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PDBsum entry 3ins

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Top Page protein ligands metals Protein-protein interface(s) links
Hormone PDB id
3ins
Jmol
Contents
Protein chains
21 a.a. *
30 a.a. *
Ligands
DOD ×321
DOD-DOD ×2
Metals
_ZN ×2
* Residue conservation analysis
HEADER    HORMONE                                 14-OCT-88   3INS
TITLE     STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: INSULIN (CHAIN A);
COMPND   3 CHAIN: A, C;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: INSULIN (CHAIN B);
COMPND   7 CHAIN: B, D;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   3 ORGANISM_COMMON: PIG;
SOURCE   4 ORGANISM_TAXID: 9823;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   7 ORGANISM_COMMON: PIG;
SOURCE   8 ORGANISM_TAXID: 9823
KEYWDS    HORMONE
EXPDTA    X-RAY DIFFRACTION; NEUTRON DIFFRACTION
AUTHOR    A.WLODAWER,H.SAVAGE
REVDAT   7   12-MAR-14 3INS    1       REMARK
REVDAT   6   21-AUG-13 3INS    1       REMARK SITE
REVDAT   5   13-JUL-11 3INS    1       VERSN
REVDAT   4   24-FEB-09 3INS    1       VERSN
REVDAT   3   01-APR-03 3INS    1       JRNL
REVDAT   2   20-JUL-95 3INS    1       EXPDTA
REVDAT   1   09-JAN-89 3INS    0
JRNL        AUTH   A.WLODAWER,H.SAVAGE,G.DODSON
JRNL        TITL   STRUCTURE OF INSULIN: RESULTS OF JOINT NEUTRON AND X-RAY
JRNL        TITL 2 REFINEMENT.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.B      V.  45    99 1989
JRNL        REFN                   ISSN 0108-7681
JRNL        PMID   2695122
JRNL        DOI    10.1107/S0108768188011012
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   N.W.ISAACS,R.C.AGARWAL
REMARK   1  TITL   EXPERIENCE WITH FAST FOURIER LEAST SQUARES IN THE REFINEMENT
REMARK   1  TITL 2 OF THE CRYSTAL STRUCTURE OF RHOMBOHEDRAL 2-ZINC INSULIN AT
REMARK   1  TITL 3 1.5 ANGSTROMS RESOLUTION
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.A      V.  34   782 1978
REMARK   1  REFN                   ISSN 0108-7673
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  X-RAY DATA.
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 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 + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.182
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            : 806
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 325
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: NULL
REMARK   3
REMARK   3  NEUTRON DATA.
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 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 + TEST SET) : 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
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            : 806
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 325
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: NULL
REMARK   4
REMARK   4 3INS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 230
REMARK 230 EXPERIMENTAL DETAILS
REMARK 230  EXPERIMENT TYPE                : NEUTRON DIFFRACTION
REMARK 230  DATE OF DATA COLLECTION        : NULL
REMARK 230  TEMPERATURE           (KELVIN) : NULL
REMARK 230  PH                             : NULL
REMARK 230  NUMBER OF CRYSTALS USED        : NULL
REMARK 230
REMARK 230  NEUTRON SOURCE                 : NULL
REMARK 230  BEAMLINE                       : NULL
REMARK 230  WAVELENGTH OR RANGE        (A) : NULL
REMARK 230  MONOCHROMATOR                  : NULL
REMARK 230  OPTICS                         : NULL
REMARK 230
REMARK 230  DETECTOR TYPE                  : NULL
REMARK 230  DETECTOR MANUFACTURER          : NULL
REMARK 230  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 230  DATA SCALING SOFTWARE          : NULL
REMARK 230
REMARK 230  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 230  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 230  RESOLUTION RANGE LOW       (A) : NULL
REMARK 230  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 230
REMARK 230 OVERALL.
REMARK 230  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 230  DATA REDUNDANCY                : NULL
REMARK 230  R MERGE                    (I) : NULL
REMARK 230  R SYM                      (I) : NULL
REMARK 230   FOR THE DATA SET  : NULL
REMARK 230
REMARK 230 IN THE HIGHEST RESOLUTION SHELL.
