HEADER OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 14-MAR-95 1XSO
TITLE THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN
TITLE 2 SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY
TITLE 3 AT 1.5 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER,ZINC SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKK233-2 TRC PROMOTER
KEYWDS OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR K.DJINOVIC CARUGO,A.CODA,A.BATTISTONI,M.T.CARRI,
AUTHOR 2 F.POLTICELLI,A.DESIDERI,G.ROTILIO,K.S.WILSON,M.BOLOGNESI
REVDAT 3 24-FEB-09 1XSO 1 VERSN
REVDAT 2 03-MAY-99 1XSO 1 JRNL
REVDAT 1 10-JUL-95 1XSO 0
JRNL AUTH K.DJINOVIC CARUGO,A.BATTISTONI,M.T.CARRI,
JRNL AUTH 2 F.POLTICELLI,A.DESIDERI,G.ROTILIO,A.CODA,
JRNL AUTH 3 K.S.WILSON,M.BOLOGNESI
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS
JRNL TITL 2 CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY
JRNL TITL 3 CRYSTALLOGRAPHY AT 1.5 A RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 52 176 1996
JRNL REFN ISSN 0907-4449
JRNL PMID 15299740
JRNL DOI 10.1107/S0907444995007608
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.BORDO,K.DJINOVIC,K.M.BOLOGNESI
REMARK 1 TITL CONSERVED PATTERNS IN THE CU,ZN SUPEROXIDE
REMARK 1 TITL 2 DISMUTASE FAMILY
REMARK 1 REF J.MOL.BIOL. V. 238 366 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.DJINOVIC CARUGO,K.F.POLTICELLI,A.DESIDERI,
REMARK 1 AUTH 2 G.ROTILIO,K.S.WILSON,M.BOLOGNESI
REMARK 1 TITL CRYSTALLOGRAPHIC STUDY OF AZIDE-INHIBITED BOVINE
REMARK 1 TITL 2 CU,ZN SUPEROXIDE DISMUTASE
REMARK 1 REF J.MOL.BIOL. V. 240 179 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.DJINOVIC CARUGO,K.A.BATTISTONI,M.T.CARRI,
REMARK 1 AUTH 2 F.POLTICELLI,A.DESIDERI,G.ROTILIO,A.CODA,
REMARK 1 AUTH 3 M.BOLOGNESI
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CYANIDE-INHIBITED XENOPUS
REMARK 1 TITL 2 LAEVIS CU,ZN SUPEROXIDE DISMUTASE AT 98 K
REMARK 1 REF FEBS LETT. V. 349 93 1994
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 4
REMARK 1 AUTH K.DJINOVIC CARUGO,K.C.COLLYER,A.CODA,M.T.CARRI,
REMARK 1 AUTH 2 A.BATTISTONI,G.BOTARO,F.POLTICELLI,A.DESIDERI,
REMARK 1 AUTH 3 M.BOLOGNESI
REMARK 1 TITL CRYSTALLISATION AND PRELIMINARY CRYSTALLOGRAPHIC
REMARK 1 TITL 2 ANALYSIS OF RECOMBINANT XENOPUS LAEVIS CU,ZN
REMARK 1 TITL 3 SUPEROXIDE DISMUTASE B
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 194 1008 1993
REMARK 1 REFN ISSN 0006-291X
REMARK 1 REFERENCE 5
REMARK 1 AUTH K.DJINOVIC,G.GATTI,L.ANTOLINI,G.PELOSI,A.DESIDERI,
REMARK 1 AUTH 2 M.FALCONI,F.MARMOCCHI,G.ROTILIO,M.BOLOGNESI
REMARK 1 TITL CRYSTAL STRUCTURE OF YEAST CU,ZN SUPEROXIDE
REMARK 1 TITL 2 DISMUTASE
REMARK 1 REF J.MOL.BIOL. V. 225 791 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ, X-PLOR, SHELXL-93
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 49209
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.104
REMARK 3 R VALUE (WORKING SET) : 0.104
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2187
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.580 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.530 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.520 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.920 ; 6.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUE 24 IS IN POOR ELECTRON
REMARK 3 DENSITY.
REMARK 4
REMARK 4 1XSO 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 : 18-AUG-93
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49209
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.980
REMARK 200 R MERGE (I) : 0.07800
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 (%): 49.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 36.72500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.38000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.47000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.38000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.72500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.47000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: MTRIX
REMARK 300 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 300 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300 SECOND.
