HEADER OXIDOREDUCTASE 02-APR-03 1OEZ
TITLE ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: W, X, Y, Z;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: EG118;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: YEP351
KEYWDS OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,J.S.ELAM,
AUTHOR 2 P.J.HART,L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN
REVDAT 3 13-JUL-11 1OEZ 1 VERSN
REVDAT 2 24-FEB-09 1OEZ 1 VERSN
REVDAT 1 29-MAY-03 1OEZ 0
JRNL AUTH J.S.ELAM,A.B.TAYLOR,R.W.STRANGE,S.ANTONYUK,P.DOUCETTE,
JRNL AUTH 2 J.RODRIGUEZ,S.S.HASNAIN,L.J.HAYWARD,J.S.VALENTINE,
JRNL AUTH 3 T.O.YEATES,P.J.HART
JRNL TITL AMYLOID-LIKE FILAMENTS AND WATER-FILLED NANOTUBES FORMED BY
JRNL TITL 2 SOD1 MUTANT PROTEINS LINKED TO FAMILIAL ALS
JRNL REF NAT.STRUCT.BIOL. V. 10 461 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 12754496
JRNL DOI 10.1038/NSB935
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 33576
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1774
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2326
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 124
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3576
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 277
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.61000
REMARK 3 B22 (A**2) : -2.61000
REMARK 3 B33 (A**2) : 5.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.210
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.174
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.548
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3640 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4917 ; 1.612 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 484 ; 4.514 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 588 ;17.442 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 567 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2736 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1486 ; 0.218 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 499 ; 0.166 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 8 ; 0.194 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 38 ; 0.183 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.200 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2415 ; 0.799 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3834 ; 1.491 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1225 ; 2.302 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1083 ; 3.625 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 65
REMARK 3 RESIDUE RANGE : Y 78 Y 125
REMARK 3 RESIDUE RANGE : Y 142 Y 153
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4610 56.7720 3.7120
REMARK 3 T TENSOR
REMARK 3 T11: 0.2703 T22: 0.2386
REMARK 3 T33: 0.0002 T12: -0.0342
REMARK 3 T13: -0.0054 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 2.6630 L22: 3.3396
REMARK 3 L33: 2.1324 L12: -0.2456
REMARK 3 L13: 0.0620 L23: 0.0270
REMARK 3 S TENSOR
REMARK 3 S11: 0.0312 S12: 0.0815 S13: 0.1936
REMARK 3 S21: -0.0571 S22: -0.0249 S23: -0.0198
REMARK 3 S31: -0.2065 S32: 0.1394 S33: -0.0063
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 65
REMARK 3 RESIDUE RANGE : Z 78 Z 125
REMARK 3 RESIDUE RANGE : Z 142 Z 153
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0380 32.2460 3.8350
REMARK 3 T TENSOR
REMARK 3 T11: 0.2953 T22: 0.2356
REMARK 3 T33: 0.0171 T12: 0.0518
REMARK 3 T13: -0.0004 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 2.4959 L22: 2.9681
REMARK 3 L33: 2.3894 L12: -0.3256
REMARK 3 L13: 0.0540 L23: 0.0863
REMARK 3 S TENSOR
REMARK 3 S11: 0.0056 S12: -0.0494 S13: -0.2656
REMARK 3 S21: 0.1451 S22: 0.0093 S23: 0.0338
REMARK 3 S31: 0.2031 S32: 0.1502 S33: -0.0149
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 65
REMARK 3 RESIDUE RANGE : W 78 W 125
REMARK 3 RESIDUE RANGE : W 142 W 153
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9400 38.6770 4.0880
REMARK 3 T TENSOR
REMARK 3 T11: 0.2860 T22: 0.2314
REMARK 3 T33: 0.0065 T12: -0.0336
REMARK 3 T13: 0.0080 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 2.4246 L22: 2.6938
REMARK 3 L33: 2.3857 L12: -0.3369
REMARK 3 L13: -0.0310 L23: -0.1111
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: 0.0279 S13: -0.2627
REMARK 3 S21: -0.0169 S22: -0.0168 S23: 0.0135
REMARK 3 S31: 0.2122 S32: -0.1556 S33: 0.0208
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 65
REMARK 3 RESIDUE RANGE : X 78 X 125
REMARK 3 RESIDUE RANGE : X 142 X 153
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5450 63.1830 3.4550
REMARK 3 T TENSOR
REMARK 3 T11: 0.3023 T22: 0.2163
REMARK 3 T33: 0.0103 T12: 0.0502
REMARK 3 T13: -0.0073 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 2.8193 L22: 3.0994
REMARK 3 L33: 2.6248 L12: -0.0806
REMARK 3 L13: -0.1105 L23: -0.1313
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.0069 S13: 0.2889
REMARK 3 S21: 0.1255 S22: -0.0142 S23: -0.0990
REMARK 3 S31: -0.2434 S32: -0.1395 S33: 0.0107
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS DISORDERED REGIONS IN MONOMERS A, F, D, AND G
REMARK 3 WERE OMMITED
REMARK 4
REMARK 4 1OEZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-03.
