spacer
spacer

PDBsum entry 8pap

Go to PDB code: 
Top Page protein links
Hydrolase (sulfhydryl proteinase) PDB id
8pap
Jmol
Contents
Protein chain
212 a.a.
Waters ×30
HEADER    HYDROLASE (SULFHYDRYL PROTEINASE)       01-NOV-76   8PAP
OBSLTE     15-JAN-87 8PAP      9PAP
TITLE     STRUCTURE OF PAPAIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE:;
COMPND   3 CHAIN: NULL;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1
KEYWDS    HYDROLASE (SULFHYDRYL PROTEINASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.DRENTH,J.N.JANSONIUS,R.KOEKOEK,H.M.SWEN,B.G.WOLTHERS
REVDAT   8   15-JAN-87 8PAP    3       OBSLTE
REVDAT   7   17-FEB-84 8PAP    1       REMARK
REVDAT   6   30-SEP-83 8PAP    1       REVDAT
REVDAT   5   14-SEP-81 8PAP    1       REMARK
REVDAT   4   31-DEC-80 8PAP    1       REMARK
REVDAT   3   30-DEC-77 8PAP    1       REMARK
REVDAT   2   01-NOV-77 8PAP    1       COMPND SOURCE AUTHOR REMARK
REVDAT   2 2                   1       FORMUL SSBOND
REVDAT   1   02-DEC-76 8PAP    0
SPRSDE     02-DEC-76 8PAP      1PAP
JRNL        AUTH   J.DRENTH,J.N.JANSONIUS,R.KOEKOEK,H.M.SWEN,
JRNL        AUTH 2 B.G.WOLTHERS
JRNL        TITL   STRUCTURE OF PAPAIN
JRNL        REF    NATURE                        V. 218   929 1968
JRNL        REFN   ASTM NATUAS  UK ISSN 0028-0836
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   ASTM APCHA2  US 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   ASTM PTRBAE  UK ISSN 0080-4622
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.DRENTH,K.H.KALK,H.M.SWEN
REMARK   1  TITL   BINDING OF CHLOROMETHYL KETONE SUBSTRATE ANALOGUES
REMARK   1  TITL 2 TO CRYSTALLINE PAPAIN
REMARK   1  REF    BIOCHEMISTRY                  V.  15  3731 1976
REMARK   1  REFN   ASTM BICHAW  US ISSN 0006-2960
REMARK   1 REFERENCE 4
REMARK   1  EDIT   R.J.FELDMANN
REMARK   1  REF    ATLAS OF MACROMOLECULAR                244 1976
REMARK   1  REF  2 STRUCTURE ON MICROFICHE
REMARK   1  PUBL   TRACOR JITCO INC.,ROCKVILLE,MD.
REMARK   1  REFN                   ISBN 0-917934-01-6
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
REMARK   1  PUBL 2 SPRING,MD.
REMARK   1  REFN                   ISBN 0-912466-02-2
REMARK   2
REMARK   2 RESOLUTION. NULL 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) : NULL
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          : 0
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: NULL
REMARK   4
REMARK   4 8PAP COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK   5
REMARK   5 8PAP THE SHEET SUBSTRUCTURE OF THIS MOLECULE IS DOUBLY 8PAP
REMARK   5 BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE 8PAP
REMARK   5 SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. STRANDS 4,5,6
REMARK   5 8PAP OF S1A ARE IDENTICAL TO STRANDS 2,3,4 OF S1B. 8PAP
REMARK   6
REMARK   6 8PAP THE AXIAL SYSTEM OF THIS COORDINATE SET IS RELATED TO
REMARK   6 THE 8PAP CRYSTALLOGRAPHIC AXES BY THE FOLLOWING - 8PAP (I)
REMARK   6 ITS ORIGIN IS DISPLACED BY THE VECTOR 8PAP (11.6,-101.2,-
REMARK   6 38.55) IN ANGSTROMS. 8PAP (II) ROTATION OF THE OLD AXES BY
REMARK   6 +178.785 DEGREES 8PAP ABOUT X. 8PAP A PRECISE STATEMENT OF
REMARK   6 THIS TRANSFORMATION IS CONTAINED 8PAP IN THE SCALE RECORDS
REMARK   6 BELOW WHICH CAN BE USED TO PRODUCE 8PAP FRACTIONAL
REMARK   6 CRYSTALLOGRAPHIC COORDINATES FROM THOSE 8PAP STORED HERE.
