HEADER HORMONE 18-DEC-96 1XDA
TITLE STRUCTURE OF INSULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID ACYLATED INSULIN;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 SYNONYM: NN304 INSULIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FATTY ACID ACYLATED INSULIN;
COMPND 8 CHAIN: B, D, F, H;
COMPND 9 SYNONYM: NN304 INSULIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 13 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS HORMONE, METABOLIC ROLE, CHEMICAL ACTIVITY, INSULIN ALBUMIN, FATTY
KEYWDS 2 ACID, GLUCOSE METABOLISM, DIABETES
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.WHITTINGHAM,S.HAVELUND,I.JONASSEN
REVDAT 3 03-APR-24 1XDA 1 REMARK LINK
REVDAT 2 24-FEB-09 1XDA 1 VERSN
REVDAT 1 07-JUL-97 1XDA 0
JRNL AUTH J.L.WHITTINGHAM,S.HAVELUND,I.JONASSEN
JRNL TITL CRYSTAL STRUCTURE OF A PROLONGED-ACTING INSULIN WITH
JRNL TITL 2 ALBUMIN-BINDING PROPERTIES.
JRNL REF BIOCHEMISTRY V. 36 2826 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9062110
JRNL DOI 10.1021/BI9625105
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.MARKUSSEN,S.HAVELUND,P.KURTZHALS,A.S.ANDERSEN,J.HALSTROM,
REMARK 1 AUTH 2 E.HASSELAGER,U.D.LARSEN,U.RIBEL,L.SCHAFFER,K.VAD,I.JONASSEN
REMARK 1 TITL SOLUBLE, FATTY ACID ACYLATED INSULINS BIND TO ALBUMIN AND
REMARK 1 TITL 2 SHOW PROTRACTED ACTION IN PIGS
REMARK 1 REF DIABETOLOGIA V. 39 281 1996
REMARK 1 REFN ISSN 0012-186X
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.D.SMITH,G.G.DODSON
REMARK 1 TITL THE STRUCTURE OF A RHOMBOHEDRAL R6 INSULIN HEXAMER THAT
REMARK 1 TITL 2 BINDS PHENOL
REMARK 1 REF BIOPOLYMERS V. 32 441 1992
REMARK 1 REFN ISSN 0006-3525
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 16624
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) : 0.174
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 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1592
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.40
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.010 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.030 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.030 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.020 ; 0.030
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.080 ; 0.100
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.180 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.280 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.270 ; 0.300
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) : 4.500 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 15.700; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 24.700; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.630 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.270 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.990 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.030 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XDA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177249.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUN-96
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X31
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16624
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.05500
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) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27800
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 4-IODOPHENOL INSULIN DIMER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP, 0.1M TRI-SODIUM CITRATE,
REMARK 280 6% (W/V) TRIS, 0.02% (W/V) ZINC ACETATE, PH 8.2.
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 39.37600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.73374
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.39967
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 39.37600
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 22.73374
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 26.39967
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 39.37600
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 22.73374
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 26.39967
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.46749
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 52.79933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 45.46749
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 52.79933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 45.46749
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 52.79933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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: 1870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 4
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: 1650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -332.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -287.0 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: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 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
REMARK 350 BIOMOLECULE: 8
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 9
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -149.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 10
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 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: 11
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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: 12
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 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 30 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL B 31 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN D 30 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL D 31 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN F 30 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL F 31 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN H 30 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL H 31 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 57 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 53 LIES ON A SPECIAL POSITION.
REMARK 375 HOH F 51 LIES ON A SPECIAL POSITION.
REMARK 375 HOH H 47 LIES ON A SPECIAL POSITION.
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 GLN A 5 CG CD OE1 NE2
REMARK 480 TYR A 14 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 LYS B 29 N CA C O CB CG CD
REMARK 480 LYS B 29 CE NZ
REMARK 480 GLU C 4 CG CD OE1 OE2
REMARK 480 GLU D 21 CB CG CD OE1 OE2
REMARK 480 LYS D 29 CB CG CD CE NZ
REMARK 480 TYR E 14 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 LYS F 29 O CB CG CD CE NZ
REMARK 480 GLU G 4 CG CD OE1 OE2
REMARK 480 GLU H 21 CG CD OE1 OE2
REMARK 480 LYS H 29 C O CB CG CD CE NZ
REMARK 480 LYS H 29 OXT
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 NE2 GLN C 5 OH TYR C 19 1.61
REMARK 500 OE1 GLN A 5 O HOH A 94 1.86
REMARK 500 OE2 GLU A 17 O HOH A 122 1.95
REMARK 500 O HOH C 113 O HOH D 44 2.10
REMARK 500 OH TYR H 26 O HOH H 59 2.12
REMARK 500
REMARK 500 REMARK: NULL
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 CD2 LEU D 17 O HOH B 61 2555 1.52
REMARK 500 CD1 LEU D 17 O HOH B 62 2555 1.79
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 LEU A 16 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG B 22 CD - NE - CZ ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TYR B 26 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG D 22 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 PRO D 28 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG F 22 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TYR F 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 PRO B 28 -74.87 -63.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 AT THE END OF CHAINS B, D, F, AND H, ATOM C1 OF A FATTY
REMARK 600 ACID (RESIDUE 30) IS COVALENTLY LINKED TO THE NZ ATOM OF A
REMARK 600 LYS SIDE CHAIN (RESIDUE 29).