REMARK 100 THE PDBE ID CODE IS EBI-12508.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35679
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1HL5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA2SO4, 15% PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 17.33300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 95.40600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 95.40600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 8.66650
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 95.40600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 95.40600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.99950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 95.40600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 95.40600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 8.66650
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 95.40600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 95.40600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 25.99950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 17.33300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, Z
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 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, X
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 ENGINEERED MUTATION HIS 46 ARG IN CHAINS W,X,Y AND Z
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO W 66
REMARK 465 LEU W 67
REMARK 465 SER W 68
REMARK 465 ARG W 69
REMARK 465 LYS W 70
REMARK 465 HIS W 71
REMARK 465 GLY W 72
REMARK 465 GLY W 73
REMARK 465 PRO W 74
REMARK 465 LYS W 75
REMARK 465 ASP W 76
REMARK 465 GLU W 77
REMARK 465 LEU W 126
REMARK 465 GLY W 127
REMARK 465 LYS W 128
REMARK 465 GLY W 129
REMARK 465 GLY W 130
REMARK 465 ASN W 131
REMARK 465 GLU W 132
REMARK 465 GLU W 133
REMARK 465 SER W 134
REMARK 465 THR W 135
REMARK 465 LYS W 136
REMARK 465 THR W 137
REMARK 465 GLY W 138
REMARK 465 ASN W 139
REMARK 465 ALA W 140
REMARK 465 GLY W 141
REMARK 465 PRO X 66
REMARK 465 LEU X 67
REMARK 465 SER X 68
REMARK 465 ARG X 69
REMARK 465 LYS X 70
REMARK 465 HIS X 71
REMARK 465 GLY X 72
REMARK 465 GLY X 73
REMARK 465 PRO X 74
REMARK 465 LYS X 75
REMARK 465 ASP X 76
REMARK 465 GLU X 77
REMARK 465 LEU X 126
REMARK 465 GLY X 127
REMARK 465 LYS X 128
REMARK 465 GLY X 129
REMARK 465 GLY X 130
REMARK 465 ASN X 131
REMARK 465 GLU X 132
REMARK 465 GLU X 133
REMARK 465 SER X 134
REMARK 465 THR X 135
REMARK 465 LYS X 136
REMARK 465 THR X 137
REMARK 465 GLY X 138
REMARK 465 ASN X 139
REMARK 465 ALA X 140
REMARK 465 GLY X 141
REMARK 465 PRO Y 66
REMARK 465 LEU Y 67
REMARK 465 SER Y 68
REMARK 465 ARG Y 69
REMARK 465 LYS Y 70
REMARK 465 HIS Y 71
REMARK 465 GLY Y 72
REMARK 465 GLY Y 73
REMARK 465 PRO Y 74
REMARK 465 LYS Y 75
REMARK 465 ASP Y 76
REMARK 465 GLU Y 77
REMARK 465 LEU Y 126
REMARK 465 GLY Y 127
REMARK 465 LYS Y 128
REMARK 465 GLY Y 129
REMARK 465 GLY Y 130
REMARK 465 ASN Y 131
REMARK 465 GLU Y 132
REMARK 465 GLU Y 133
REMARK 465 SER Y 134
REMARK 465 THR Y 135
REMARK 465 LYS Y 136
REMARK 465 THR Y 137
REMARK 465 GLY Y 138
REMARK 465 ASN Y 139
REMARK 465 ALA Y 140
REMARK 465 GLY Y 141
REMARK 465 PRO Z 66
REMARK 465 LEU Z 67
REMARK 465 SER Z 68
REMARK 465 ARG Z 69
REMARK 465 LYS Z 70
REMARK 465 HIS Z 71
REMARK 465 GLY Z 72
REMARK 465 GLY Z 73
REMARK 465 PRO Z 74
REMARK 465 LYS Z 75
REMARK 465 ASP Z 76
