HEADER OXIDOREDUCTASE 23-NOV-09 2WZ6
TITLE G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, F;
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
KEYWDS OXIDOREDUCTASE, DISEASE MUTATION, NEURODEGENERATION, AMYOTROPHIC
KEYWDS 2 LATERAL SCLEROSIS, METAL-BINDING, ANTIOXIDANT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.V.ANTONYUK,R.W.STRANGE,S.S.HASNAIN
REVDAT 2 17-AUG-11 2WZ6 1 REMARK HET HETNAM FORMUL
REVDAT 2 2 HETATM VERSN
REVDAT 1 08-DEC-10 2WZ6 0
JRNL AUTH S.ANTONYUK,R.W.STRANGE,S.S.HASNAIN
JRNL TITL STRUCTURAL DISCOVERY OF SMALL MOLECULE BINDING SITES IN
JRNL TITL 2 CU-ZN HUMAN SUPEROXIDE DISMUTASE FAMILIAL AMYOTROPHIC
JRNL TITL 3 LATERAL SCLEROSIS MUTANTS PROVIDES INSIGHTS FOR LEAD
JRNL TITL 4 OPTIMIZATION.
JRNL REF J.MED.CHEM. V. 53 1402 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 20067275
JRNL DOI 10.1021/JM9017948
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0106
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.39
REMARK 3 NUMBER OF REFLECTIONS : 33843
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) : 0.19782
REMARK 3 R VALUE (WORKING SET) : 0.19518
REMARK 3 FREE R VALUE : 0.24755
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1780
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) : 1.550
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.590
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2128
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.266
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.265
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2284
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 426
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.279
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.59
REMARK 3 B22 (A**2) : -0.88
REMARK 3 B33 (A**2) : 0.35
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.11
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.114
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.824
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2393 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1576 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3255 ; 1.647 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3897 ; 0.966 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 325 ; 6.896 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 101 ;37.128 ;25.644
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 393 ;12.761 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;12.290 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 354 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2751 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 432 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1528 ; 0.988 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 660 ; 0.296 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2448 ; 1.662 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 865 ; 2.265 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 797 ; 3.442 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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.
REMARK 4
REMARK 4 2WZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-NOV-09.
REMARK 100 THE PDBE ID CODE IS EBI-41801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX10.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33843
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.55
REMARK 200 RESOLUTION RANGE LOW (A) : 24.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.6
REMARK 200 R MERGE FOR SHELL (I) : 0.39
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.00
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 2C9V
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM NACL, 2.0-3.0 M AMMONIUM
REMARK 280 SULPHATE, 100 MM ACETATE BUFFER PH 4.75
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 34.01250
REMARK 290 SMTRY3 2 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 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: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
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 RESIDUE IN CHAIN A, GLY 94 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, GLY 94 TO ALA
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 O3 SO4 A 156 O HOH A 2215 1.82
REMARK 500 O3 SO4 F 156 O HOH F 2201 2.05
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 CD1 ILE F 17 O LYS F 128 2655 2.09
REMARK 500 O HOH A 2013 O HOH A 2182 2646 2.11
REMARK 500 O HOH A 2147 O HOH F 2203 2656 2.01
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 A 154A ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 48 NE2
REMARK 620 2 HIS A 46 ND1 105.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 154A ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 46 ND1
REMARK 620 2 HIS F 48 NE2 108.2
REMARK 620 3 HIS F 120 NE2 90.0 118.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 71 ND1
REMARK 620 2 HIS A 80 ND1 121.6
REMARK 620 3 ASP A 83 OD1 96.2 117.0
REMARK 620 4 HIS A 63 ND1 106.0 110.1 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 80 ND1
REMARK 620 2 HIS F 71 ND1 122.0
REMARK 620 3 ASP F 83 OD1 114.9 98.6
REMARK 620 4 HIS F 63 ND1 108.5 106.2 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 48 NE2
REMARK 620 2 HIS A 46 ND1 148.2
REMARK 620 3 HIS A 120 NE2 111.6 100.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU F 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 46 ND1
REMARK 620 2 HIS F 48 NE2 145.7
REMARK 620 3 HIS F 120 NE2 99.6 113.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 154A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZO0 A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 154A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 157
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZO0 F 170
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PTZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC
REMARK 900 LATERAL SCLEROSIS (FALS) MUTANT H43R
REMARK 900 RELATED ID: 1OEZ RELATED DB: PDB
REMARK 900 ZN HIS46ARG MUTANT OF HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1AZV RELATED DB: PDB
REMARK 900 FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)
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: 2WYZ RELATED DB: PDB
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH UMP
REMARK 900 RELATED ID: 1OZU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT
REMARK 900 S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (
REMARK 900 CUZNSOD) TO 1.3A RESOLUTION
REMARK 900 RELATED ID: 2VR6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF
REMARK 900 HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)
REMARK 900 AT 1.3 A RESOLUTION
REMARK 900 RELATED ID: 2C9V RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN
REMARK 900 SUPEROXIDE DISMUTASE
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: 1PU0 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN CU,ZN SUPEROXIDE
REMARK 900 DISMUTASE
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: 1N19 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT
REMARK 900 RELATED ID: 1P1V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN
REMARK 900 COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT
REMARK 900 D125H TO 1.4A
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: 2WZ0 RELATED DB: PDB
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH ANILINE.