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 MYR B 39
REMARK 615 MYR F 39
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 30 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 HIS B 10 NE2 104.8
REMARK 620 3 HIS B 10 NE2 104.8 104.8
REMARK 620 4 CL B 31 CL 113.8 113.8 113.8
REMARK 620 5 CL B 31 CL 113.8 113.8 113.8 0.0
REMARK 620 6 CL B 31 CL 113.8 113.8 113.8 0.0 0.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 30 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 10 NE2
REMARK 620 2 HIS D 10 NE2 105.8
REMARK 620 3 HIS D 10 NE2 105.8 105.8
REMARK 620 4 CL D 31 CL 113.0 113.0 113.0
REMARK 620 5 CL D 31 CL 113.0 113.0 113.0 0.0
REMARK 620 6 CL D 31 CL 113.0 113.0 113.0 0.0 0.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 30 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 10 NE2
REMARK 620 2 HIS F 10 NE2 108.0
REMARK 620 3 HIS F 10 NE2 108.0 108.0
REMARK 620 4 CL F 31 CL 110.9 110.9 110.9
REMARK 620 5 CL F 31 CL 110.9 110.9 110.9 0.0
REMARK 620 6 CL F 31 CL 110.9 110.9 110.9 0.0 0.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 30 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 10 NE2
REMARK 620 2 HIS H 10 NE2 105.7
REMARK 620 3 HIS H 10 NE2 105.7 105.7
REMARK 620 4 CL H 31 CL 113.0 113.0 113.0
REMARK 620 5 CL H 31 CL 113.0 113.0 113.0 0.0
REMARK 620 6 CL H 31 CL 113.0 113.0 113.0 0.0 0.0
REMARK 620 N 1 2 3 4 5
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 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH A 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR B 39
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH C 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR D 39
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH E 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR F 39
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH G 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR H 39
DBREF 1XDA A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1XDA B 1 29 UNP P01308 INS_HUMAN 25 53
DBREF 1XDA C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1XDA D 1 29 UNP P01308 INS_HUMAN 25 53
DBREF 1XDA E 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1XDA F 1 29 UNP P01308 INS_HUMAN 25 53
DBREF 1XDA G 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1XDA H 1 29 UNP P01308 INS_HUMAN 25 53
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 29 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 29 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 B 29 THR PRO LYS
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 29 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 D 29 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 D 29 THR PRO LYS
SEQRES 1 E 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 E 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 F 29 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 F 29 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 F 29 THR PRO LYS
SEQRES 1 G 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 G 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 H 29 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 H 29 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 H 29 THR PRO LYS
HET IPH A 22 7
HET ZN B 30 1
HET CL B 31 1
HET MYR B 39 15
HET IPH C 22 7
HET ZN D 30 1
HET CL D 31 1
HET MYR D 39 15
HET IPH E 22 7
HET ZN F 30 1
HET CL F 31 1
HET MYR F 39 15
HET IPH G 22 7
HET ZN H 30 1
HET CL H 31 1
HET MYR H 39 15
HETNAM IPH PHENOL
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM MYR MYRISTIC ACID