REMARK 465 GLU Z 77
REMARK 465 LEU Z 126
REMARK 465 GLY Z 127
REMARK 465 LYS Z 128
REMARK 465 GLY Z 129
REMARK 465 GLY Z 130
REMARK 465 ASN Z 131
REMARK 465 GLU Z 132
REMARK 465 GLU Z 133
REMARK 465 SER Z 134
REMARK 465 THR Z 135
REMARK 465 LYS Z 136
REMARK 465 THR Z 137
REMARK 465 GLY Z 138
REMARK 465 ASN Z 139
REMARK 465 ALA Z 140
REMARK 465 GLY Z 141
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 GLU W 24 CD OE1 OE2
REMARK 470 ASN W 26 CG OD1 ND2
REMARK 470 ASN W 65 CA C O CB CG OD1 ND2
REMARK 470 ASP W 124 CG OD1 OD2
REMARK 470 ASP W 125 CB CG OD1 OD2
REMARK 470 LYS X 23 CD CE NZ
REMARK 470 GLU X 24 CG CD OE1 OE2
REMARK 470 ASN X 65 CA C O CB CG OD1 ND2
REMARK 470 LYS X 122 CD CE NZ
REMARK 470 ASP X 125 CG OD1 OD2
REMARK 470 LYS Y 23 CD CE NZ
REMARK 470 LYS Y 30 CE NZ
REMARK 470 ASN Y 65 CA C O CB CG OD1 ND2
REMARK 470 LYS Y 122 CE NZ
REMARK 470 LYS Z 23 CD CE NZ
REMARK 470 GLU Z 24 CG CD OE1 OE2
REMARK 470 ASN Z 26 CG OD1 ND2
REMARK 470 ASN Z 65 CA C O CB CG OD1 ND2
REMARK 470 GLU Z 78 CD OE1 OE2
REMARK 470 LYS Z 91 CD CE NZ
REMARK 470 ASP Z 125 CG OD1 OD2
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 N GLU X 78 O HOH X 2042 2.11
REMARK 500 OE2 GLU Z 49 O HOH Z 2034 2.19
REMARK 500 O HOH Z 2024 O HOH W 2041 2.06
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 ASP X 101 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 CYS Y 111 CA - CB - SG ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP Z 83 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP Z 101 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 CYS Z 111 CA - CB - SG ANGL. DEV. = -7.2 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 ARG Y 79 113.34 -30.63
REMARK 500 ASN Z 26 -34.16 70.32
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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: (10X,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 ARG Y 79 21.5 L L OUTSIDE RANGE
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 W1154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP W 83 OD1
REMARK 620 2 ASP W 83 OD2 55.1
REMARK 620 3 HOH W2067 O 105.9 85.7
REMARK 620 4 HIS W 63 ND1 89.5 141.6 91.2
REMARK 620 5 HIS W 80 ND1 128.8 107.8 121.7 106.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN X1154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS X 63 ND1
REMARK 620 2 HIS X 80 ND1 108.7
REMARK 620 3 HOH X2066 O 91.4 114.6
REMARK 620 4 ASP X 83 OD1 89.7 128.6 112.3
REMARK 620 5 ASP X 83 OD2 140.7 105.1 92.4 53.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Y1154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Y 83 OD1
REMARK 620 2 HIS Y 63 ND1 85.0
REMARK 620 3 HIS Y 80 ND1 128.0 108.1
REMARK 620 4 ASP Y 83 OD2 53.0 137.4 104.3
REMARK 620 5 HOH Y2067 O 107.7 95.1 120.4 91.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Z1154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Z 63 ND1
REMARK 620 2 HIS Z 80 ND1 108.5
REMARK 620 3 HOH Z2076 O 94.9 118.7
REMARK 620 4 ASP Z 83 OD1 86.5 127.4 109.4
REMARK 620 5 ASP Z 83 OD2 135.4 108.9 87.9 51.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN W1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 W1155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN X1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X1155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Y1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 Y1155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Z1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 Z1155