REMARK 900 RELATED ID: 2WKO RELATED DB: PDB
REMARK 900 STRUCTURE OF METAL LOADED PATHOGENIC SOD1
REMARK 900 MUTANT G93A.
REMARK 900 RELATED ID: 2AF2 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF DISULFIDE REDUCED AND
REMARK 900 COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1UXL RELATED DB: PDB
REMARK 900 I113T MUTANT OF HUMAN SOD1
REMARK 900 RELATED ID: 2VR8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF
REMARK 900 HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)
REMARK 900 AT 1.36 A RESOLUTION
REMARK 900 RELATED ID: 1RK7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE
REMARK 900 DISMUTASE: ROLEOF METAL IONS IN PROTEIN
REMARK 900 FOLDING
REMARK 900 RELATED ID: 2VR7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF
REMARK 900 HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)
REMARK 900 AT 1.58 A RESOLUTION
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: 1MFM RELATED DB: PDB
REMARK 900 MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q
REMARK 900 AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 2C9S RELATED DB: PDB
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-
REMARK 900 ZN HUMAN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2V0A RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2WYT RELATED DB: PDB
REMARK 900 1.0 A RESOLUTION STRUCTURE OF L38V SOD1
REMARK 900 MUTANT
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: 1OZT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS
REMARK 900 MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE (
REMARK 900 CUZNSOD) TO 2.5A RESOLUTION
REMARK 900 RELATED ID: 1KMG RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF MONOMERIC COPPER-
REMARK 900 FREE SUPEROXIDEDISMUTASE
REMARK 900 RELATED ID: 1N18 RELATED DB: PDB
REMARK 900 THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE
REMARK 900 DISMUTASE, C6A,C111S
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: 1HL5 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2C9U RELATED DB: PDB
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-
REMARK 900 ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1UXM RELATED DB: PDB
REMARK 900 A4V MUTANT OF HUMAN SOD1
REMARK 900 RELATED ID: 1SPD RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2WZ5 RELATED DB: PDB
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE
DBREF 2WZ6 A 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 2WZ6 F 1 153 UNP P00441 SODC_HUMAN 2 154
SEQADV 2WZ6 ALA A 93 UNP P00441 GLY 94 ENGINEERED MUTATION
SEQADV 2WZ6 ALA F 93 UNP P00441 GLY 94 ENGINEERED MUTATION
SEQRES 1 A 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 A 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 A 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 A 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 A 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 A 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 A 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 A 153 ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 A 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 A 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 A 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 A 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 F 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 F 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 F 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 F 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 F 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 F 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 F 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 F 153 ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 F 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 F 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 F 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 F 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET CU A 154 1
HET ZN A 154A 1
