HEADER HORMONE 21-JUN-94 1TYM
TITLE THE STRUCTURE OF A COMPLEX OF HEXAMERIC INSULIN AND 4'-
TITLE 2 HYDROXYACETANILIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN;
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.D.SMITH,E.CISZAK
REVDAT 3 24-FEB-09 1TYM 1 VERSN
REVDAT 2 15-JAN-95 1TYM 1 JRNL
REVDAT 1 30-SEP-94 1TYM 0
JRNL AUTH G.D.SMITH,E.CISZAK
JRNL TITL THE STRUCTURE OF A COMPLEX OF HEXAMERIC INSULIN
JRNL TITL 2 AND 4'-HYDROXYACETANILIDE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 91 8851 1994
JRNL REFN ISSN 0027-8424
JRNL PMID 8090735
JRNL DOI 10.1073/PNAS.91.19.8851
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.CISZAK,G.D.SMITH
REMARK 1 TITL CRYSTALLOGRAPHIC EVIDENCE FOR DUAL COORDINATION
REMARK 1 TITL 2 AROUND ZINC IN THE T3R3 HUMAN INSULIN HEXAMER
REMARK 1 REF BIOCHEMISTRY V. 33 1512 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.D.SMITH,D.C.SWENSON,E.J.DODSON,G.G.DODSON,
REMARK 1 AUTH 2 C.D.REYNOLDS
REMARK 1 TITL STRUCTURAL STABILITY IN THE 4-ZINC HUMAN INSULIN
REMARK 1 TITL 2 HEXAMER
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 81 7093 1984
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
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) : 0.173
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 : 779
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 98
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) : 0.019 ; 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 1TYM 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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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 (%): 39.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
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 40.44000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.34804
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 12.53333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 40.44000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 23.34804
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 12.53333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 40.44000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 23.34804
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 12.53333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.69609
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 25.06667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 46.69609
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 25.06667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 46.69609
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 25.06667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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:
REMARK 300 THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT OF INSULIN CONSISTS
REMARK 300 OF TWO INSULIN MONOMERS EACH CONSISTING OF TWO
REMARK 300 HETEROCHAINS. THE ENTRY PRESENTS COORDINATES FOR MONOMER
REMARK 300 I (CHAIN IDENTIFIERS A AND B) AND II (CHAIN IDENTIFIERS C
REMARK 300 AND D). APPLYING THE THREE-FOLD CRYSTALLOGRAPHIC SYMMETRY
REMARK 300 AXIS YIELDS A HEXAMER AROUND THE AXIS. THERE ARE TWO ZINC
REMARK 300 IONS PER INSULIN HEXAMER LOCATED ON THE THREE-FOLD AXIS.
REMARK 300 WATERS HOH 1, HOH 2, HOH 4, AND HOH 105, AND CL D 2 ARE
REMARK 300 LOCATED ON THE THREE-FOLD AXIS.
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: 1670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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: 1110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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: 18770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -285.0 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: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 APPLY THE FOLLOWING TO CHAINS: A, B
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
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -142.0 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 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: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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 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 CL CL D 32 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 32 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 33 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 35 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 48 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE CONFORMATIONS OF THE TWO MONOMERS ARE DIFFERENT AS THE
REMARK 400 RESULT OF A DIFFERENCE IN CONFORMATION AT THE N-TERMINI
REMARK 400 OF THE B AND D CHAINS. IN MONOMER I, B 1 - B 8 ADOPT
REMARK 400 AN EXTENDED CONFORMATION (T STATE) WHILE IN MONOMER II
REMARK 400 RESIDUES D 4 THROUGH D 8 ARE ALPHA-HELICAL (R STATE).
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PHE D 1
REMARK 465 VAL D 2
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 THR B 30 CA C O CB OG1 CG2
REMARK 470 LYS D 29 CG CD CE NZ
REMARK 470 THR D 30 CA C O CB OG1 CG2
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 OE1 GLN A 5 O HOH A 24 2.00
REMARK 500 O HOH D 37 O HOH D 41 2.04
REMARK 500 O ILE C 10 O HOH C 107 2.11
REMARK 500 O HOH B 42 O HOH D 41 2.15
REMARK 500 OE1 GLU B 21 O HOH B 58 2.17
REMARK 500 N GLY C 1 OE1 GLU C 4 2.18
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 14 CA - CB - CG ANGL. DEV. = -13.9 DEGREES
REMARK 500 TYR A 14 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TYR B 16 CB - CG - CD2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 LEU B 15 O - C - N ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLN C 5 CB - CG - CD ANGL. DEV. = 18.5 DEGREES
REMARK 500 HIS D 10 CE1 - NE2 - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 CYS D 19 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 GLU D 21 CB - CG - CD ANGL. DEV. = 19.1 DEGREES
REMARK 500 GLU D 21 OE1 - CD - OE2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 GLU D 21 CG - CD - OE1 ANGL. DEV. = 19.3 DEGREES
REMARK 500 ARG D 22 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG D 22 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 TYR D 26 CB - CG - CD1 ANGL. DEV. = -4.2 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 CYS A 7 -60.72 -104.50
REMARK 500 SER A 9 -162.73 -121.97
REMARK 500 LYS B 29 108.46 -53.43
REMARK 500 LYS D 29 -135.28 -121.91
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 B 29 12.51
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 D 33 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH D 48 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH A 39 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH A 40 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH A 41 DISTANCE = 8.36 ANGSTROMS
REMARK 525 HOH D 56 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B 61 DISTANCE = 9.11 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 EACH OF TWO ZINC IONS IS COORDINATED BY THE THREE SYMMETRY
REMARK 600 RELATED HIS B 10 SIDE CHAINS. THE COORDINATION SPHERE OF
REMARK 600 ZN B 1 IS TETRAHEDRAL WITH THE FOURTH SITE FILLED BY WATER,
REMARK 600 HOH 1. THE COORDINATION OF ZN D 1 IS TETRAHEDRAL TO
REMARK 600 CL D 2.