REMARK 300
REMARK 300 APPLIED TO TRANSFORMED TO
REMARK 300 MTRIX RESIDUES RESIDUES RMSD
REMARK 300 M1 A 2 .. A 151 B 2 .. B 151 0.279
REMARK 300
REMARK 300 CALCULATED FOR C-ALPHA ATOMS
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: 1590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 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 LYS A 3 NZ
REMARK 480 LYS A 15 CD NZ
REMARK 480 GLN A 23 OE1 NE2
REMARK 480 ASP A 24 CB
REMARK 480 GLU A 25 CB CG CD OE1 OE2
REMARK 480 GLU A 34 CD OE1 OE2
REMARK 480 MET A 56 CG
REMARK 480 GLN A 94 CG
REMARK 480 LYS A 105 CD
REMARK 480 LYS A 120 CE
REMARK 480 LYS A 126 CD CE NZ
REMARK 480 LYS B 3 NZ
REMARK 480 ASP B 13 OD2
REMARK 480 LYS B 15 CE NZ
REMARK 480 GLN B 23 CG CD OE1 NE2
REMARK 480 ASP B 24 CG OD1 OD2
REMARK 480 GLU B 30 OE2
REMARK 480 LYS B 32 NZ
REMARK 480 ASN B 66 ND2
REMARK 480 LYS B 96 CD CE NZ
REMARK 480 LYS B 105 CD CE NZ
REMARK 480 LYS B 120 NZ
REMARK 480 LYS B 126 CE NZ
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 O HOH A 167 O HOH A 263 2.09
REMARK 500 O HOH B 222 O HOH B 298 2.10
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 CYS A 6 CB CYS A 6 SG -0.103
REMARK 500 CYS A 6 CB CYS A 6 SG -0.098
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 CYS A 6 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 CYS A 6 N - CA - CB ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 CYS B 6 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 CYS B 6 N - CA - CB ANGL. DEV. = -19.0 DEGREES
REMARK 500 LEU B 8 N - CA - CB ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASN B 51 CB - CA - C ANGL. DEV. = -16.1 DEGREES
REMARK 500 VAL B 92 N - CA - CB ANGL. DEV. = 16.0 DEGREES
REMARK 500 SER B 100 N - CA - CB ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG B 141 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 SER B 150 N - CA - CB ANGL. DEV. = -13.2 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 ASP A 24 -138.67 56.46
REMARK 500 ASN A 53 51.00 -115.30
REMARK 500 ASP B 24 -136.64 50.71
REMARK 500 ASN B 63 58.35 -145.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 CYS A 6 23.6 L L OUTSIDE RANGE
REMARK 500 ASP A 38 23.4 L L OUTSIDE RANGE
REMARK 500 ASN A 51 20.7 L L OUTSIDE RANGE
REMARK 500 MET A 56 24.3 L L OUTSIDE RANGE
REMARK 500 CYS B 6 45.2 L L OUTSIDE RANGE
REMARK 500 LEU B 8 24.3 L L OUTSIDE RANGE
REMARK 500 VAL B 92 19.9 L L OUTSIDE RANGE
REMARK 500 SER B 100 19.0 L L OUTSIDE RANGE
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 253 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH A 275 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH A 286 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH A 314 DISTANCE = 5.43 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 CU A 1 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 118 NE2
REMARK 620 2 HIS A 46 NE2 99.9
REMARK 620 3 HIS A 44 ND1 90.6 139.7
