HEADER HORMONE 10-MAY-82 2INS
TITLE THE STRUCTURE OF DES-PHE B1 BOVINE INSULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DES-PHE B1 INSULIN (CHAIN A);
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DES-PHE B1 INSULIN (CHAIN B);
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: CATTLE;
SOURCE 8 ORGANISM_TAXID: 9913
KEYWDS HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.D.SMITH,W.L.DUAX,E.J.DODSON,G.G.DODSON,R.A.G.DEGRAAF,C.D.REYNOLDS
REVDAT 11 29-NOV-17 2INS 1 HELIX
REVDAT 10 16-NOV-11 2INS 1 VERSN HETATM
REVDAT 9 29-SEP-10 2INS 1 REMARK
REVDAT 8 24-FEB-09 2INS 1 VERSN
REVDAT 7 31-MAY-84 2INS 1 REMARK
REVDAT 6 31-JAN-84 2INS 1 REMARK
REVDAT 5 27-OCT-83 2INS 1 REMARK
REVDAT 4 30-SEP-83 2INS 1 REVDAT
REVDAT 3 13-JUN-83 2INS 1 AUTHOR JRNL
REVDAT 2 07-MAR-83 2INS 3 JRNL REMARK MTRIX
REVDAT 1 05-AUG-82 2INS 0
JRNL AUTH G.D.SMITH,W.L.DUAX,E.J.DODSON,G.G.DODSON,R.A.G.DEGRAAF,
JRNL AUTH 2 C.D.REYNOLDS
JRNL TITL THE STRUCTURE OF DES-PHE B1 BOVINE INSULIN
JRNL REF ACTA CRYSTALLOGR.,SECT.B V. 38 3028 1982
JRNL REFN ISSN 0108-7681
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.BORDAS,G.G.DODSON,H.GREWE,M.H.J.KOCH,B.KREBS,J.RANDALL
REMARK 1 TITL A COMPARATIVE ASSESSMENT OF THE ZINC-PROTEIN COORDINATION IN
REMARK 1 TITL 2 2ZN-INSULIN AS DETERMINED BY X-RAY ABSORPTION FINE STRUCTURE
REMARK 1 TITL 3 (EXAFS) AND X-RAY CRYSTALLOGRAPHY
REMARK 1 REF PROC.R.SOC.LONDON,SER.B V. 219 21 1983
REMARK 1 REFN ISSN 0080-4649
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.J.DODSON,G.G.DODSON,D.C.HODGKIN,C.D.REYNOLDS
REMARK 1 TITL STRUCTURAL RELATIONSHIPS IN THE TWO-ZINC INSULIN HEXAMER
REMARK 1 REF CAN.J.BIOCHEM. V. 57 469 1979
REMARK 1 REFN ISSN 0008-4018
REMARK 1 REFERENCE 3
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 1 REFERENCE 4
REMARK 1 AUTH G.BENTLEY,G.DODSON,A.LEWITOVA
REMARK 1 TITL RHOMBOHEDRAL INSULIN CRYSTAL TRANSFORMATION
REMARK 1 REF J.MOL.BIOL. V. 126 871 1978
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH E.J.DODSON,N.W.ISAACS,J.S.ROLLETT
REMARK 1 TITL A METHOD FOR FITTING SATISFACTORY MODELS TO SETS OF ATOMIC
REMARK 1 TITL 2 POSITIONS IN PROTEIN STRUCTURE REFINEMENTS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 32 311 1976
REMARK 1 REFN ISSN 0108-7673
REMARK 1 REFERENCE 6
REMARK 1 AUTH D.C.HODGKIN
REMARK 1 TITL VARIETIES OF INSULIN
REMARK 1 REF J.ENDOCRINOL. V. 63 1 1974
REMARK 1 REFN ISSN 0022-0795
REMARK 1 REFERENCE 7
REMARK 1 AUTH D.C.HODGKIN
REMARK 1 TITL THE STRUCTURE OF INSULIN
REMARK 1 REF DAN.TIDSSKR.FARM. V. 46 1 1972
REMARK 1 REFN ISSN 0011-6513
REMARK 1 REFERENCE 8
REMARK 1 AUTH T.BLUNDELL,G.DODSON,D.HODGKIN,D.MERCOLA
REMARK 1 TITL INSULIN. THE STRUCTURE IN THE CRYSTAL AND ITS REFLECTION IN
REMARK 1 TITL 2 CHEMISTRY AND BIOLOGY
REMARK 1 REF ADV.PROTEIN CHEM. V. 26 279 1972
REMARK 1 REFN ISSN 0065-3233
REMARK 1 REFERENCE 9
REMARK 1 AUTH T.L.BLUNDELL,J.F.CUTFIELD,E.J.DODSON,G.G.DODSON,D.C.HODGKIN,
REMARK 1 AUTH 2 D.A.MERCOLA
REMARK 1 TITL THE CRYSTAL STRUCTURE OF RHOMBOHEDRAL 2 ZINC INSULIN
REMARK 1 REF COLD SPRING HARBOR V. 36 233 1972
REMARK 1 REF 2 SYMP.QUANT.BIOL.