REMARK   6 8PAP
REMARK   7
REMARK   7 8PAP CORRECTION. REFORMAT HEADER INFORMATION TO MEET NEW
REMARK   7 8PAP SPECIFICATIONS. 8PAP ADD FORMUL RECORDS. 8PAP ADD
REMARK   7 SSBOND RECORDS. 8PAP 01-NOV-77. 8PAP
REMARK   8
REMARK   8 8PAP CORRECTION. CHANGE CODEN ON REFN RECORD OF REFERENCE
REMARK   8 3. 8PAP 30-DEC-77. 8PAP
REMARK   9
REMARK   9 8PAP CORRECTION. STANDARDIZE FORMAT OF REMARKS 2 AND 3.
REMARK   9 8PAP 31-DEC-80. 8PAP
REMARK  10
REMARK  10 8PAP CORRECTION. CORRECT ASTM CODE FOR REFERENCE 2. 14-SEP-
REMARK  10 81. 8PAP
REMARK  11
REMARK  11 8PAP CORRECTION. INSERT REVDAT RECORDS. 30-SEP-83. 8PAP
REMARK  12
REMARK  12 8PAP CORRECTION. CORRECT JOURNAL NAME FOR REFERENCES 3 AND
REMARK  12 4. 8PAP 17-FEB-84. 8PAP
REMARK  13
REMARK  13 8PAP CORRECTION. THIS ENTRY IS OBSOLETE. 15-JAN-87. 8PAP
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   (%): 51.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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   1/2-X,-Y,1/2+Z
REMARK 290       3555   -X,1/2+Y,1/2-Z
REMARK 290       4555   1/2+X,1/2-Y,-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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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     GLN     9    OE1   NE2
REMARK 470     ASN    18    OD1   ND2
REMARK 470     GLN    19    OE1   NE2
REMARK 470     ASN    44    OD1   ND2
REMARK 470     ASN    46    OD1   ND2
REMARK 470     GLN    47    OE1   NE2
REMARK 470     GLN    51    OE1   NE2
REMARK 470     ASN    64    OD1   ND2
REMARK 470     GLN    73    OE1   NE2
REMARK 470     GLN    77    OE1   NE2
REMARK 470     ASN    84    OD1   ND2
REMARK 470     GLN    92    OE1   NE2
REMARK 470     GLN   112    OE1   NE2
REMARK 470     GLN   114    OE1   NE2
REMARK 470     ASN   117    OD1   ND2
REMARK 470     GLN   118    OE1   NE2
REMARK 470     ASN   127    OD1   ND2
REMARK 470     GLN   128    OE1   NE2
REMARK 470     GLN   135    OE1   NE2
REMARK 470     GLN   142    OE1   NE2
REMARK 470     ASN   155    OD1   ND2
REMARK 470     ASN   169    OD1   ND2
REMARK 470     ASN   175    OD1   ND2
REMARK 470     ASN   184    OD1   ND2
REMARK 470     ASN   195    OD1   ND2
REMARK 470     ASN   212    OD1   ND2
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
REMARK 500   OH   TYR     203     O    HOH      25              1.11
REMARK 500   O    GLN      19     OH   TYR      88              1.75
REMARK 500   CZ   TYR     203     O    HOH      25              1.91
REMARK 500   O    ALA      30     OG1  THR      33              1.93
REMARK 500  AE1   GLN     135     N    GLY     154              1.93
REMARK 500   O    GLY      11     O    HOH       6              2.02
REMARK 500   CB   GLN     112     CE2  PHE     207              2.15
REMARK 500   O    ALA     136     N    GLY     138              2.16
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      58     C    GLY     180     4466     0.67
REMARK 500   NH2  ARG      58     N    TRP     181     4466     0.79
REMARK 500   CE1  TYR      94     CD   ARG     145     4466     0.80
REMARK 500   CZ   TYR      94     NE   ARG     145     4466     0.84
REMARK 500   CG   TYR      94     CB   ARG     145     4466     1.09
REMARK 500   CA   GLY     178     O    HOH       2     4566     1.15