REMARK 230  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 230  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 230  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 230  DATA REDUNDANCY IN SHELL       : NULL
REMARK 230  R MERGE FOR SHELL          (I) : NULL
REMARK 230  R SYM FOR SHELL            (I) : NULL
REMARK 230   FOR SHELL         : NULL
REMARK 230
REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 230 SOFTWARE USED : NULL
REMARK 230 STARTING MODEL: NULL
REMARK 230
REMARK 230 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 36.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.25000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.81570
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       11.33333
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       41.25000
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       23.81570
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       11.33333
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       41.25000
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       23.81570
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       11.33333
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       47.63140
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       22.66667
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       47.63140
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       22.66667
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       47.63140
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       22.66667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 300 REMARK: THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT OF INSULIN CONSISTS OF
REMARK 300 TWO INSULIN MOLECULES EACH CONSISTING OF TWO CHAINS.  THIS
REMARK 300 ENTRY PRESENTS COORDINATES FOR MOLECULES I (CHAIN
REMARK 300 INDICATORS A AND B) AND II (CHAIN INDICATORS C AND D).  THE
REMARK 300 QUASI-TWO-FOLD AXIS THAT TRANSFORMS MOLECULE I INTO
REMARK 300 MOLECULE II IS GIVEN IN THE MTRIX RECORDS BELOW.  APPLYING
REMARK 300 THE THREE-FOLD CRYSTALLOGRAPHIC AXIS YIELDS A HEXAMER
REMARK 300 AROUND THE AXIS.  THERE ARE TWO ZINC IONS SITUATED ON THIS
REMARK 300 THREE-FOLD AXIS.  COORDINATES FOR THE ZINC IONS AND WATER
REMARK 300 MOLECULES ARE INCLUDED BELOW WITH A BLANK CHAIN INDICATOR.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -268.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -206.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000       34.00000
REMARK 350   BIOMT1   5 -0.500000 -0.866025  0.000000        0.00000
REMARK 350   BIOMT2   5  0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000       34.00000
REMARK 350   BIOMT1   6 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   6 -0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000       34.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN    ZN B  31  LIES ON A SPECIAL POSITION.
REMARK 375 ZN    ZN D  31  LIES ON A SPECIAL POSITION.
REMARK 375 O    DOD D  83  LIES ON A SPECIAL POSITION.
REMARK 375 O    DOD D  40  LIES ON A SPECIAL POSITION.
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    DOD B  83        DISTANCE =  9.11 ANGSTROMS
REMARK 525    DOD B  84        DISTANCE =  8.73 ANGSTROMS
REMARK 525    DOD B  85        DISTANCE =  7.18 ANGSTROMS
REMARK 525    DOD B  86        DISTANCE =  8.48 ANGSTROMS
REMARK 525    DOD B  87        DISTANCE =  8.20 ANGSTROMS
REMARK 525    DOD B  88        DISTANCE =  8.22 ANGSTROMS
REMARK 525    DOD B  89        DISTANCE =  9.71 ANGSTROMS
REMARK 525    DOD B  90        DISTANCE = 10.85 ANGSTROMS
REMARK 525    DOD B  91        DISTANCE =  9.69 ANGSTROMS
REMARK 525    DOD B  92        DISTANCE = 15.42 ANGSTROMS
REMARK 525    DOD C  22        DISTANCE = 14.64 ANGSTROMS
REMARK 525    DOD C  35        DISTANCE =  5.21 ANGSTROMS
REMARK 525    DOD C  55        DISTANCE = 11.04 ANGSTROMS
REMARK 525    DOD C 120        DISTANCE = 26.64 ANGSTROMS
REMARK 525    DOD C 128        DISTANCE = 30.38 ANGSTROMS
REMARK 525    DOD C 129        DISTANCE = 27.43 ANGSTROMS
