HEADER HYDROLASE(METALLOPROTEINASE) 21-APR-93 1AST
TITLE STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF
TITLE 2 ASTACINS AND ZINC-LIGATION OF COLLAGENASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASTACIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.24.21;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASTACUS ASTACUS;
SOURCE 3 ORGANISM_COMMON: BROAD-FINGERED CRAYFISH;
SOURCE 4 ORGANISM_TAXID: 6715
KEYWDS HYDROLASE(METALLOPROTEINASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR W.BODE,F.X.GOMIS-RUETH,W.STOECKER
REVDAT 3 24-FEB-09 1AST 1 VERSN
REVDAT 2 01-APR-03 1AST 1 JRNL
REVDAT 1 31-JUL-94 1AST 0
JRNL AUTH W.BODE,F.X.GOMIS-RUTH,R.HUBER,R.ZWILLING,W.STOCKER
JRNL TITL STRUCTURE OF ASTACIN AND IMPLICATIONS FOR
JRNL TITL 2 ACTIVATION OF ASTACINS AND ZINC-LIGATION OF
JRNL TITL 3 COLLAGENASES.
JRNL REF NATURE V. 358 164 1992
JRNL REFN ISSN 0028-0836
JRNL PMID 1319561
JRNL DOI 10.1038/358164A0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.X.GOMIS-RUETH,W.STOECKER,R.HUBER,R.ZWILLING,
REMARK 1 AUTH 2 W.BODE
REMARK 1 TITL REFINED 1.8 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF
REMARK 1 TITL 2 ASTACIN, A ZINC-ENDOPEPTIDASE FROM THE CRAYFISH
REMARK 1 TITL 3 ASTACUS ASTACUS L. STRUCTURE DETERMINATION,
REMARK 1 TITL 4 REFINEMENT, MOLECULAR STRUCTURE AND COMPARISON
REMARK 1 TITL 5 WITH THERMOLYSIN
REMARK 1 REF J.MOL.BIOL. V. 229 945 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.158
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 : 1591
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AST 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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 32.84000
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 65.68000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.68000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.84000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 ASN A 169 CB CG OD1 ND2
REMARK 480 LEU A 200 OXT
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 THR A 49 -73.45 -122.06
REMARK 500 SER A 72 143.16 80.39
REMARK 500 VAL A 160 -56.15 -122.69
REMARK 500 SER A 199 60.68 62.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 8 0.07 SIDE_CHAIN
REMARK 500 TYR A 67 0.07 SIDE_CHAIN
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 A 305 DISTANCE = 8.58 ANGSTROMS
REMARK 525 HOH A 389 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 417 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH A 420 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH A 422 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A 428 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A 432 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH A 447 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A 452 DISTANCE = 6.27 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 A 999 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 96 NE2
