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PDBsum entry 1ppn

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Hydrolase(sulfhydryl proteinase) PDB id
1ppn
Jmol
Contents
Protein chain
212 a.a.
Ligands
__O
MOH
Waters ×226
HEADER    HYDROLASE(SULFHYDRYL PROTEINASE)        25-OCT-91   1PPN
TITLE     STRUCTURE OF MONOCLINIC PAPAIN AT 1.60 ANGSTROMS RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PAPAIN;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CARICA PAPAYA;
SOURCE   3 ORGANISM_COMMON: PAPAYA;
SOURCE   4 ORGANISM_TAXID: 3649
KEYWDS    HYDROLASE(SULFHYDRYL PROTEINASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.W.PICKERSGILL,G.W.HARRIS,E.GARMAN
REVDAT   3   25-AUG-09 1PPN    1       SOURCE
REVDAT   2   24-FEB-09 1PPN    1       VERSN
REVDAT   1   31-JAN-94 1PPN    0
JRNL        AUTH   R.W.PICKERSGILL,G.W.HARRIS,E.GARMAN
JRNL        TITL   STRUCTURE OF MONOCLINIC PAPAIN AT 1.60 ANGSTROMS
JRNL        TITL 2 RESOLUTION
JRNL        REF    ACTA CRYSTALLOGR.,SECT.B      V.  48    59 1992
JRNL        REFN                   ISSN 0108-7681
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   G.W.HARRIS,R.W.PICKERSGILL,B.HOWLIN,D.S.MOSS
REMARK   1  TITL   THE SEGMENTED ANISOTROPIC REFINEMENT OF MONOCLINIC
REMARK   1  TITL 2 PAPAIN BY THE APPLICATION OF THE RIGID-BODY TLS
REMARK   1  TITL 3 MODEL AND COMPARISON TO BOVINE RIBONUCLEASE A
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.B      V.  48    67 1992
REMARK   1  REFN                   ISSN 0108-7681
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 20172
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 + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.160
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  FIT/AGREEMENT OF MODEL WITH ALL DATA.
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            : 1659
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 228
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS:
REMARK   3  A SECOND SITE FOR ASN 169 WAS IDENTIFIED AND REFINED,
REMARK   3  THE OCCUPANCY OF THE TWO SITES REFINED TO 0.47 AND 0.53.
REMARK   3
REMARK   3  THE SG ATOM OF ACTIVE SITE RESIDUE CYS 25 HAS ANOTHER
REMARK   3  ATOM BOUND TO IT, TREATED AS AN OXYGEN IN THE REFINEMENT.
REMARK   4
REMARK   4 1PPN 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        : 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   (%): 44.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       25.35000
REMARK 290   SMTRY3   2  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: MONOMERIC
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   O    HOH A   359     O    HOH A   440              1.55
REMARK 500   CE2  TYR A    61     O    HOH A   416              1.82
REMARK 500   CG2  THR A    85     O    HOH A   376              1.91
REMARK 500   OD1  ASN A   169     O    HOH A   387              2.03
REMARK 500   O    HOH A   346     O    HOH A   403              2.10
REMARK 500   OE2  GLU A    52     OG   SER A    97              2.19
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    ASN A 169   CG    ASN A 169   OD1     0.156
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    TYR A   4   CB  -  CG  -  CD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TYR A   4   CG  -  CD1 -  CE1 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    TRP A   7   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ARG A   8   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG A   8   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.5 DEGREES
REMARK 500    VAL A  13   CA  -  CB  -  CG1 ANGL. DEV. =  11.0 DEGREES
REMARK 500    GLY A  23   O   -  C   -  N   ANGL. DEV. =  11.7 DEGREES
REMARK 500    LEU A  54   CB  -  CA  -  C   ANGL. DEV. =  13.2 DEGREES
REMARK 500    ASP A  55   CB  -  CG  -  OD1 ANGL. DEV. =   9.6 DEGREES