REMARK 1 REFN ISSN 0091-7451
REMARK 1 REFERENCE 10
REMARK 1 AUTH T.L.BLUNDELL,J.F.CUTFIELD,S.M.CUTFIELD,E.J.DODSON,
REMARK 1 AUTH 2 G.G.DODSON,D.C.HODGKIN,D.A.MERCOLA,M.VIJAYAN
REMARK 1 TITL ATOMIC POSITIONS IN RHOMBOHEDRAL 2-ZINC INSULIN CRYSTALS
REMARK 1 REF NATURE V. 231 506 1971
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 11
REMARK 1 AUTH T.L.BLUNDELL,G.G.DODSON,E.DODSON,D.C.HODGKIN,M.VIJAYAN
REMARK 1 TITL X-RAY ANALYSIS AND THE STRUCTURE OF INSULIN
REMARK 1 REF RECENT PROG.HORM.RES. V. 27 1 1971
REMARK 1 REFN ISSN 0079-9963
REMARK 1 REFERENCE 12
REMARK 1 AUTH E.N.BAKER,G.DODSON
REMARK 1 TITL X-RAY DIFFRACTION DATA ON SOME CRYSTALLINE VARIETIES OF
REMARK 1 TITL 2 INSULIN
REMARK 1 REF J.MOL.BIOL. V. 54 605 1970
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 13
REMARK 1 AUTH M.J.ADAMS,T.L.BLUNDELL,E.J.DODSON,G.G.DODSON,M.VIJAYAN,
REMARK 1 AUTH 2 E.N.BAKER,M.M.HARDING,D.C.HODGKIN,B.RIMMER,S.SHEAT
REMARK 1 TITL STRUCTURE OF RHOMBOHEDRAL 2 ZINC INSULIN CRYSTALS
REMARK 1 REF NATURE V. 224 491 1969
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 14
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 187 1972
REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FAST FOURIER LEAST-SQUARES REFINEMENT
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
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 : 2128
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) : 0.180
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 : 770
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 184
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) : 0.200
REMARK 3 BOND ANGLES (DEGREES) : 3.000
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:
REMARK 3 THE FOLLOWING RESIDUES ARE DISORDERED - ARG B 22,
REMARK 3 LYS D 29.
REMARK 3
REMARK 3 THE MODEL OF THE WATER STRUCTURE OBTAINED FROM THE
REMARK 3 REFINEMENT OF 2 ZN PORCINE INSULIN AT 1.5 ANGSTROMS
REMARK 3 RESOLUTION WAS USED THROUGHOUT THE DES-PHE B1 INSULIN
REMARK 3 REFINEMENT.
REMARK 4
REMARK 4 2INS 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_1000178259.
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 (%): 36.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
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 40.80000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.55589
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 11.33333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 40.80000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 23.55589
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 11.33333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 40.80000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 23.55589
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 47.11178
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 47.11178
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 47.11178
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, 5
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 SOME
REMARK 300 WATER MOLECULES ARE INCLUDED BELOW WITH A BLANK CHAIN
REMARK 300 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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -242.0 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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: 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: 1580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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: 5
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: 1630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 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 1 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN D 31 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 52 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 133 LIES ON A SPECIAL POSITION.
