HEADER OXIDOREDUCTASE 17-MAR-95 1SXA
TITLE CRYSTAL STRUCTURE OF REDUCED BOVINE ERYTHROCYTE SUPEROXIDE
TITLE 2 DISMUTASE AT 1.9 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 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: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS OXIDOREDUCTASE, SUPEROXIDE ACCEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR W.R.RYPNIEWSKI,S.MANGANI,B.BRUNI,P.ORIOLI,M.CASATI,
AUTHOR 2 K.S.WILSON
REVDAT 2 24-FEB-09 1SXA 1 VERSN
REVDAT 1 03-JUN-95 1SXA 0
JRNL AUTH W.R.RYPNIEWSKI,S.MANGANI,B.BRUNI,P.L.ORIOLI,
JRNL AUTH 2 M.CASATI,K.S.WILSON
JRNL TITL CRYSTAL STRUCTURE OF REDUCED BOVINE ERYTHROCYTE
JRNL TITL 2 SUPEROXIDE DISMUTASE AT 1.9 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 251 282 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7643403
JRNL DOI 10.1006/JMBI.1995.0434
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 25783
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : NULL
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 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 : 2186
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 299
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) : 0.015 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.043 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.043 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.014 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.182 ; 0.200
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.191 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.349 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.191 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 2.600 ; 5.000
REMARK 3 STAGGERED (DEGREES) : 15.900; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.500 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.500 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.300 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.900 ; 6.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: GLU 119 (BOTH SUBUNITS) APPEARS ON
REMARK 3 THE ELECTRON DENSITY TO BE COVALENTLY MODIFIED. THE NATURE OF
REMARK 3 THE MODIFICATION IS UNKNOWN AND IT HAS NOT BEEN MODELLED. THE
REMARK 3 APPEARANCE OF THE ELECTRON DENSITY IS CONSISTENT WITH OE1
REMARK 3 REPLACED BY A HYDROXYLAMINE GROUP. THE MODIFICATION IS ALSO
REMARK 3 OBSERVED IN THE STRUCTURE OF NATIVE, OXIDIZED SOD. THEREFORE,
REMARK 3 IT CANNOT BE AN ARTIFACT OF THE TREATMENT WITH DITHIONITE,
REMARK 3 USED IN REDUCING THE ENZYME. THE POSITION OF THE MODIFICATION
REMARK 3 RELATIVE TO THE ACTIVE SITE SUGGESTS A ROLE IN THE REACTION
REMARK 3 MECHANISM. SEE THE PAPER CITED ON JRNL RECORDS ABOVE FOR
REMARK 3 DETAILS. RESIDUES WITH POOR ELECTRON DENSITY: LYS A 3, LYS A
REMARK 3 23, LYS A 89. A NUMBER OF CLOSE CONTACTS OCCURS BETWEEN
REMARK 3 SOLVENT MOLECULES. INSPECTION OF THE ELECTRON DENSITY CONFIRMS
REMARK 3 THAT THESE SITES ARE REAL BUT PROBABLY CORRESPOND TO PARTIALLY
REMARK 3 OCCUPIED, ALTERNATIVE SOLVENT SITES.
REMARK 4
REMARK 4 1SXA 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 : 16-NOV-92
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26203
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.07300
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 (%): 57.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
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 23.94500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.07500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.57000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.07500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.94500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.57000
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:
REMARK 300 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 1 .. A 151 B 1 .. B 151 0.295
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: 1620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 COMPND
REMARK 400 REDUCED WITH SODIUM DITHIONITE TO CU(I).
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 CE NZ
REMARK 480 LYS A 23 CE NZ
REMARK 480 LYS A 89 CD 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 187 O HOH A 252 2.15
REMARK 500 O HOH B 207 O HOH B 266 2.16
REMARK 500 OE2 GLU A 130 O HOH A 164 2.18
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 LYS A 3 CD LYS A 3 CE -0.414
REMARK 500 LYS A 89 CG LYS A 89 CD -0.222
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 LYS A 3 CG - CD - CE ANGL. DEV. = 27.6 DEGREES
REMARK 500 LYS A 3 CD - CE - NZ ANGL. DEV. = 14.9 DEGREES
REMARK 500 LYS A 23 CD - CE - NZ ANGL. DEV. = -15.6 DEGREES
REMARK 500 HIS A 61 CE1 - NE2 - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 HIS A 78 CE1 - NE2 - CD2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP A 81 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP A 123 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 141 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ASP B 40 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASN B 51 CB - CG - OD1 ANGL. DEV. = -13.6 DEGREES
REMARK 500 LYS B 68 CB - CG - CD ANGL. DEV. = 19.2 DEGREES
REMARK 500 ARG B 77 CD - NE - CZ ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG B 77 NE - CZ - NH2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 96 CB - CG - OD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ASP B 96 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG B 113 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 GLU B 119 CG - CD - OE1 ANGL. DEV. = 16.0 DEGREES
REMARK 500 GLU B 119 CG - CD - OE2 ANGL. DEV. = -22.8 DEGREES