REMARK 500    ASP A  55   CB  -  CG  -  OD2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A  59   CD  -  NE  -  CZ  ANGL. DEV. =  13.2 DEGREES
REMARK 500    ARG A  59   NH1 -  CZ  -  NH2 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    ARG A  59   NE  -  CZ  -  NH2 ANGL. DEV. =   6.6 DEGREES
REMARK 500    TYR A  61   CB  -  CG  -  CD1 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ASN A  64   CB  -  CA  -  C   ANGL. DEV. = -16.0 DEGREES
REMARK 500    TYR A  67   CB  -  CG  -  CD2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TYR A  67   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    TYR A  67   CG  -  CD2 -  CE2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    SER A  70   N   -  CA  -  CB  ANGL. DEV. =  10.7 DEGREES
REMARK 500    ALA A  76   N   -  CA  -  CB  ANGL. DEV. =   9.2 DEGREES
REMARK 500    TYR A  78   CG  -  CD2 -  CE2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    HIS A  81   CE1 -  NE2 -  CD2 ANGL. DEV. =   4.4 DEGREES
REMARK 500    TYR A  86   CB  -  CG  -  CD1 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ARG A  93   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES
REMARK 500    TYR A  94   CB  -  CG  -  CD2 ANGL. DEV. =   4.5 DEGREES
REMARK 500    TYR A  94   CB  -  CG  -  CD1 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG A  96   CB  -  CA  -  C   ANGL. DEV. =  14.3 DEGREES
REMARK 500    ARG A  96   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    TYR A 103   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ASP A 108   CB  -  CG  -  OD2 ANGL. DEV. =   9.8 DEGREES
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    TYR A 116   CD1 -  CG  -  CD2 ANGL. DEV. =   7.2 DEGREES
REMARK 500    TYR A 116   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    TYR A 116   CG  -  CD1 -  CE1 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    TYR A 116   CZ  -  CE2 -  CD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TYR A 123   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    LYS A 139   N   -  CA  -  CB  ANGL. DEV. =  13.6 DEGREES
REMARK 500    ASP A 140   CB  -  CG  -  OD1 ANGL. DEV. =  -9.8 DEGREES
REMARK 500    ASP A 140   CB  -  CG  -  OD2 ANGL. DEV. =  12.8 DEGREES
REMARK 500    TYR A 144   CB  -  CG  -  CD1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ASN A 169   N   -  CA  -  CB  ANGL. DEV. =  11.3 DEGREES
REMARK 500    TYR A 170   CB  -  CG  -  CD2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TYR A 170   CG  -  CD1 -  CE1 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    TYR A 186   CD1 -  CG  -  CD2 ANGL. DEV. =   7.2 DEGREES
REMARK 500    TYR A 186   CB  -  CG  -  CD1 ANGL. DEV. =  -4.9 DEGREES
REMARK 500    TYR A 186   CG  -  CD1 -  CE1 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ARG A 191   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    ARG A 191   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES
REMARK 500    GLY A 194   C   -  N   -  CA  ANGL. DEV. =  12.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      55 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    ARG A  58      -49.92    -22.01
REMARK 500    TYR A  78      -71.08   -115.78
REMARK 500    ARG A  93     -162.95   -112.12
REMARK 500    ASP A 158       -1.96   -146.84
REMARK 500    SER A 205      111.43   -161.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASP A   57     ARG A   58                  146.65
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  41         0.26    SIDE_CHAIN
REMARK 500    ARG A  58         0.25    SIDE_CHAIN
REMARK 500    ARG A  59         0.10    SIDE_CHAIN
REMARK 500    ARG A  98         0.21    SIDE_CHAIN
REMARK 500    ARG A 111         0.16    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    LYS A  17        -10.04
REMARK 500    HIS A  81        -13.78
REMARK 500    ARG A 188         10.32