REMARK 500   CG   GLN      92     OG1  THR     179     4466     1.18
REMARK 500  AE2   GLN      92     CG2  THR     179     4466     1.18
REMARK 500   CZ   TYR      94     CD   ARG     145     4466     1.19
REMARK 500   CB   GLN      92     OG1  THR     179     4466     1.24
REMARK 500   CE1  TYR      94     CG   ARG     145     4466     1.32
REMARK 500   OH   TYR      94     NE   ARG     145     4466     1.32
REMARK 500  AE2   GLN      92     CB   THR     179     4466     1.37
REMARK 500   CD   GLN      92     OG1  THR     179     4466     1.40
REMARK 500   CD1  TYR      94     CB   ARG     145     4466     1.40
REMARK 500   CD2  TYR      94     CB   ARG     145     4466     1.47
REMARK 500   CD   GLN      92     N    THR     179     4466     1.48
REMARK 500   OH   TYR      94     CZ   ARG     145     4466     1.50
REMARK 500   CZ   ARG      58     C    GLY     180     4466     1.51
REMARK 500   NH2  ARG      58     O    GLY     180     4466     1.52
REMARK 500   CD   ARG      98     NH2  ARG     145     4466     1.57
REMARK 500   NH1  ARG      58     O    GLY     178     4466     1.62
REMARK 500  AE1   GLN      92     N    THR     179     4466     1.63
REMARK 500   CZ   ARG      58     N    TRP     181     4466     1.65
REMARK 500   CD   GLN      92     CB   THR     179     4466     1.66
REMARK 500   CD   GLN      92     CA   THR     179     4466     1.69
REMARK 500   OH   TYR      94     CD   ARG     145     4466     1.71
REMARK 500   CZ   TYR      94     CG   ARG     145     4466     1.72
REMARK 500   CG   GLN      92     CB   THR     179     4466     1.74
REMARK 500   CE2  TYR      94     NE   ARG     145     4466     1.74
REMARK 500   CG   GLN      92     C    THR     179     4466     1.75
REMARK 500   CE1  TYR      94     NE   ARG     145     4466     1.78
REMARK 500  AE2   GLN      92     N    THR     179     4466     1.83
REMARK 500   N    ARG      93     O    THR     179     4466     1.83
REMARK 500   NZ   LYS     139     O    GLY     192     2665     1.83
REMARK 500   NH2  ARG      58     CA   TRP     181     4466     1.85
REMARK 500  AE2   GLN      92     OG1  THR     179     4466     1.85
REMARK 500   OH   TYR      94     NH1  ARG     145     4466     1.85
REMARK 500   CD1  TYR      94     CG   ARG     145     4466     1.88
REMARK 500   CG   TYR      94     CA   ARG     145     4466     1.89
REMARK 500   CG   GLN      92     CA   THR     179     4466     1.90
REMARK 500  AE2   GLN      92     CA   THR     179     4466     1.95
REMARK 500   CE1  TYR      94     CB   ARG     145     4466     1.96
REMARK 500   O    ASP      55     O    GLY     180     4466     1.97
REMARK 500   CE2  TYR      94     CB   ARG     145     4466     1.97
REMARK 500   N    GLY     178     O    HOH       2     4566     1.97
REMARK 500   O    CYS      95     NE   ARG     145     4466     2.04
REMARK 500   CG   GLN      92     O    THR     179     4466     2.07
REMARK 500   CZ   TYR      94     CZ   ARG     145     4466     2.09
REMARK 500   NH2  ARG      58     CA   GLY     180     4466     2.10
REMARK 500   C    GLN      92     O    THR     179     4466     2.13
REMARK 500   CZ   TYR      94     CB   ARG     145     4466     2.16
REMARK 500   CZ   ARG      58     O    GLY     180     4466     2.17
REMARK 500   NH1  ARG      58     N    TRP     181     4466     2.17
