spacer
spacer

PDBsum entry 1bqi

Go to PDB code: 
Top Page protein ligands links
Hydrolase PDB id
1bqi
Jmol
Contents
Protein chain
212 a.a.
Ligands
SBA
Waters ×42
HEADER    HYDROLASE                               16-AUG-98   1BQI
TITLE     USE OF PAPAIN AS A MODEL FOR THE STRUCTURE-BASED DESIGN OF
TITLE    2 CATHEPSIN K INHIBITORS. CRYSTAL STRUCTURES OF TWO PAPAIN
TITLE    3 INHIBITOR COMPLEXES DEMONSTRATE BINDING TO S'-SUBSITES.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PAPAIN;
COMPND   3 CHAIN: A;
COMPND   4 OTHER_DETAILS: METHOXYMETHYLKETONE BOUND NON-COVALENTLY IN
COMPND   5 S'-SUBSITE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CARICA PAPAYA;
SOURCE   3 ORGANISM_COMMON: PAPAYA;
SOURCE   4 ORGANISM_TAXID: 3649
KEYWDS    HYDROLASE, SULFHYDRYL PROTEINASE, PAPAIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.M.LALONDE,B.ZHAO,W.W.SMITH,C.A.JANSON,R.L.DESJARLAIS,
AUTHOR   2 T.A.TOMASZEK,T.J.CARR,S.K.THOMPSON,D.S.YAMASHITA,D.F.VEBER,
AUTHOR   3 S.S.ABDEL-MEQUID
REVDAT   3   24-FEB-09 1BQI    1       VERSN
REVDAT   2   01-APR-03 1BQI    1       JRNL
REVDAT   1   16-AUG-99 1BQI    0
JRNL        AUTH   J.M.LALONDE,B.ZHAO,W.W.SMITH,C.A.JANSON,
JRNL        AUTH 2 R.L.DESJARLAIS,T.A.TOMASZEK,T.J.CARR,S.K.THOMPSON,
JRNL        AUTH 3 H.J.OH,D.S.YAMASHITA,D.F.VEBER,S.S.ABDEL-MEGUID
JRNL        TITL   USE OF PAPAIN AS A MODEL FOR THE STRUCTURE-BASED
JRNL        TITL 2 DESIGN OF CATHEPSIN K INHIBITORS: CRYSTAL
JRNL        TITL 3 STRUCTURES OF TWO PAPAIN-INHIBITOR COMPLEXES
JRNL        TITL 4 DEMONSTRATE BINDING TO S'-SUBSITES.
JRNL        REF    J.MED.CHEM.                   V.  41  4567 1998
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   9804696
JRNL        DOI    10.1021/JM980249F
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 80.0
REMARK   3   NUMBER OF REFLECTIONS             : 11372
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.217
REMARK   3   FREE R VALUE                     : 0.306
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.300
REMARK   3   FREE R VALUE TEST SET COUNT      : 1174
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.61
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 53.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 649
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830
REMARK   3   BIN FREE R VALUE                    : 0.3100
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.20
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 47
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            : 1633
REMARK   3   NUCLEIC ACID ATOMS       : NULL
REMARK   3   HETEROGEN ATOMS          : 30
REMARK   3   SOLVENT ATOMS            : 42
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.40
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) : 0.011
REMARK   3   BOND ANGLES            (DEGREES) : 1.59
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.85
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.44
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP RESTRAINED
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  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : TOPHCSDX.PR
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: DISORDERED SIDE-CHAINS HAVE THEIR
REMARK   3  OCCUPANCIES SET TO ZERO IN THE ENTRY, RESIDUES 59, 73, 77, 98,
REMARK   3  145
REMARK   4
REMARK   4 1BQI 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        : JUN-95
REMARK 200  TEMPERATURE           (KELVIN) : 287
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : SIEMENS
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : MONOCHROMATOR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200  DATA SCALING SOFTWARE          : XENGEN
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11412