HET ZN A 155 1
HET SO4 A 156 5
HET ZO0 A 170 22
HET CU F 154 1
HET ZN F 154A 1
HET ZN F 155 1
HET SO4 F 156 5
HET SO4 F 157 5
HET ZO0 F 170 22
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM ZO0 4-(4-METHYL-1,4-DIAZEPAN-1-YL)-2-(TRIFLUOROMETHYL)QUINAZOLINE
FORMUL 3 CU 2(CU 2+)
FORMUL 4 ZN 4(ZN 2+)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 6 ZO0 2(C15 H17 F3 N4)
FORMUL 7 HOH *426(H2 O)
HELIX 1 1 GLY A 56 GLY A 61 5 6
HELIX 2 2 GLU A 132 LYS A 136 5 5
HELIX 3 3 GLY F 56 GLY F 61 5 6
HELIX 4 4 SER F 107 HIS F 110 5 4
HELIX 5 5 GLU F 132 LYS F 136 5 5
SHEET 1 AA 5 VAL A 94 ASP A 101 0
SHEET 2 AA 5 VAL A 29 LYS A 36 -1 O VAL A 29 N ASP A 101
SHEET 3 AA 5 VAL A 14 GLN A 22 -1 O GLN A 15 N LYS A 36
SHEET 4 AA 5 THR A 2 GLY A 10 -1 O THR A 2 N GLN A 22
SHEET 5 AA 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5
SHEET 1 AB 4 ASP A 83 ALA A 89 0
SHEET 2 AB 4 GLY A 41 HIS A 48 -1 O GLY A 41 N ALA A 89
SHEET 3 AB 4 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 4 AB 4 ARG A 143 VAL A 148 -1 N LEU A 144 O VAL A 119
SHEET 1 FA 5 ALA F 95 ASP F 101 0
SHEET 2 FA 5 VAL F 29 LYS F 36 -1 O VAL F 29 N ASP F 101
SHEET 3 FA 5 GLN F 15 GLN F 22 -1 O GLN F 15 N LYS F 36
SHEET 4 FA 5 THR F 2 LEU F 8 -1 O THR F 2 N GLN F 22
SHEET 5 FA 5 GLY F 150 ILE F 151 -1 O GLY F 150 N VAL F 5
SHEET 1 FB 4 ASP F 83 ALA F 89 0
SHEET 2 FB 4 GLY F 41 HIS F 48 -1 O GLY F 41 N ALA F 89
SHEET 3 FB 4 THR F 116 HIS F 120 -1 O THR F 116 N HIS F 48
SHEET 4 FB 4 ARG F 143 VAL F 148 -1 N LEU F 144 O VAL F 119
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.08
SSBOND 2 CYS F 57 CYS F 146 1555 1555 2.08
LINK ZN B ZN A 154A NE2 HIS A 48 1555 1555 2.20
LINK ZN B ZN A 154A ND1 HIS A 46 1555 1555 2.54
LINK CU A CU A 154 NE2 HIS A 48 1555 1555 1.98
LINK CU A CU A 154 ND1 HIS A 46 1555 1555 1.96
LINK CU A CU A 154 NE2 HIS A 120 1555 1555 2.09
LINK ZN ZN A 155 ND1 HIS A 71 1555 1555 2.07
LINK ZN ZN A 155 ND1 HIS A 80 1555 1555 2.02
LINK ZN ZN A 155 OD1 ASP A 83 1555 1555 1.94
LINK ZN ZN A 155 ND1 HIS A 63 1555 1555 2.07
LINK CU A CU F 154 NE2 HIS F 48 1555 1555 1.98
LINK CU A CU F 154 ND1 HIS F 46 1555 1555 2.02
LINK ZN B ZN F 154A NE2 HIS F 48 1555 1555 2.14
LINK ZN B ZN F 154A ND1 HIS F 46 1555 1555 2.56
LINK CU A CU F 154 NE2 HIS F 120 1555 1555 2.12
LINK ZN B ZN F 154A NE2 HIS F 120 1555 1555 1.85
LINK ZN ZN F 155 ND1 HIS F 63 1555 1555 2.04
LINK ZN ZN F 155 OD1 ASP F 83 1555 1555 1.98
LINK ZN ZN F 155 ND1 HIS F 71 1555 1555 2.07
LINK ZN ZN F 155 ND1 HIS F 80 1555 1555 2.03
CISPEP 1 GLY A 12 PRO A 13 0 2.96
SITE 1 AC1 5 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC1 5 SO4 F 157
SITE 1 AC2 5 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC2 5 SO4 F 157
SITE 1 AC3 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC4 13 HOH A2210 HOH A2211 HOH A2212 HOH A2214
SITE 2 AC4 13 HOH A2215 HIS F 48 HIS F 63 HIS F 120
SITE 3 AC4 13 THR F 137 ARG F 143 CU F 154 ZN F 154A
SITE 4 AC4 13 SO4 F 156
SITE 1 AC5 8 GLU A 21 LYS A 30 VAL A 31 TRP A 32
SITE 2 AC5 8 SER A 98 ILE A 99 HOH A2054 HOH A2216
SITE 1 AC6 6 SO4 A 156 HOH A2212 HIS F 46 HIS F 48
SITE 2 AC6 6 HIS F 63 HIS F 120
SITE 1 AC7 6 SO4 A 156 HOH A2212 HIS F 46 HIS F 48
SITE 2 AC7 6 HIS F 63 HIS F 120
SITE 1 AC8 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 AC9 10 SO4 A 156 HOH A2214 THR F 137 ASN F 139
SITE 2 AC9 10 GLY F 141 HOH F2166 HOH F2180 HOH F2201
SITE 3 AC9 10 HOH F2202 HOH F2204
SITE 1 BC1 12 HIS A 48 HIS A 63 HIS A 120 THR A 137
SITE 2 BC1 12 ARG A 143 CU A 154 ZN A 154A HOH F2205
SITE 3 BC1 12 HOH F2206 HOH F2207 HOH F2208 HOH F2210
SITE 1 BC2 9 GLU F 21 LYS F 30 VAL F 31 TRP F 32
SITE 2 BC2 9 SER F 98 ILE F 99 HOH F2132 HOH F2211
SITE 3 BC2 9 HOH F2212
CRYST1 38.996 68.025 50.633 90.00 105.88 90.00 P 1 21 1 4
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 0.025644 0.000000 0.007295 0.00000
SCALE2 0.000000 0.014700 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020534 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