FORMUL 9 IPH 4(C6 H6 O)
FORMUL 10 ZN 4(ZN 2+)
FORMUL 11 CL 4(CL 1-)
FORMUL 12 MYR 4(C14 H28 O2)
FORMUL 25 HOH *154(H2 O)
HELIX 1 1 ILE A 2 CYS A 6 1 5
HELIX 2 2 LEU A 13 TYR A 19 1 7
HELIX 3 3 VAL B 2 ARG B 22 1 21
HELIX 4 4 ILE C 2 CYS C 6 1 5
HELIX 5 5 LEU C 13 TYR C 19 1 7
HELIX 6 6 VAL D 2 ARG D 22 1 21
HELIX 7 7 ILE E 2 CYS E 6 1 5
HELIX 8 8 LEU E 13 TYR E 19 1 7
HELIX 9 9 VAL F 2 ARG F 22 1 21
HELIX 10 10 ILE G 2 THR G 8 1 7
HELIX 11 11 LEU G 13 TYR G 19 1 7
HELIX 12 12 VAL H 2 ARG H 22 1 21
SHEET 1 A 2 PHE B 24 TYR B 26 0
SHEET 2 A 2 PHE D 24 TYR D 26 -1 N TYR D 26 O PHE B 24
SHEET 1 B 2 PHE F 24 TYR F 26 0
SHEET 2 B 2 PHE H 24 TYR H 26 -1 N TYR H 26 O PHE F 24
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.02
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.00
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.04
SSBOND 4 CYS C 6 CYS C 11 1555 1555 1.98
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.02
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.02
SSBOND 7 CYS E 6 CYS E 11 1555 1555 2.00
SSBOND 8 CYS E 7 CYS F 7 1555 1555 2.03
SSBOND 9 CYS E 20 CYS F 19 1555 1555 2.02
SSBOND 10 CYS G 6 CYS G 11 1555 1555 1.98
SSBOND 11 CYS G 7 CYS H 7 1555 1555 2.02
SSBOND 12 CYS G 20 CYS H 19 1555 1555 2.03
LINK NZ LYS B 29 C1 MYR B 39 1555 1555 1.25
LINK ND2 ASN D 3 C13 MYR F 39 1555 1555 1.55
LINK NZ LYS D 29 C1 MYR D 39 1555 1555 1.28
LINK NZ LYS F 29 C1 MYR F 39 1555 1555 1.31
LINK NZ LYS H 29 C1 MYR H 39 1555 1555 1.32
LINK NE2 HIS B 10 ZN ZN B 30 1555 1555 2.02
LINK NE2 HIS B 10 ZN ZN B 30 3555 1555 2.02
LINK NE2 HIS B 10 ZN ZN B 30 2555 1555 2.02
LINK ZN ZN B 30 CL CL B 31 1555 1555 2.17
LINK ZN ZN B 30 CL CL B 31 1555 2555 2.17
LINK ZN ZN B 30 CL CL B 31 1555 3555 2.17
LINK NE2 HIS D 10 ZN ZN D 30 1555 1555 1.94
LINK NE2 HIS D 10 ZN ZN D 30 3555 1555 1.94
LINK NE2 HIS D 10 ZN ZN D 30 2555 1555 1.94
LINK ZN ZN D 30 CL CL D 31 1555 1555 2.17
LINK ZN ZN D 30 CL CL D 31 1555 2555 2.17
LINK ZN ZN D 30 CL CL D 31 1555 3555 2.17
LINK NE2 HIS F 10 ZN ZN F 30 1555 1555 1.98
LINK NE2 HIS F 10 ZN ZN F 30 3555 1555 1.98
LINK NE2 HIS F 10 ZN ZN F 30 2555 1555 1.98
LINK ZN ZN F 30 CL CL F 31 1555 1555 2.14
LINK ZN ZN F 30 CL CL F 31 1555 3555 2.14
LINK ZN ZN F 30 CL CL F 31 1555 2555 2.14
LINK NE2 HIS H 10 ZN ZN H 30 1555 1555 1.99
LINK NE2 HIS H 10 ZN ZN H 30 3555 1555 1.99
LINK NE2 HIS H 10 ZN ZN H 30 2555 1555 1.99
LINK ZN ZN H 30 CL CL H 31 1555 1555 2.17
LINK ZN ZN H 30 CL CL H 31 1555 3555 2.17
LINK ZN ZN H 30 CL CL H 31 1555 2555 2.17
SITE 1 AC1 2 HIS B 10 CL B 31
SITE 1 AC2 2 HIS B 10 ZN B 30
SITE 1 AC3 2 HIS D 10 CL D 31
SITE 1 AC4 2 HIS D 10 ZN D 30
SITE 1 AC5 2 HIS F 10 CL F 31
SITE 1 AC6 2 HIS F 10 ZN F 30
SITE 1 AC7 2 HIS H 10 CL H 31
SITE 1 AC8 2 HIS H 10 ZN H 30
SITE 1 AC9 6 CYS A 6 SER A 9 ILE A 10 CYS A 11
SITE 2 AC9 6 HIS B 5 LEU B 11
SITE 1 BC1 3 CYS A 7 ASN B 3 GLN B 4
SITE 1 BC2 6 CYS C 6 SER C 9 ILE C 10 CYS C 11
SITE 2 BC2 6 HIS D 5 LEU D 11
SITE 1 BC3 4 GLN D 4 HOH D 56 CYS E 7 ASN F 3
SITE 1 BC4 6 CYS E 6 SER E 9 ILE E 10 CYS E 11
SITE 2 BC4 6 HIS F 5 LEU F 11
SITE 1 BC5 3 PHE D 1 ASN D 3 PHE F 1
SITE 1 BC6 6 CYS G 6 SER G 9 ILE G 10 CYS G 11
SITE 2 BC6 6 HIS H 5 LEU H 11
SITE 1 BC7 5 PHE B 1 CYS G 7 PHE H 1 ASN H 3
SITE 2 BC7 5 GLN H 4
CRYST1 78.752 78.752 79.199 90.00 90.00 120.00 H 3 36
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 0.012698 0.007331 0.000000 0.00000
SCALE2 0.000000 0.014662 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012626 0.00000
(ATOM LINES ARE NOT SHOWN.)
END