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : 0.13700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1PIP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 63.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       50.50000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.49500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.50000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.49500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ARG A   59   CG    CD    NE    CZ    NH1   NH2
REMARK 480     GLN A   73   CD    OE1   NE2
REMARK 480     GLN A   77   CG    CD    OE1   NE2
REMARK 480     ARG A   98   CD    NE    CZ    NH1   NH2
REMARK 480     ARG A  145   CD    NE    CZ    NH1   NH2
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    ARG A  59   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A  93   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A  98   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PRO A  15      157.38    -47.43
REMARK 500    ASN A  64       57.41   -115.23
REMARK 500    VAL A  75        6.36    -66.25
REMARK 500    GLN A  77      -77.07    -71.46
REMARK 500    TYR A  78      -84.12    -75.83
REMARK 500    PRO A  87      159.83    -47.77
REMARK 500    CYS A  95       78.28    -64.26
REMARK 500    ARG A  96       35.47    -75.85
REMARK 500    SER A  97      -81.35    -62.21
REMARK 500    GLU A  99        0.24    -62.44
REMARK 500    TYR A 144      162.01    -48.74
REMARK 500    ARG A 145       25.58   -169.76
REMARK 500    ASP A 158      -69.30   -134.08
REMARK 500    SER A 176       57.76   -105.02
REMARK 500    CYS A 200       -0.87     59.06
REMARK 500    LEU A 202      -11.41    -40.19
REMARK 500    SER A 205      117.48   -162.84
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         0.27    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SBA A 300
DBREF  1BQI A    1   212  UNP    P00784   PAPA1_CARPA    134    345
SEQADV 1BQI GLN A   47  UNP  P00784    GLU   180 CONFLICT
SEQADV 1BQI GLN A  118  UNP  P00784    GLU   251 CONFLICT
SEQADV 1BQI 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    SBA  A 300      29
HETNAM     SBA CARBOBENZYLOXY-(L)-LEUCINYL-(L)LEUCINYL
HETNAM   2 SBA  METHOXYMETHYLKETONE
FORMUL   2  SBA    C22 H36 N2 O5
FORMUL   3  HOH   *42(H2 O)
HELIX    1   1 TRP A    7  LYS A   10  5                                   4
HELIX    2   2 CYS A   25  ARG A   41  1                                  17
HELIX    3   3 GLU A   50  CYS A   56  1                                   7
HELIX    4   4 PRO A   68  GLN A   77  1                                  10
HELIX    5   5 ARG A   98  LYS A  100  5                                   3
HELIX    6   6 ALA A  120  ILE A  125  1                                   6
HELIX    7   7 LYS A  139  LEU A  143  1                                   5
HELIX    8   8 VAL A  199  GLY A  201  5                                   3
SHEET    1   A 2 GLY A 109  VAL A 113  0
SHEET    2   A 2 SER A 206  VAL A 210 -1  N  VAL A 210   O  GLY A 109
SHEET    1   B 4 VAL A 130  VAL A 133  0
SHEET    2   B 4 ALA A 160  GLY A 167 -1  N  ALA A 163   O  VAL A 130
SHEET    3   B 4 TYR A 170  LYS A 174 -1  N  LYS A 174   O  ALA A 162
SHEET    4   B 4 TYR A 186  LYS A 190 -1  N  ILE A 189   O  ILE A 171
SSBOND   1 CYS A   22    CYS A   63                          1555   1555  2.04
SSBOND   2 CYS A   56    CYS A   95                          1555   1555  2.05
SSBOND   3 CYS A  153    CYS A  200                          1555   1555  2.03
CISPEP   1 GLY A  151    PRO A  152          0        -0.48
SITE     1 CAT  3 CYS A  25  HIS A 159  ASN A 175
SITE     1 AC1  5 GLN A 142  TRP A 177  GLY A 180  TRP A 181
SITE     2 AC1  5 HOH A 511
CRYST1  101.000   50.990   62.480  90.00  99.60  90.00 C 1 2 1       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      0.009901  0.000000  0.001675        0.00000
SCALE2      0.000000  0.019612  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016232        0.00000
      
PROCHECK
Go to PROCHECK summary
 References