REMARK 500 LYS B 120 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 ASP B 122 CB - CG - OD1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 126 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
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 240 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B 279 DISTANCE = 5.23 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 152 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 44 ND1
REMARK 620 2 HIS A 46 NE2 145.0
REMARK 620 3 HIS A 118 NE2 96.7 98.2
REMARK 620 4 HIS A 61 NE2 83.5 93.7 158.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 61 ND1
REMARK 620 2 HIS A 78 ND1 109.1
REMARK 620 3 HIS A 69 ND1 110.2 118.9
REMARK 620 4 ASP A 81 OD1 110.9 111.9 95.1
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 HOH B 164 O
REMARK 620 2 HIS B 118 NE2 93.1
REMARK 620 3 HIS B 61 NE2 82.2 170.0
REMARK 620 4 HIS B 46 NE2 91.6 99.6 89.5
REMARK 620 5 HIS B 44 ND1 128.8 87.2 88.8 138.9
REMARK 620 N 1 2 3 4
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 61 ND1
REMARK 620 2 HIS B 69 ND1 108.6
REMARK 620 3 ASP B 81 OD1 102.0 92.4
REMARK 620 4 HIS B 78 ND1 109.1 120.3 122.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, CHAIN A
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, CHAIN B
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 152
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 153
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 1SXA A 1 151 UNP P00442 SODC_BOVIN 1 151
DBREF 1SXA B 1 151 UNP P00442 SODC_BOVIN 1 151
SEQRES 1 A 151 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 A 151 VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP THR
SEQRES 3 A 151 VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU GLY
SEQRES 4 A 151 ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN THR
SEQRES 5 A 151 GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO LEU
SEQRES 6 A 151 SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG HIS
SEQRES 7 A 151 VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN GLY
SEQRES 8 A 151 VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER LEU
SEQRES 9 A 151 SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL VAL
SEQRES 10 A 151 HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN GLU
SEQRES 11 A 151 GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU ALA
SEQRES 12 A 151 CYS GLY VAL ILE GLY ILE ALA LYS
SEQRES 1 B 151 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 B 151 VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP THR
SEQRES 3 B 151 VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU GLY
SEQRES 4 B 151 ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN THR
SEQRES 5 B 151 GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO LEU
SEQRES 6 B 151 SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG HIS
SEQRES 7 B 151 VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN GLY
SEQRES 8 B 151 VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER LEU
SEQRES 9 B 151 SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL VAL
SEQRES 10 B 151 HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN GLU
SEQRES 11 B 151 GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU ALA
SEQRES 12 B 151 CYS GLY VAL ILE GLY ILE ALA LYS
HET CU A 152 1
HET ZN A 153 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 *299(H2 O)
HELIX 1 1 THR A 56 ALA A 58 5 3
HELIX 2 2 GLU A 131 THR A 135 5 5
HELIX 3 3 GLY B 54 ALA B 58 5 5
HELIX 4 4 GLU B 130 THR B 135 5 6
SHEET 1 A 4 LYS A 3 LEU A 8 0
SHEET 2 A 4 GLN A 15 LYS A 23 -1 N PHE A 20 O ALA A 4
SHEET 3 A 4 THR A 26 THR A 34 -1 N THR A 34 O GLN A 15
SHEET 4 A 4 ALA A 93 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 MET A 115
SHEET 1 D 4 LYS B 3 LEU B 8 0
SHEET 2 D 4 GLN B 15 LYS B 23 -1 N PHE B 20 O ALA B 4
SHEET 3 D 4 THR B 26 THR B 34 -1 N THR B 34 O GLN B 15
SHEET 4 D 4 ALA B 93 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 MET B 115
SSBOND 1 CYS A 55 CYS A 144 1555 1555 2.03
SSBOND 2 CYS B 55 CYS B 144 1555 1555 2.06
LINK CU CU A 152 ND1 HIS A 44 1555 1555 2.20
LINK CU CU A 152 NE2 HIS A 46 1555 1555 2.24
LINK CU CU A 152 NE2 HIS A 118 1555 1555 2.17
LINK CU CU A 152 NE2 HIS A 61 1555 1555 2.27
LINK ZN ZN A 153 ND1 HIS A 61 1555 1555 2.07
LINK ZN ZN A 153 ND1 HIS A 78 1555 1555 2.20
LINK ZN ZN A 153 ND1 HIS A 69 1555 1555 2.25
LINK ZN ZN A 153 OD1 ASP A 81 1555 1555 1.83
LINK CU CU B 152 O HOH B 164 1555 1555 2.46
LINK CU CU B 152 NE2 HIS B 118 1555 1555 2.10
LINK CU CU B 152 NE2 HIS B 61 1555 1555 2.01
LINK CU CU B 152 NE2 HIS B 46 1555 1555 2.27
LINK CU CU B 152 ND1 HIS B 44 1555 1555 2.12
LINK ZN ZN B 153 ND1 HIS B 61 1555 1555 2.17
LINK ZN ZN B 153 ND1 HIS B 69 1555 1555 2.30
LINK ZN ZN B 153 OD1 ASP B 81 1555 1555 1.90
LINK ZN ZN B 153 ND1 HIS B 78 1555 1555 1.91
SITE 1 CAA 9 HIS A 44 HIS A 46 HIS A 61 HIS A 69
SITE 2 CAA 9 HIS A 78 ASP A 81 HIS A 118 CU A 152
SITE 3 CAA 9 ZN A 153
SITE 1 CAB 9 HIS B 44 HIS B 46 HIS B 61 HIS B 69
SITE 2 CAB 9 HIS B 78 ASP B 81 HIS B 118 CU B 152
SITE 3 CAB 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 209
SITE 1 AC2 4 HIS A 61 HIS A 69 HIS A 78 ASP A 81
SITE 1 AC3 5 HIS B 44 HIS B 46 HIS B 61 HIS B 118
SITE 2 AC3 5 HOH B 164
SITE 1 AC4 5 HIS B 61 HIS B 69 HIS B 78 ASP B 81
SITE 2 AC4 5 LYS B 134
CRYST1 47.890 51.140 148.150 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 0.020881 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006750 0.00000
MTRIX1 1 -0.599530 -0.795050 0.091960 24.19712 1
MTRIX2 1 -0.791130 0.571300 -0.218460 28.25224 1
MTRIX3 1 0.121150 -0.203730 -0.971500 119.80469 1
(ATOM LINES ARE NOT SHOWN.)
END