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 TYR C 14 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR C 14 OH
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 NH2 ARG D 22 O HOH D 34 1.80
REMARK 500 O HOH D 116 O HOH D 120 1.89
REMARK 500 OE1 GLU D 21 O HOH D 77 2.02
REMARK 500 O HOH B 49 O HOH B 53 2.03
REMARK 500 O HOH B 56 O HOH D 73 2.09
REMARK 500 O HOH D 125 O HOH D 128 2.14
REMARK 500 O ALA B 30 O HOH B 65 2.16
REMARK 500 O HOH B 60 O HOH D 69 2.18
REMARK 500 O HOH D 48 O HOH D 60 2.18
REMARK 500 O HOH A 24 O HOH B 43 2.18
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 NZ LYS D 29 O HOH D 103 2554 1.50
REMARK 500 O ASN D 3 O HOH D 107 1554 1.63
REMARK 500 CB TYR A 19 O HOH D 40 2555 1.66
REMARK 500 CE LYS D 29 O HOH D 103 2554 1.76
REMARK 500 CG ARG B 22 O HOH D 126 2554 1.83
REMARK 500 OH TYR D 26 O HOH A 40 1554 1.94
REMARK 500 CD2 LEU B 15 O HOH D 40 2555 1.99
REMARK 500 NE2 GLN C 5 O HOH B 71 1554 2.03
REMARK 500 O HOH B 80 O HOH D 121 2555 2.05
REMARK 500 NE2 GLN D 4 O HOH D 118 1554 2.13
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG B 22 CD ARG B 22 NE -0.165
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 ILE A 2 CA - CB - CG2 ANGL. DEV. = 19.7 DEGREES
REMARK 500 CYS A 7 CB - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 TYR A 14 CA - CB - CG ANGL. DEV. = -13.0 DEGREES
REMARK 500 TYR A 19 CA - CB - CG ANGL. DEV. = -13.3 DEGREES
REMARK 500 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 CYS A 20 C - N - CA ANGL. DEV. = -15.2 DEGREES
REMARK 500 ASN A 21 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASN A 21 N - CA - CB ANGL. DEV. = -17.1 DEGREES
REMARK 500 ASN A 21 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 HIS B 5 CA - CB - CG ANGL. DEV. = -10.2 DEGREES
REMARK 500 GLU B 21 N - CA - CB ANGL. DEV. = -16.6 DEGREES
REMARK 500 GLU B 21 CB - CG - CD ANGL. DEV. = -25.8 DEGREES
REMARK 500 GLU B 21 OE1 - CD - OE2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG B 22 CG - CD - NE ANGL. DEV. = 19.3 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 GLN C 5 CB - CA - C ANGL. DEV. = 18.1 DEGREES
REMARK 500 GLN C 5 CA - CB - CG ANGL. DEV. = 47.6 DEGREES
REMARK 500 GLN C 5 CB - CG - CD ANGL. DEV. = -19.3 DEGREES
REMARK 500 CYS C 6 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 SER C 9 CB - CA - C ANGL. DEV. = 14.6 DEGREES
REMARK 500 SER C 9 N - CA - CB ANGL. DEV. = 11.7 DEGREES
REMARK 500 CYS C 20 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 LYS D 29 CA - CB - CG ANGL. DEV. = 33.1 DEGREES
REMARK 500 LYS D 29 CB - CG - CD ANGL. DEV. = 39.4 DEGREES
REMARK 500 ALA D 30 N - CA - C ANGL. DEV. = 18.3 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 ILE A 2 -74.52 -38.32
REMARK 500 GLU A 4 -72.26 -46.51
REMARK 500 SER A 9 -131.24 -104.08
REMARK 500 GLU B 21 -56.06 -21.26
REMARK 500 SER C 9 -135.30 -66.14
REMARK 500
REMARK 500 REMARK: NULL
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 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 HOH B 44 O 90.4
REMARK 620 3 HIS B 10 NE2 97.6 167.3
REMARK 620 4 HIS B 10 NE2 97.6 90.9 97.6
REMARK 620 5 HOH B 44 O 90.9 79.6 90.4 167.3
REMARK 620 6 HOH B 44 O 167.3 79.6 90.9 90.4 79.6
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 HIS D 10 NE2
REMARK 620 2 HOH D 115 O 96.7
REMARK 620 3 HOH D 115 O 157.3 71.1
REMARK 620 4 HIS D 10 NE2 101.8 87.0 96.7
REMARK 620 5 HIS D 10 NE2 101.8 157.3 87.0 101.8
REMARK 620 6 HOH D 115 O 87.0 71.1 71.1 157.3 96.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: D1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: DIMER-FORMING RESIDUES IN MOLECULE I
REMARK 800
REMARK 800 SITE_IDENTIFIER: D2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: DIMER-FORMING RESIDUES IN MOLECULE II
REMARK 800