REMARK 525    DOD C 132        DISTANCE = 25.98 ANGSTROMS
REMARK 525    DOD C 136        DISTANCE = 17.18 ANGSTROMS
REMARK 525    DOD C 137        DISTANCE = 30.98 ANGSTROMS
REMARK 525    DOD C 138        DISTANCE = 23.21 ANGSTROMS
REMARK 525    DOD C 141        DISTANCE = 27.24 ANGSTROMS
REMARK 525    DOD C 142        DISTANCE = 24.59 ANGSTROMS
REMARK 525    DOD C 143        DISTANCE = 33.11 ANGSTROMS
REMARK 525    DOD C 144        DISTANCE = 31.21 ANGSTROMS
REMARK 525    DOD D  98        DISTANCE = 19.05 ANGSTROMS
REMARK 525    DOD D 143        DISTANCE = 16.88 ANGSTROMS
REMARK 525    DOD D 144        DISTANCE = 19.72 ANGSTROMS
REMARK 525    DOD D 146        DISTANCE = 16.95 ANGSTROMS
REMARK 525    DOD D 148        DISTANCE = 15.10 ANGSTROMS
REMARK 525    DOD D 151        DISTANCE = 19.82 ANGSTROMS
REMARK 525    DOD D 152        DISTANCE = 18.68 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B  31  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  10   NE2
REMARK 620 2 DOD B  41   O    95.0
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 31
DBREF  3INS A    1    21  UNP    P01315   INS_PIG         88    108
DBREF  3INS B    1    30  UNP    P01315   INS_PIG         25     54
DBREF  3INS C    1    21  UNP    P01315   INS_PIG         88    108
DBREF  3INS D    1    30  UNP    P01315   INS_PIG         25     54
SEQRES   1 A   21  GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES   2 A   21  TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES   1 B   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES   2 B   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES   3 B   30  THR PRO LYS ALA
SEQRES   1 C   21  GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES   2 C   21  TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES   1 D   30  PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES   2 D   30  ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES   3 D   30  THR PRO LYS ALA
HET     ZN  B  31       1
HET     ZN  D  31       1
HETNAM      ZN ZINC ION
FORMUL   5   ZN    2(ZN 2+)
FORMUL   7  DOD   *325(D2 O)
HELIX    1 A11 GLY A    1  ILE A   10  1VAL 203 O H-BONDED TO HOH         10
HELIX    2 A12 SER A   12  GLU A   17  5CNTCTS MOSTLY GT 3A,NOT IDEAL      6
HELIX    3 B11 SER B    9  GLY B   20  1CYS 67 GLY 68, 3(10) CONTACTS     12
HELIX    4 A21 GLY C    1  ILE C   10  1NOT IDEAL ALPH,SOME PI CNTCTS     10
HELIX    5 A22 SER C   12  GLU C   17  5CNTCTS MOSTLY GT 3A,NOT IDEAL      6
HELIX    6 B21 SER D    9  GLY D   20  1CYS 67,GLY 68, 3(10) CONTACTS     12
SHEET    1   B 2 PHE B  24  TYR B  26  0
SHEET    2   B 2 PHE D  24  TYR D  26 -1  N  PHE B  24   O  TYR D  26
SSBOND   1 CYS A    6    CYS A   11                          1555   1555  2.03
SSBOND   2 CYS A    7    CYS B    7                          1555   1555  2.01
SSBOND   3 CYS A   20    CYS B   19                          1555   1555  2.06
SSBOND   4 CYS C    6    CYS C   11                          1555   1555  2.06
SSBOND   5 CYS C    7    CYS D    7                          1555   1555  1.99
SSBOND   6 CYS C   20    CYS D   19                          1555   1555  2.02
LINK         NE2 HIS B  10                ZN    ZN B  31     1555   1555  2.12
LINK         NE2 HIS D  10                ZN    ZN D  31     1555   1555  2.17
LINK        ZN    ZN B  31                 O   DOD B  41     1555   1555  2.20
SITE     1 AC1  2 HIS B  10  DOD B  41
SITE     1 AC2  2 HIS D  10  DOD D 129
CRYST1   82.500   82.500   34.000  90.00  90.00 120.00 H 3          18
ORIGX1      0.012121  0.006998  0.000000        0.00000
ORIGX2      0.000000  0.013996  0.000000        0.00000
ORIGX3      0.000000  0.000000  0.029412        0.00000
SCALE1      0.012121  0.006998  0.000000        0.00000
SCALE2      0.000000  0.013996  0.000000        0.00000
SCALE3      0.000000  0.000000  0.029412        0.00000
MTRIX1   1 -0.878620 -0.476960  0.023050        0.00000    1
MTRIX2   1 -0.477430  0.878370 -0.022860        0.00000    1
MTRIX3   1 -0.009350 -0.031090 -0.999470        0.00000    1
      
PROCHECK
Go to PROCHECK summary
 References