REMARK 620 2 HIS A 102 NE2 92.3
REMARK 620 3 HOH A 300 O 97.2 134.3
REMARK 620 4 HIS A 92 NE2 98.0 112.4 110.3
REMARK 620 5 TYR A 149 OH 167.7 82.9 78.4 94.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 999
DBREF 1AST A 1 200 UNP P07584 ASTA_ASTFL 50 249
SEQRES 1 A 200 ALA ALA ILE LEU GLY ASP GLU TYR LEU TRP SER GLY GLY
SEQRES 2 A 200 VAL ILE PRO TYR THR PHE ALA GLY VAL SER GLY ALA ASP
SEQRES 3 A 200 GLN SER ALA ILE LEU SER GLY MET GLN GLU LEU GLU GLU
SEQRES 4 A 200 LYS THR CYS ILE ARG PHE VAL PRO ARG THR THR GLU SER
SEQRES 5 A 200 ASP TYR VAL GLU ILE PHE THR SER GLY SER GLY CYS TRP
SEQRES 6 A 200 SER TYR VAL GLY ARG ILE SER GLY ALA GLN GLN VAL SER
SEQRES 7 A 200 LEU GLN ALA ASN GLY CYS VAL TYR HIS GLY THR ILE ILE
SEQRES 8 A 200 HIS GLU LEU MET HIS ALA ILE GLY PHE TYR HIS GLU HIS
SEQRES 9 A 200 THR ARG MET ASP ARG ASP ASN TYR VAL THR ILE ASN TYR
SEQRES 10 A 200 GLN ASN VAL ASP PRO SER MET THR SER ASN PHE ASP ILE
SEQRES 11 A 200 ASP THR TYR SER ARG TYR VAL GLY GLU ASP TYR GLN TYR
SEQRES 12 A 200 TYR SER ILE MET HIS TYR GLY LYS TYR SER PHE SER ILE
SEQRES 13 A 200 GLN TRP GLY VAL LEU GLU THR ILE VAL PRO LEU GLN ASN
SEQRES 14 A 200 GLY ILE ASP LEU THR ASP PRO TYR ASP LYS ALA HIS MET
SEQRES 15 A 200 LEU GLN THR ASP ALA ASN GLN ILE ASN ASN LEU TYR THR
SEQRES 16 A 200 ASN GLU CYS SER LEU
HET ZN A 999 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
FORMUL 3 HOH *182(H2 O)
HELIX 1 1 GLY A 5 LEU A 9 5 5
HELIX 2 2 TRP A 10 GLY A 12 5 3
HELIX 3 3 SER A 23 THR A 41 1 19
HELIX 4 4 TYR A 86 GLY A 99 1 14
HELIX 5 5 HIS A 102 ARG A 106 5 5
HELIX 6 6 ASP A 108 ASN A 111 5 4
HELIX 7 7 TYR A 117 ASN A 119 5 3
HELIX 8 8 MET A 124 ASP A 129 5 6
HELIX 9 9 ASP A 175 LYS A 179 5 5
HELIX 10 10 LEU A 183 TYR A 194 1 12
HELIX 11 11 TYR A 194 SER A 199 1 6
SHEET 1 A 2 ALA A 2 ILE A 3 0
SHEET 2 A 2 SER A 134 ARG A 135 -1 O ARG A 135 N ALA A 2
SHEET 1 B 5 ARG A 44 PRO A 47 0
SHEET 2 B 5 VAL A 14 ALA A 20 1 N ILE A 15 O ARG A 44
SHEET 3 B 5 TYR A 54 PHE A 58 1 N VAL A 55 O PRO A 16
SHEET 4 B 5 ALA A 74 LEU A 79 1 O GLN A 75 N GLU A 56
SHEET 5 B 5 CYS A 64 SER A 66 -1 N TRP A 65 O SER A 78
SHEET 1 C 2 VAL A 113 ILE A 115 0
SHEET 2 C 2 ILE A 164 PRO A 166 -1 N VAL A 165 O THR A 114
SSBOND 1 CYS A 42 CYS A 198 1555 1555 2.02
SSBOND 2 CYS A 64 CYS A 84 1555 1555 2.02
LINK ZN ZN A 999 NE2 HIS A 96 1555 1555 2.19
LINK ZN ZN A 999 NE2 HIS A 102 1555 1555 2.01
LINK ZN ZN A 999 O HOH A 300 1555 1555 2.01
LINK ZN ZN A 999 NE2 HIS A 92 1555 1555 2.03
LINK ZN ZN A 999 OH TYR A 149 1555 1555 2.54
SITE 1 CAT 4 HIS A 92 HIS A 96 HIS A 102 TYR A 149
SITE 1 AC1 5 HIS A 92 HIS A 96 HIS A 102 TYR A 149
SITE 2 AC1 5 HOH A 300
CRYST1 61.960 61.960 98.520 90.00 90.00 120.00 P 31 2 1 6
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 0.016139 0.009318 0.000000 0.00000
SCALE2 0.000000 0.018636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010150 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