REMARK 800 SITE_IDENTIFIER: H1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: HEXAMER-FORMING RESIDUES IN MOLECULE I
REMARK 800
REMARK 800 SITE_IDENTIFIER: H2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: HEXAMER-FORMING RESIDUES IN MOLECULE II
REMARK 800
REMARK 800 SITE_IDENTIFIER: SI1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: SURFACE-INVARIANT RESIDUES IN MOLECULE I NOT
REMARK 800 INVOLVED IN DIMERIZATION
REMARK 800
REMARK 800 SITE_IDENTIFIER: SI2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: SURFACE-INVARIANT RESIDUES IN MOLECULE II NOT
REMARK 800 INVOLVED IN DIMERIZATION
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 31
DBREF 2INS A 1 21 UNP P01317 INS_BOVIN 85 105
DBREF 2INS B 2 30 UNP P01317 INS_BOVIN 26 54
DBREF 2INS C 1 21 UNP P01317 INS_BOVIN 85 105
DBREF 2INS D 2 30 UNP P01317 INS_BOVIN 26 54
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS ALA SER VAL CYS SER LEU
SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 B 29 VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU ALA
SEQRES 2 B 29 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR THR
SEQRES 3 B 29 PRO LYS ALA
SEQRES 1 C 21 GLY ILE VAL GLU GLN CYS CYS ALA SER VAL CYS SER LEU
SEQRES 2 C 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 D 29 VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU ALA
SEQRES 2 D 29 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR THR
SEQRES 3 D 29 PRO LYS ALA
HET ZN B 1 1
HET ZN D 31 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 HOH *184(H2 O)
HELIX 1 A11 GLY A 1 VAL A 10 1NOT IDEAL ALPH,SOME PI CNTCTS 10
HELIX 2 A12 SER A 12 GLU A 17 5NOT IDEAL 3(10) 6
HELIX 3 B11 SER B 9 GLY B 20 1NOT IDEAL ALPH,3(10) CONTCTS 12
HELIX 4 A21 GLY C 1 VAL C 10 1NOT IDEAL ALPH,SOME PI CNTCTS 10
HELIX 5 A22 SER C 12 GLU C 17 5NOT IDEAL 3(10) 6
HELIX 6 B21 SER D 9 GLY D 20 1NOT IDEAL ALPH,3(10) CONTCTS 12
SHEET 1 B 2 PHE B 24 TYR B 26 0
SHEET 2 B 2 PHE D 24 TYR D 26 -1 O TYR D 26 N PHE B 24
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.14
SSBOND 2 CYS A 7 CYS B 7 1555 1555 1.88
SSBOND 3 CYS A 20 CYS B 19 1555 1555 1.97
SSBOND 4 CYS C 6 CYS C 11 1555 1555 2.26
SSBOND 5 CYS C 7 CYS D 7 1555 1555 1.92
SSBOND 6 CYS C 20 CYS D 19 1555 1555 1.85
LINK ZN ZN B 1 NE2 HIS B 10 1555 1555 2.10
LINK ZN ZN B 1 O HOH B 44 1555 1555 2.30
LINK ZN ZN D 31 NE2 HIS D 10 1555 1555 1.94
LINK ZN ZN B 1 NE2 HIS B 10 1555 2555 2.10
LINK ZN ZN B 1 NE2 HIS B 10 1555 3555 2.10
LINK ZN ZN B 1 O HOH B 44 1555 2555 2.30
LINK ZN ZN B 1 O HOH B 44 1555 3555 2.30
LINK ZN ZN D 31 O HOH D 115 1555 2554 2.25
LINK ZN ZN D 31 O HOH D 115 1555 3554 2.25
LINK ZN ZN D 31 NE2 HIS D 10 1555 2555 1.94
LINK ZN ZN D 31 NE2 HIS D 10 1555 3555 1.94
LINK ZN ZN D 31 O HOH D 115 1555 1554 2.25
SITE 1 D1 5 VAL B 12 TYR B 16 PHE B 24 PHE B 25
SITE 2 D1 5 TYR B 26
SITE 1 D2 5 VAL D 12 TYR D 16 PHE D 24 PHE D 25
SITE 2 D2 5 TYR D 26
SITE 1 H1 6 LEU A 13 TYR A 14 GLU B 13 ALA B 14
SITE 2 H1 6 LEU B 17 VAL B 18
SITE 1 H2 6 LEU C 13 TYR C 14 GLU D 13 ALA D 14
SITE 2 H2 6 LEU D 17 VAL D 18
SITE 1 SI1 7 GLY A 1 GLU A 4 GLN A 5 CYS A 7
SITE 2 SI1 7 TYR A 19 ASN A 21 CYS B 7
SITE 1 SI2 7 GLY C 1 GLU C 4 GLN C 5 CYS C 7
SITE 2 SI2 7 TYR C 19 ASN C 21 CYS D 7
SITE 1 AC1 2 HIS B 10 HOH B 44
SITE 1 AC2 2 HIS D 10 HOH D 115
CRYST1 81.600 81.600 34.000 90.00 90.00 120.00 H 3 18
ORIGX1 0.012255 0.007075 0.000000 0.00000
ORIGX2 0.000000 0.014151 0.000000 0.00000
ORIGX3 0.000000 0.000000 0.029412 0.00000
SCALE1 0.012255 0.007075 0.000000 0.00000
SCALE2 0.000000 0.014151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029412 0.00000
MTRIX1 1 -0.880000 -0.480000 0.020000 0.00000 1
MTRIX2 1 -0.480000 0.880000 -0.020000 0.00000 1
MTRIX3 1 -0.010000 -0.030000 -1.000000 0.00000 1
(ATOM LINES ARE NOT SHOWN.)
END