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    SER    70   N     SER    70   CA     0.226
REMARK 500    PRO   152   CD    PRO   152   N     -0.158
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ILE     1   N   -  CA  -  C   ANGL. DEV. =-21.0 DEGREES
REMARK 500    ASN   169   N   -  CA  -  C   ANGL. DEV. = 16.8 DEGREES
REMARK 500    PHE   207   N   -  CA  -  C   ANGL. DEV. = 22.2 DEGREES
REMARK 500    TYR   208   N   -  CA  -  C   ANGL. DEV. = 17.1 DEGREES
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  M RES CSSEQI        PSI       PHI
REMARK 500    ASN    64       67.34    139.01
SEQRES   1    212  ILE PRO GLU TYR VAL ASP TRP ARG GLN LYS GLY ALA VAL
SEQRES   2    212  THR PRO VAL LYS ASN GLN GLY SER CYS GLY SER CYS TRP
SEQRES   3    212  ALA PHE SER ALA VAL VAL THR ILE GLU GLY ILE ILE LYS
SEQRES   4    212  ILE ARG THR GLY ASN LEU ASN GLN TYR SER GLU GLN GLU
SEQRES   5    212  LEU LEU ASP CYS ASP ARG ARG SER TYR GLY CYS ASN GLY
SEQRES   6    212  GLY TYR PRO TRP SER ALA LEU GLN LEU VAL ALA GLN TYR
SEQRES   7    212  GLY ILE HIS TYR ARG ASN THR TYR PRO TYR GLU GLY VAL
SEQRES   8    212  GLN ARG TYR CYS ARG SER ARG GLU LYS GLY PRO TYR ALA
SEQRES   9    212  ALA LYS THR ASP GLY VAL ARG GLN VAL GLN PRO TYR ASN
SEQRES  10    212  GLN GLY ALA LEU LEU TYR SER ILE ALA ASN GLN PRO VAL
SEQRES  11    212  SER VAL VAL LEU GLN ALA ALA GLY LYS ASP PHE GLN LEU
SEQRES  12    212  TYR ARG GLY GLY ILE PHE VAL GLY PRO CYS GLY ASN LYS
SEQRES  13    212  VAL ASP HIS ALA VAL ALA ALA VAL GLY TYR GLY PRO ASN
SEQRES  14    212  TYR ILE LEU ILE LYS ASN SER TRP GLY THR GLY TRP GLY
SEQRES  15    212  GLU ASN GLY TYR ILE ARG ILE LYS ARG GLY THR GLY ASN
SEQRES  16    212  SER TYR GLY VAL CYS GLY LEU TYR THR SER SER PHE TYR
SEQRES  17    212  PRO VAL LYS ASN
FTNOTE   1 RESIDUE 152 IS A CIS PROLINE.
FORMUL   2  HOH   *30(H2 O1)
HELIX    1  H1 SER     24  GLY     43  1                                  20
HELIX    2  H2 GLU     50  ARG     58  1                                   9
HELIX    3  H3 TYR     67  TYR     78  1                                  12
HELIX    4  H4 ASN    117  GLN    128  1                                  12
HELIX    5  H5 ALA    137  LEU    143  1                                   7
SHEET    1 S1A 7 ARG   111  GLN   112  0
SHEET    2 S1A 7 SER   206  TYR   208 -1  N  TYR   208   O  ARG   111
SHEET    3 S1A 7 VAL   130  SER   131 -1  N  SER   131   O  PHE   207
SHEET    4 S1A 7 ALA   162  GLY   167 -1  N  ALA   163   O  VAL   130
SHEET    5 S1A 7 ASN   169  ASN   175 -1  N  LYS   174   O  ALA   162
SHEET    6 S1A 7 GLY   185  ARG   191 -1  N  ILE   187   O  ILE   173
SHEET    7 S1A 7 GLU   183  GLU   183 -1  N  GLU   183   O  TYR   186
SHEET    1 S1B 5 VAL     5  TRP     7  0
SHEET    2 S1B 5 ALA   162  GLY   167 -1  N  TYR   166   O  VAL     5
SHEET    3 S1B 5 ASN   169  ASN   175 -1  N  LEU   172   O  GLY   165
SHEET    4 S1B 5 GLY   185  ARG   191 -1  N  ILE   189   O  ILE   171
SHEET    5 S1B 5 PHE   149  PHE   149  1  N  PHE   149   O  ARG   188
TURN     1  T1 GLY    62  GLY    65
TURN     2  T2 GLY   167  TYR   170
SSBOND   1 CYS     22    CYS     63
SSBOND   2 CYS     56    CYS     95
SSBOND   3 CYS    153    CYS    200
CISPEP   1 GLY    151    PRO    152          0       -12.60
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