HEADER HYDROLASE(METALLOPROTEINASE) 24-JUN-99 1QJI
TITLE STRUCTURE OF ASTACIN WITH A TRANSITION-STATE ANALOGUE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASTACIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: CRAYFISH SMALL MOLECULE PROTEINASE;
COMPND 6 EC: 3.4.24.21;
COMPND 7 OTHER_DETAILS: IN COMPLEX WITH A BOUND TRANSITION-STATE ANALOGUE
COMPND 8 PHOSPHINIC PSEUDOPEPTIDE CARBOBENZOXY-PRO-LYS-PHE-Y(PO2)-ALA-PRO-OME
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASTACUS FLUVIATILIS;
SOURCE 3 ORGANISM_COMMON: BROAD-FINGERED CRAYFISH;
SOURCE 4 ORGANISM_TAXID: 6715;
SOURCE 5 ORGAN: MIDGUT GLAND;
SOURCE 6 CELL: F-CELL;
SOURCE 7 SECRETION: DIGESTIVE FLUID
KEYWDS HYDROLASE(METALLOPROTEINASE), ASTACINS, METZINCINS
EXPDTA X-RAY DIFFRACTION
AUTHOR F.GRAMS,W.BODE,W.STOCKER
REVDAT 6 13-DEC-23 1QJI 1 REMARK
REVDAT 5 08-MAY-19 1QJI 1 REMARK
REVDAT 4 12-JUL-17 1QJI 1
REVDAT 3 05-JUL-17 1QJI 1 REMARK
REVDAT 2 24-FEB-09 1QJI 1 VERSN
REVDAT 1 21-JAN-00 1QJI 0
JRNL AUTH F.GRAMS,V.DIVE,A.YIOTAKIS,I.YIALLOUROS,S.VASSILIOU,
JRNL AUTH 2 R.ZWILLING,W.BODE,W.STOCKER
JRNL TITL STRUCTURE OF ASTACIN WITH A TRANSITION-STATE ANALOGUE
JRNL TITL 2 INHIBITOR
JRNL REF NAT.STRUCT.BIOL. V. 3 671 1996
JRNL REFN ISSN 1072-8368
JRNL PMID 8756323
JRNL DOI 10.1038/NSB0896-671
REMARK 2
REMARK 2 RESOLUTION. 2.14 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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 70.0
REMARK 3 NUMBER OF REFLECTIONS : 7942
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.164
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 : 1590
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.44
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.700
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 1QJI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1290002853.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-94
REMARK 200 TEMPERATURE (KELVIN) : 289.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.14
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : COLLIMATOR PINHOLES
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : BRUKER NONIUS FAST
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNESS
REMARK 200 DATA SCALING SOFTWARE : PROTEIN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12071
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 8.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.6
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.10900
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) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 30.4
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1AST
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOUR DIFFUSION PH 7.0,
REMARK 280 1M AMMONIUM SULFATE, PH 7.00, VAPOR DIFFUSION, HANGING DROP
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 33.18667
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 66.37333
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 66.37333
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 33.18667
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 THE CDNA ENCODES TWO ADDITIONAL C-TERMINAL RESIDUES
REMARK 400 ARG-HIS THAT ARE CLEAVED OFF POSTTRANSLATIONALLY AND
REMARK 400 NOT PRESENT IN THE PROTEIN STUDIED
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 HG1 THR A 59 H1 HOH A 2066 1.30
REMARK 500 HH11 ARG A 106 H1 HOH A 2002 1.30
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 HD21 ASN A 111 HD21 ASN A 111 4555 1.22
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 SER A 72 132.06 74.35
REMARK 500 GLN A 80 131.54 -37.79
REMARK 500 ASN A 82 78.55 -111.17
REMARK 500 HIS A 104 0.33 -67.98
REMARK 500 VAL A 160 -58.16 -120.22
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 A2004 DISTANCE = 5.82 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PKF A1202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AST RELATED DB: PDB
REMARK 900 RELATED ID: 1IAA RELATED DB: PDB
REMARK 900 RELATED ID: 1IAB RELATED DB: PDB
REMARK 900 RELATED ID: 1IAC RELATED DB: PDB
REMARK 900 RELATED ID: 1IAD RELATED DB: PDB
REMARK 900 RELATED ID: 1IAE RELATED DB: PDB
REMARK 900 RELATED ID: 1QJJ RELATED DB: PDB
DBREF 1QJI 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 A1201 1
HET PKF A1202 58
HETNAM ZN ZINC ION
HETNAM PKF CARBOBENZOXY-PRO-LYS-PHE-Y(PO2)-ALA-PRO-OME
FORMUL 2 ZN ZN 2+
FORMUL 3 PKF C36 H52 N6 O9 P 1+
FORMUL 4 HOH *165(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 ASP A 121 ASP A 129 5 9
HELIX 9 9 ASP A 175 LYS A 179 5 5
HELIX 10 10 LEU A 183 TYR A 194 1 12
SHEET 1 A 5 ARG A 44 PRO A 47 0
SHEET 2 A 5 VAL A 14 PHE A 19 1 N ILE A 15 O ARG A 44
SHEET 3 A 5 TYR A 54 PHE A 58 1 N VAL A 55 O THR A 18
SHEET 4 A 5 ALA A 74 LEU A 79 1 N GLN A 75 O TYR A 54
SHEET 5 A 5 CYS A 64 SER A 66 -1 N TRP A 65 O SER A 78
SHEET 1 B 2 VAL A 113 ILE A 115 0
SHEET 2 B 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 2.01
SSBOND 2 CYS A 64 CYS A 84 1555 1555 2.02
SITE 1 AC1 4 HIS A 92 HIS A 96 HIS A 102 PKF A1202
SITE 1 AC2 17 CYS A 64 TRP A 65 SER A 66 TYR A 67
SITE 2 AC2 17 GLY A 83 HIS A 92 GLU A 93 HIS A 96
SITE 3 AC2 17 HIS A 102 TYR A 149 SER A 153 ASP A 175
SITE 4 AC2 17 ZN A1201 HOH A2070 HOH A2085 HOH A2147
SITE 5 AC2 17 HOH A2165
CRYST1 61.170 61.170 99.560 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 0.016348 0.009438 0.000000 0.00000
SCALE2 0.000000 0.018877 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010044 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
