -109.40
REMARK 500    ASN A 184       36.87     73.65
REMARK 500    THR A 193      -24.79   -148.37
REMARK 500    ASN A 195       96.14    -52.89
REMARK 500    TYR A 208      135.04   -177.86
REMARK 500    PRO A 209     -158.16    -46.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A  59         0.20    SIDE CHAIN
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    ILE A   1        45.1      L          L   OUTSIDE RANGE
REMARK 500    CYS A  25        21.8      L          L   OUTSIDE RANGE
REMARK 500    ASN A 169        24.4      L          L   OUTSIDE RANGE
REMARK 500    PHE A 207        22.1      L          L   OUTSIDE RANGE
REMARK 500    TYR A 208        24.5      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1S)-3-CHLORO-1-
REMARK 630 METHYL-2-OXOPROPYL]-L-PHENYLALANINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630   M RES C SSSEQI
REMARK 630     0PC A   213
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP:    PHQ PHE ALA 0QE
REMARK 630 DETAILS: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET SUBSTRUCTURE OF THIS MOLECULE IS DOUBLY
REMARK 700 BIFURCATED.  IN ORDER TO REPRESENT THIS FEATURE IN THE
REMARK 700 SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. STRANDS 4,5,6
REMARK 700 OF S1A ARE IDENTICAL TO STRANDS 2,3,4 OF S1B.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0PC A 213
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PAD   RELATED DB: PDB
REMARK 900 UNSPECIFIED
REMARK 900 RELATED ID: 2PAD   RELATED DB: PDB
REMARK 900 UNSPECIFIED
REMARK 900 RELATED ID: 4PAD   RELATED DB: PDB
REMARK 900 UNSPECIFIED
REMARK 900 RELATED ID: 5PAD   RELATED DB: PDB
REMARK 900 UNSPECIFIED
DBREF  6PAD A    1   212  UNP    P00784   PAPA_CARPA     134    345
SEQADV 6PAD GLN A   47  UNP  P00784    GLU   180 CONFLICT
SEQADV 6PAD GLN A  118  UNP  P00784    GLU   251 CONFLICT
SEQADV 6PAD GLN A  135  UNP  P00784    GLU   268 CONFLICT
SEQRES   1 A  212  ILE PRO GLU TYR VAL ASP TRP ARG GLN LYS GLY ALA VAL
SEQRES   2 A  212  THR PRO VAL LYS ASN GLN GLY SER CYS GLY SER CYS TRP
SEQRES   3 A  212  ALA PHE SER ALA VAL VAL THR ILE GLU GLY ILE ILE LYS
SEQRES   4 A  212  ILE ARG THR GLY ASN LEU ASN GLN TYR SER GLU GLN GLU
SEQRES   5 A  212  LEU LEU ASP CYS ASP ARG ARG SER TYR GLY CYS ASN GLY
SEQRES   6 A  212  GLY TYR PRO TRP SER ALA LEU GLN LEU VAL ALA GLN TYR
SEQRES   7 A  212  GLY ILE HIS TYR ARG ASN THR TYR PRO TYR GLU GLY VAL
SEQRES   8 A  212  GLN ARG TYR CYS ARG SER ARG GLU LYS GLY PRO TYR ALA
SEQRES   9 A  212  ALA LYS THR ASP GLY VAL ARG GLN VAL GLN PRO TYR ASN
SEQRES  10 A  212  GLN GLY ALA LEU LEU TYR SER ILE ALA ASN GLN PRO VAL
SEQRES  11 A  212  SER VAL VAL LEU GLN ALA ALA GLY LYS ASP PHE GLN LEU
SEQRES  12 A  212  TYR ARG GLY GLY ILE PHE VAL GLY PRO CYS GLY ASN LYS
SEQRES  13 A  212  VAL ASP HIS ALA VAL ALA ALA VAL GLY TYR GLY PRO ASN
SEQRES  14 A  212  TYR ILE LEU ILE LYS ASN SER TRP GLY THR GLY TRP GLY
SEQRES  15 A  212  GLU ASN GLY TYR ILE ARG ILE LYS ARG GLY THR GLY ASN
SEQRES  16 A  212  SER TYR GLY VAL CYS GLY LEU TYR THR SER SER PHE TYR
SEQRES  17 A  212  PRO VAL LYS ASN
HET    0PC  A 213      27
HETNAM     0PC NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1S)-3-CHLORO-1-METHYL-
HETNAM   2 0PC  2-OXOPROPYL]-L-PHENYLALANINAMIDE
HETSYN     0PC ZPACK
FORMUL   2  0PC    C21 H23 CL N2 O4
FORMUL   3  HOH   *30(H2 O)
HELIX    1  H1 SER A   24  GLY A   43  1                                  20
HELIX    2  H2 GLU A   50  ARG A   58  1                                   9
HELIX    3  H3 TYR A   67  TYR A   78  1                                  12
HELIX    4  H4 ASN A  117  GLN A  128  1                                  12
HELIX    5  H5 ALA A  137  LEU A  143  1                                   7
SHEET    1 S1A 7 ARG A 111  GLN A 112  0
SHEET    2 S1A 7 SER A 206  TYR A 208 -1  N  TYR A 208   O  ARG A 111
SHEET    3 S1A 7 VAL A 130  SER A 131 -1  N  SER A 131   O  PHE A 207
SHEET    4 S1A 7 ALA A 162  GLY A 167 -1  N  ALA A 163   O  VAL A 130
SHEET    5 S1A 7 ASN A 169  ASN A 175 -1  N  LYS A 174   O  ALA A 162
SHEET    6 S1A 7 GLY A 185  ARG A 191 -1  N  ILE A 187   O  ILE A 173
SHEET    7 S1A 7 GLU A 183  GLU A 183 -1  N  GLU A 183   O  TYR A 186
SHEET    1 S1B 5 VAL A   5  TRP A   7  0
SHEET    2 S1B 5 ALA A 162  GLY A 167 -1  N  TYR A 166   O  VAL A   5
SHEET    3 S1B 5 ASN A 169  ASN A 175 -1  N  LEU A 172   O  GLY A 165
SHEET    4 S1B 5 GLY A 185  ARG A 191 -1  N  ILE A 189   O  ILE A 171
SHEET    5 S1B 5 PHE A 149  PHE A 149  1  N  PHE A 149   O  ARG A 188
SSBOND   1 CYS A   22    CYS A   63                          1555   1555  2.07
SSBOND   2 CYS A   56    CYS A   95                          1555   1555  1.69
SSBOND   3 CYS A  153    CYS A  200                          1555   1555  2.06
LINK         SG  CYS A  25                 CM  0PC A 213     1555   1555  1.70
CISPEP   1 GLY A  151    PRO A  152          0       -12.60
SITE     1 AC1 12 GLN A  19  GLY A  23  SER A  24  CYS A  25
SITE     2 AC1 12 TRP A  26  TYR A  61  GLY A  65  GLY A  66
SITE     3 AC1 12 TYR A  67  VAL A 157  ASP A 158  HIS A 159
CRYST1   45.000  104.300   50.800  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      0.022222  0.000000  0.000000        0.25778
SCALE2      0.000000 -0.009855  0.000208        0.96204
SCALE3      0.000000 -0.000427 -0.019680        0.80185
      
PROCHECK
Go to PROCHECK summary
 References