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AZV RELATED DB: PDB
REMARK 900 FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)
REMARK 900 RELATED ID: 1BA9 RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED MONOMERIC
REMARK 900 SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES
REMARK 900 RELATED ID: 1DSW RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF A MONOMERIC,
REMARK 900 REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE
REMARK 900 DISMUTASE BEARING THE SAMECHARGE AS THE
REMARK 900 NATIVE PROTEIN
REMARK 900 RELATED ID: 1FUN RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH LYS 136
REMARK 900 REPLACED BY GLU, CYS 6 REPLACED BY ALA
REMARK 900 AND CYS 111 REPLACED BY SER (K136E, C6A,
REMARK 900 C111S)
REMARK 900 RELATED ID: 1HL4 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF APO TYPE HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1HL5 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1KMG RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF MONOMERIC COPPER-
REMARK 900 FREE SUPEROXIDEDISMUTASE
REMARK 900 RELATED ID: 1L3N RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED DIMERIC
REMARK 900 COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF
REMARK 900 DIMERIZATION
REMARK 900 RELATED ID: 1MFM RELATED DB: PDB
REMARK 900 MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q
REMARK 900 AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 1N18 RELATED DB: PDB
REMARK 900 THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE
REMARK 900 DISMUTASE, C6A,C111S
REMARK 900 RELATED ID: 1N19 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT
REMARK 900 RELATED ID: 1SOS RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH CYS 6
REMARK 900 REPLACED BY ALA AND CYS 111 REPLACED BY
REMARK 900 SER (C6A, C111S)
REMARK 900 RELATED ID: 1SPD RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 4SOD RELATED DB: PDB
REMARK 900 CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS
REMARK 900 6 REPLACED BY ALA AND CYS 111 REPLACED
REMARK 900 BY SER (C6A,C111S) WITH AN 18-RESIDUE
REMARK 900 HEPARIN-BINDING PEPTIDE FUSED TO THE C-
REMARK 900 TERMINUS (THEORETICAL MODEL)
REMARK 900 RELATED ID: 1OZT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO H46R MUTANT OF HUMAN CU,ZN
REMARK 900 SUPEROXIDE DISMUTASE (CUZNSOD)
REMARK 900 RELATED ID: 1OZU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S134N MUTANT OF HUMAN CU,ZN SUPEROXIDE
REMARK 900 DISMUTASE (CUZNSOD)
DBREF 1OEZ W 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1OEZ X 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1OEZ Y 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1OEZ Z 1 153 UNP P00441 SODC_HUMAN 1 153
SEQADV 1OEZ ARG W 46 UNP P00441 HIS 46 ENGINEERED MUTATION
SEQADV 1OEZ ARG X 46 UNP P00441 HIS 46 ENGINEERED MUTATION
SEQADV 1OEZ ARG Y 46 UNP P00441 HIS 46 ENGINEERED MUTATION
SEQADV 1OEZ ARG Z 46 UNP P00441 HIS 46 ENGINEERED MUTATION
SEQRES 1 W 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 W 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 W 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 W 153 GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP
SEQRES 5 W 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 W 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 W 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 W 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 W 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 W 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 W 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 W 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 X 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 X 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 X 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 X 153 GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP
SEQRES 5 X 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 X 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 X 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 X 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 X 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 X 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 X 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 X 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 Y 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 Y 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 Y 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 Y 153 GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP
SEQRES 5 Y 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 Y 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 Y 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 Y 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 Y 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 Y 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 Y 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 Y 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 Z 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 Z 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 Z 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 Z 153 GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP
SEQRES 5 Z 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 Z 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 Z 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 Z 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 Z 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 Z 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 Z 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 Z 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET ZN W1154 1
HET SO4 W1155 5
HET ZN X1154 1
HET SO4 X1155 5
HET ZN Y1154 1
HET SO4 Y1155 5
HET ZN Z1154 1
HET SO4 Z1155 5
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 SO4 4(O4 S 2-)
FORMUL 13 HOH *277(H2 O)
HELIX 1 1 ALA Y 55 GLY Y 61 5 7
HELIX 2 2 ALA W 55 GLY W 61 5 7
HELIX 3 3 ALA Z 55 GLY Z 61 5 7
HELIX 4 4 ALA X 55 GLY X 61 5 7
SHEET 1 YA 5 ALA Y 95 ASP Y 101 0
SHEET 2 YA 5 VAL Y 29 LYS Y 36 -1 O VAL Y 29 N ASP Y 101
SHEET 3 YA 5 GLN Y 15 GLU Y 21 -1 O GLN Y 15 N LYS Y 36
SHEET 4 YA 5 LYS Y 3 LEU Y 8 -1 O ALA Y 4 N PHE Y 20
SHEET 5 YA 5 GLY Y 150 ILE Y 151 -1 O GLY Y 150 N VAL Y 5
SHEET 1 YB 4 ASP Y 83 ALA Y 89 0
SHEET 2 YB 4 GLY Y 41 HIS Y 48 -1 O GLY Y 41 N ALA Y 89
SHEET 3 YB 4 THR Y 116 HIS Y 120 -1 O THR Y 116 N HIS Y 48
SHEET 4 YB 4 ARG Y 143 VAL Y 148 -1 N LEU Y 144 O VAL Y 119
SHEET 1 WA 5 ALA W 95 ASP W 101 0
SHEET 2 WA 5 VAL W 29 LYS W 36 -1 O VAL W 29 N ASP W 101