REMARK 620 4 HIS A 61 NE2 166.3 90.5 87.1
REMARK 620 5 HOH A 167 O 87.3 100.6 118.8 82.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 152 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 81 OD1
REMARK 620 2 HIS A 78 ND1 112.3
REMARK 620 3 HIS A 69 ND1 96.7 121.8
REMARK 620 4 HIS A 61 ND1 105.0 109.4 109.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 44 ND1
REMARK 620 2 HOH B 159 O 126.0
REMARK 620 3 HOH B 154 O 89.0 38.4
REMARK 620 4 HIS B 118 NE2 91.8 89.2 79.5
REMARK 620 5 HIS B 61 NE2 86.4 80.7 86.7 166.1
REMARK 620 6 HIS B 46 NE2 137.8 95.3 133.2 97.8 92.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 69 ND1
REMARK 620 2 HIS B 78 ND1 122.4
REMARK 620 3 ASP B 81 OD1 97.2 111.2
REMARK 620 4 HIS B 61 ND1 109.4 110.5 104.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: A
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: B
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 152
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 152
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 153
DBREF 1XSO A 2 151 UNP P15107 SODC2_XENLA 1 150
DBREF 1XSO B 2 151 UNP P15107 SODC2_XENLA 1 150
SEQADV 1XSO SER A 60 UNP P15107 PRO 60 CONFLICT
SEQADV 1XSO SER B 60 UNP P15107 PRO 60 CONFLICT
SEQRES 1 A 150 VAL LYS ALA VAL CYS VAL LEU ALA GLY SER GLY ASP VAL
SEQRES 2 A 150 LYS GLY VAL VAL HIS PHE GLU GLN GLN ASP GLU GLY ALA
SEQRES 3 A 150 VAL SER VAL GLU GLY LYS ILE GLU GLY LEU THR ASP GLY
SEQRES 4 A 150 LEU HIS GLY PHE HIS ILE HIS VAL PHE GLY ASP ASN THR
SEQRES 5 A 150 ASN GLY CYS MET SER ALA GLY SER HIS PHE ASN PRO GLU
SEQRES 6 A 150 ASN LYS ASN HIS GLY ALA PRO GLY ASP THR ASP ARG HIS
SEQRES 7 A 150 VAL GLY ASP LEU GLY ASN VAL THR ALA GLU GLY GLY VAL
SEQRES 8 A 150 ALA GLN PHE LYS ILE THR ASP SER LEU ILE SER LEU LYS
SEQRES 9 A 150 GLY PRO ASN SER ILE ILE GLY ARG THR ALA VAL VAL HIS
SEQRES 10 A 150 GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY ASN ASP GLU
SEQRES 11 A 150 SER LEU LYS THR GLY ASN ALA GLY GLY ARG LEU ALA CYS
SEQRES 12 A 150 GLY VAL ILE GLY TYR SER PRO
SEQRES 1 B 150 VAL LYS ALA VAL CYS VAL LEU ALA GLY SER GLY ASP VAL
SEQRES 2 B 150 LYS GLY VAL VAL HIS PHE GLU GLN GLN ASP GLU GLY ALA
SEQRES 3 B 150 VAL SER VAL GLU GLY LYS ILE GLU GLY LEU THR ASP GLY
SEQRES 4 B 150 LEU HIS GLY PHE HIS ILE HIS VAL PHE GLY ASP ASN THR
SEQRES 5 B 150 ASN GLY CYS MET SER ALA GLY SER HIS PHE ASN PRO GLU
SEQRES 6 B 150 ASN LYS ASN HIS GLY ALA PRO GLY ASP THR ASP ARG HIS
SEQRES 7 B 150 VAL GLY ASP LEU GLY ASN VAL THR ALA GLU GLY GLY VAL
SEQRES 8 B 150 ALA GLN PHE LYS ILE THR ASP SER LEU ILE SER LEU LYS
SEQRES 9 B 150 GLY PRO ASN SER ILE ILE GLY ARG THR ALA VAL VAL HIS
SEQRES 10 B 150 GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY ASN ASP GLU
SEQRES 11 B 150 SER LEU LYS THR GLY ASN ALA GLY GLY ARG LEU ALA CYS
SEQRES 12 B 150 GLY VAL ILE GLY TYR SER PRO
HET CU A 1 1
HET ZN A 152 1
HET CU B 152 1
HET ZN B 153 1