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 HOH B 32 O
REMARK 620 2 HIS B 10 NE2 114.9
REMARK 620 3 HIS B 10 NE2 114.9 103.5
REMARK 620 4 HOH B 32 O 0.0 114.9 114.9
REMARK 620 5 HOH B 32 O 0.0 114.9 114.9 0.0
REMARK 620 6 HIS B 10 NE2 114.9 103.5 103.5 114.9 114.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CL D 32 CL
REMARK 620 2 HIS D 10 NE2 121.4
REMARK 620 3 HIS D 10 NE2 121.4 95.3
REMARK 620 4 HIS D 10 NE2 121.4 95.3 95.3
REMARK 620 5 CL D 32 CL 0.0 121.4 121.4 121.4
REMARK 620 6 CL D 32 CL 0.0 121.4 121.4 121.4 0.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: TYL
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: TYLENOL BINDING SITE, THE TYLENOL MOLECULE IS
REMARK 800 BOUND IN AN ELLIPTICAL CAVITY BETWEEN R STATE MONOMERS
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 31
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 31
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 32
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYL C 100
DBREF 1TYM A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1TYM B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1TYM C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1TYM D 1 30 UNP P01308 INS_HUMAN 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 THR
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 THR
HET ZN B 31 1
HET ZN D 31 1
HET CL D 32 1
HET TYL C 100 11
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM TYL N-(4-HYDROXYPHENYL)ACETAMIDE (TYLENOL)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 CL CL 1-
FORMUL 8 TYL C8 H9 N O2
FORMUL 9 HOH *98(H2 O)
HELIX 1 H1 GLY A 1 SER A 9 1 9
HELIX 2 H2 SER A 12 CYS A 20 5MIXED ALPHA, 3/10 HELIX 9
HELIX 3 H3 GLY B 8 GLY B 20 1T CONFORMATION 13
HELIX 4 H4 GLY C 1 SER C 9 1 9
HELIX 5 H5 SER C 12 CYS C 20 5MIXED ALPHA, 3/10 HELIX 9
HELIX 6 H6 GLN D 4 GLY D 20 1R CONFORMATION 17
SHEET 1 S1 2 PHE B 24 TYR B 26 0
SHEET 2 S1 2 PHE D 24 TYR D 26 -1 N PHE D 24 O TYR B 26
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.01
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.02
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.02
SSBOND 4 CYS C 6 CYS C 11 1555 1555 2.02
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.02
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.06
LINK ZN ZN B 31 O HOH B 32 1555 1555 2.05
LINK ZN ZN B 31 NE2 HIS B 10 1555 1555 2.11
LINK ZN ZN D 31 CL CL D 32 1555 1555 2.33
LINK ZN ZN D 31 NE2 HIS D 10 1555 1555 2.12
LINK ZN ZN B 31 NE2 HIS B 10 1555 2555 2.11
LINK ZN ZN B 31 O HOH B 32 1555 2555 2.05
LINK ZN ZN B 31 O HOH B 32 1555 3555 2.05
LINK ZN ZN B 31 NE2 HIS B 10 1555 3555 2.11
LINK ZN ZN D 31 NE2 HIS D 10 1555 2555 2.12
LINK ZN ZN D 31 NE2 HIS D 10 1555 3555 2.12
LINK ZN ZN D 31 CL CL D 32 1555 2555 2.33
LINK ZN ZN D 31 CL CL D 32 1555 3555 2.33
SITE 1 TYL 8 GLU B 13 LEU B 17 CYS C 6 ILE C 10
SITE 2 TYL 8 CYS C 11 HIS D 5 HIS D 10 LEU D 11
SITE 1 AC1 2 HIS B 10 HOH B 32
SITE 1 AC2 2 HIS D 10 CL D 32
SITE 1 AC3 1 ZN D 31
SITE 1 AC4 8 GLU B 13 LEU B 17 CYS C 6 SER C 9
SITE 2 AC4 8 ILE C 10 CYS C 11 HIS D 5 LEU D 11
CRYST1 80.880 80.880 37.600 90.00 90.00 120.00 H 3 18
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 0.012364 0.007138 0.000000 0.00000
SCALE2 0.000000 0.014277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026596 0.00000
(ATOM LINES ARE NOT SHOWN.)
END