SHEET 3 WA 5 GLN W 15 GLU W 21 -1 O GLN W 15 N LYS W 36
SHEET 4 WA 5 LYS W 3 LEU W 8 -1 O ALA W 4 N PHE W 20
SHEET 5 WA 5 GLY W 150 ILE W 151 -1 O GLY W 150 N VAL W 5
SHEET 1 WB 4 ASP W 83 ALA W 89 0
SHEET 2 WB 4 GLY W 41 HIS W 48 -1 O GLY W 41 N ALA W 89
SHEET 3 WB 4 THR W 116 HIS W 120 -1 O THR W 116 N HIS W 48
SHEET 4 WB 4 ARG W 143 VAL W 148 -1 N LEU W 144 O VAL W 119
SHEET 1 ZA 5 ALA Z 95 ASP Z 101 0
SHEET 2 ZA 5 VAL Z 29 LYS Z 36 -1 O VAL Z 29 N ASP Z 101
SHEET 3 ZA 5 GLN Z 15 GLU Z 21 -1 O GLN Z 15 N LYS Z 36
SHEET 4 ZA 5 LYS Z 3 LEU Z 8 -1 O ALA Z 4 N PHE Z 20
SHEET 5 ZA 5 GLY Z 150 ILE Z 151 -1 O GLY Z 150 N VAL Z 5
SHEET 1 ZB 4 ASP Z 83 ALA Z 89 0
SHEET 2 ZB 4 GLY Z 41 HIS Z 48 -1 O GLY Z 41 N ALA Z 89
SHEET 3 ZB 4 THR Z 116 HIS Z 120 -1 O THR Z 116 N HIS Z 48
SHEET 4 ZB 4 ARG Z 143 VAL Z 148 -1 N LEU Z 144 O VAL Z 119
SHEET 1 XA 5 ALA X 95 ASP X 101 0
SHEET 2 XA 5 VAL X 29 LYS X 36 -1 O VAL X 29 N ASP X 101
SHEET 3 XA 5 GLN X 15 GLU X 21 -1 O GLN X 15 N LYS X 36
SHEET 4 XA 5 LYS X 3 LEU X 8 -1 O ALA X 4 N PHE X 20
SHEET 5 XA 5 GLY X 150 ILE X 151 -1 O GLY X 150 N VAL X 5
SHEET 1 XB 4 ASP X 83 ALA X 89 0
SHEET 2 XB 4 GLY X 41 HIS X 48 -1 O GLY X 41 N ALA X 89
SHEET 3 XB 4 THR X 116 HIS X 120 -1 O THR X 116 N HIS X 48
SHEET 4 XB 4 ARG X 143 VAL X 148 -1 N LEU X 144 O VAL X 119
LINK ZN ZN W1154 OD1 ASP W 83 1555 1555 2.33
LINK ZN ZN W1154 OD2 ASP W 83 1555 1555 2.21
LINK ZN ZN W1154 O HOH W2067 1555 1555 2.36
LINK ZN ZN W1154 ND1 HIS W 63 1555 1555 1.96
LINK ZN ZN W1154 ND1 HIS W 80 1555 1555 1.85
LINK ZN ZN X1154 ND1 HIS X 63 1555 1555 1.92
LINK ZN ZN X1154 ND1 HIS X 80 1555 1555 1.95
LINK ZN ZN X1154 O HOH X2066 1555 1555 2.62
LINK ZN ZN X1154 OD1 ASP X 83 1555 1555 2.36
LINK ZN ZN X1154 OD2 ASP X 83 1555 1555 2.38
LINK ZN ZN Y1154 ND1 HIS Y 63 1555 1555 1.95
LINK ZN ZN Y1154 ND1 HIS Y 80 1555 1555 1.80
LINK ZN ZN Y1154 OD2 ASP Y 83 1555 1555 2.09
LINK ZN ZN Y1154 O HOH Y2067 1555 1555 2.43
LINK ZN ZN Y1154 OD1 ASP Y 83 1555 1555 2.50
LINK ZN ZN Z1154 ND1 HIS Z 80 1555 1555 1.76
LINK ZN ZN Z1154 O HOH Z2076 1555 1555 2.42
LINK ZN ZN Z1154 OD1 ASP Z 83 1555 1555 2.52
LINK ZN ZN Z1154 OD2 ASP Z 83 1555 1555 2.20
LINK ZN ZN Z1154 ND1 HIS Z 63 1555 1555 1.84
SITE 1 AC1 4 HIS W 63 HIS W 80 ASP W 83 HOH W2067
SITE 1 AC2 3 HIS W 63 HIS W 120 ARG W 143
SITE 1 AC3 4 HIS X 63 HIS X 80 ASP X 83 HOH X2066
SITE 1 AC4 5 HIS X 48 HIS X 63 HIS X 120 ARG X 143
SITE 2 AC4 5 HOH X2067
SITE 1 AC5 4 HIS Y 63 HIS Y 80 ASP Y 83 HOH Y2067
SITE 1 AC6 4 HIS Y 48 HIS Y 63 HIS Y 120 ARG Y 143
SITE 1 AC7 4 HIS Z 63 HIS Z 80 ASP Z 83 HOH Z2076
SITE 1 AC8 3 HIS Z 63 HIS Z 120 ARG Z 143
CRYST1 190.812 190.812 34.666 90.00 90.00 90.00 P 41 21 2 32
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 0.005241 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005241 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028847 0.00000
MTRIX1 1 0.997400 -0.031810 0.064730 1.23302 1
MTRIX2 1 -0.031920 -0.999490 0.000630 89.35111 1
MTRIX3 1 0.064670 -0.002690 -0.997900 6.83338 1
MTRIX1 2 -1.000000 -0.001940 0.002360 -6.55065 1
MTRIX2 2 0.002000 -0.999700 0.024440 95.27160 1
MTRIX3 2 0.002320 0.024440 0.999700 -1.13723 1
MTRIX1 3 -1.000000 -0.001940 0.002360 -6.55065 1
MTRIX2 3 0.002000 -0.999700 0.024440 95.27160 1
MTRIX3 3 0.002320 0.024440 0.999700 -1.13723 1
(ATOM LINES ARE NOT SHOWN.)
END