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
FORMUL 3 CU 2(CU 2+)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 7 HOH *350(H2 O)
HELIX 1 1 GLY A 54 ALA A 58 5 5
HELIX 2 2 GLU A 131 THR A 135 5 5
HELIX 3 3 GLY B 54 SER B 57 5 4
HELIX 4 4 SER B 132 THR B 135 1 4
SHEET 1 A 4 LYS A 3 LEU A 8 0
SHEET 2 A 4 LYS A 15 GLN A 22 -1 N PHE A 20 O ALA A 4
SHEET 3 A 4 VAL A 27 GLU A 34 -1 N GLU A 34 O LYS A 15
SHEET 4 A 4 VAL A 92 ASP A 99 -1 N ASP A 99 O VAL A 27
SHEET 1 B 2 GLY A 39 GLY A 42 0
SHEET 2 B 2 ASN A 84 ALA A 87 -1 N ALA A 87 O GLY A 39
SHEET 1 C 3 PHE A 43 HIS A 46 0
SHEET 2 C 3 THR A 114 HIS A 118 -1 N VAL A 116 O HIS A 44
SHEET 3 C 3 ARG A 141 VAL A 146 -1 N GLY A 145 O ALA A 115
SHEET 1 D 4 LYS B 3 LEU B 8 0
SHEET 2 D 4 LYS B 15 GLU B 21 -1 N PHE B 20 O ALA B 4
SHEET 3 D 4 VAL B 27 GLU B 34 -1 N GLU B 34 O LYS B 15
SHEET 4 D 4 VAL B 92 ASP B 99 -1 N ASP B 99 O VAL B 27
SHEET 1 E 2 GLY B 39 GLY B 42 0
SHEET 2 E 2 ASN B 84 ALA B 87 -1 N ALA B 87 O GLY B 39
SHEET 1 F 3 PHE B 43 HIS B 46 0
SHEET 2 F 3 THR B 114 HIS B 118 -1 N VAL B 116 O HIS B 44
SHEET 3 F 3 ARG B 141 VAL B 146 -1 N GLY B 145 O ALA B 115
SSBOND 1 CYS A 55 CYS A 144 1555 1555 2.02
SSBOND 2 CYS B 55 CYS B 144 1555 1555 2.04
LINK CU CU A 1 NE2 HIS A 118 1555 1555 2.11
LINK CU CU A 1 NE2 HIS A 46 1555 1555 2.21
LINK CU CU A 1 ND1 HIS A 44 1555 1555 2.00
LINK CU CU A 1 NE2 HIS A 61 1555 1555 2.08
LINK CU CU A 1 O HOH A 167 1555 1555 2.26
LINK ZN ZN A 152 OD1 ASP A 81 1555 1555 2.00
LINK ZN ZN A 152 ND1 HIS A 78 1555 1555 2.06
LINK ZN ZN A 152 ND1 HIS A 69 1555 1555 2.07
LINK ZN ZN A 152 ND1 HIS A 61 1555 1555 2.04
LINK CU CU B 152 ND1 HIS B 44 1555 1555 2.02
LINK CU CU B 152 O HOH B 159 1555 1555 2.40
LINK CU CU B 152 O HOH B 154 1555 1555 2.49
LINK CU CU B 152 NE2 HIS B 118 1555 1555 2.07
LINK CU CU B 152 NE2 HIS B 61 1555 1555 2.08
LINK CU CU B 152 NE2 HIS B 46 1555 1555 2.20
LINK ZN ZN B 153 ND1 HIS B 69 1555 1555 2.04
LINK ZN ZN B 153 ND1 HIS B 78 1555 1555 2.00
LINK ZN ZN B 153 OD1 ASP B 81 1555 1555 1.97
LINK ZN ZN B 153 ND1 HIS B 61 1555 1555 2.02
SITE 1 A 9 HIS A 44 HIS A 46 HIS A 61 HIS A 118
SITE 2 A 9 HIS A 69 HIS A 78 ASP A 81 CU A 1
SITE 3 A 9 ZN A 152
SITE 1 B 9 HIS B 44 HIS B 46 HIS B 61 HIS B 118
SITE 2 B 9 HIS B 69 HIS B 78 ASP B 81 CU B 152
SITE 3 B 9 ZN B 153
SITE 1 AC1 5 HIS A 44 HIS A 46 HIS A 61 HIS A 118
SITE 2 AC1 5 HOH A 167
SITE 1 AC2 4 HIS A 61 HIS A 69 HIS A 78 ASP A 81
SITE 1 AC3 6 HIS B 44 HIS B 46 HIS B 61 HIS B 118
SITE 2 AC3 6 HOH B 154 HOH B 159
SITE 1 AC4 4 HIS B 61 HIS B 69 HIS B 78 ASP B 81
CRYST1 73.450 68.940 58.760 90.00 90.00 90.00 P 21 21 21 8
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 0.013615 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017018 0.00000
MTRIX1 1 0.987830 -0.010290 -0.155220 1.43777 1
MTRIX2 1 -0.008360 -0.999880 0.013070 33.15571 1
MTRIX3 1 -0.155330 -0.011610 -0.987790 17.07902 1
(ATOM LINES ARE NOT SHOWN.)
END