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 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: (11X,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     LEU A  54        23.9      L          L   OUTSIDE RANGE
REMARK 500     ARG A  58       -23.2      L          D   OUTSIDE RANGE
REMARK 500     ARG A  59        24.0      L          L   OUTSIDE RANGE
REMARK 500     ARG A  96         3.5      L          D   EXPECTING SP3
REMARK 500     GLU A  99        22.0      L          L   OUTSIDE RANGE
REMARK 500     LYS A 139        20.8      L          L   OUTSIDE RANGE
REMARK 500     ASN A 155        16.9      L          L   OUTSIDE RANGE
REMARK 500     ASN A 169        24.5      L          L   OUTSIDE RANGE
REMARK 500     TYR A 203        23.4      L          L   OUTSIDE RANGE
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 A 295        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH A 312        DISTANCE =  5.58 ANGSTROMS
REMARK 525    HOH A 338        DISTANCE =  8.20 ANGSTROMS
REMARK 525    HOH A 347        DISTANCE =  6.33 ANGSTROMS
REMARK 525    HOH A 356        DISTANCE =  5.61 ANGSTROMS
REMARK 525    HOH A 357        DISTANCE =  9.48 ANGSTROMS
REMARK 525    HOH A 399        DISTANCE =  7.63 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O A 213
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 456
DBREF  1PPN A    1   212  UNP    P00784   PAPA_CARPA     134    345
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 GLU 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  GLU GLY ALA LEU LEU TYR SER ILE ALA ASN GLN PRO VAL
SEQRES  11 A  212  SER VAL VAL LEU GLU 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      O  A 213       1
HET    MOH  A 456       2
HETNAM       O OXYGEN ATOM
HETNAM     MOH METHANOL
FORMUL   2    O    O
FORMUL   3  MOH    C H4 O
FORMUL   4  HOH   *226(H2 O)
HELIX    1   1 SER A   24  GLY A   43  1                                  20
HELIX    2   2 SER A   49  ASP A   57  1                                   9
HELIX    3   3 TYR A   61  CYS A   63  5                                   3
HELIX    4   4 TYR A   67  TYR A   78  1                                  12
HELIX    5   5 SER A   97  GLY A  101  5                                   5
HELIX    6   6 ASN A  117  GLN A  128  1                                  12
HELIX    7   7 GLY A  138  LEU A  143  1                                   6
HELIX    8   8 GLY A  198  LEU A  202  5                                   5
SHEET    1   A 3 VAL A 130  LEU A 134  0
SHEET    2   A 3 HIS A 159  GLY A 167 -1  O  HIS A 159   N  LEU A 134
SHEET    3   A 3 VAL A   5  ASP A   6 -1  N  VAL A   5   O  TYR A 166
SHEET    1   B 5 VAL A 130  LEU A 134  0
SHEET    2   B 5 HIS A 159  GLY A 167 -1  O  HIS A 159   N  LEU A 134
SHEET    3   B 5 TYR A 170  LYS A 174 -1  O  TYR A 170   N  GLY A 167
SHEET    4   B 5 TYR A 186  LYS A 190 -1  O  ILE A 187   N  ILE A 173
SHEET    5   B 5 ILE A 148  PHE A 149  1  N  PHE A 149   O  ARG A 188
SHEET    1   C 2 GLY A 109  VAL A 113  0
SHEET    2   C 2 SER A 206  VAL A 210 -1  O  SER A 206   N  VAL A 113
SSBOND   1 CYS A   22    CYS A   63                          1555   1555  2.01
SSBOND   2 CYS A   56    CYS A   95                          1555   1555  2.05
SSBOND   3 CYS A  153    CYS A  200                          1555   1555  2.09
LINK         SG  CYS A  25                 O     O A 213     1555   1555  1.70
CISPEP   1 GLY A  151    PRO A  152          0        -0.41
SITE     1 AC1  2 GLY A  23  CYS A  25
SITE     1 AC2  4 VAL A  16  GLY A 178  THR A 179  HOH A 231
CRYST1   65.700   50.700   31.500  90.00  98.40  90.00 P 1 21 1      2
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      0.015221  0.000000  0.002248        0.00000
SCALE2      0.000000  0.019724  0.000000        0.00000
SCALE3      0.000000  0.000000  0.032090        0.00000
      
PROCHECK
Go to PROCHECK summary
 References