HEADER OXIDOREDUCTASE 28-MAR-08 2VR8
TITLE CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN
TITLE 2 SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, F;
COMPND 4 FRAGMENT: RESIDUES 2-154;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 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 ZINC, COPPER, HUMAN CU, CYTOPLASM, ACETYLATION, UBL
KEYWDS 2 CONJUGATION, DISEASE MUTATION, ZN SUPEROXIDE DISMUTASE,
KEYWDS 3 AMYOTROPHIC LATERAL SCLEROSIS, ANTIOXIDANT, METAL-BINDING,
KEYWDS 4 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ANTONYUK,X.CAO,S.V.SEETHARAMAN,L.J.WHITSON,A.B.TAYLOR,
AUTHOR 2 S.P.HOLLOWAY,R.W.STRANGE,P.A.DOUCETTE,A.TIWARI,L.J.HAYWARD,
AUTHOR 3 S.PADUA,J.A.COHLBERG,J.SELVERSTONE VALENTINE,S.S.HASNAIN,
AUTHOR 4 P.J.HART
REVDAT 4 24-FEB-09 2VR8 1 VERSN
REVDAT 3 17-JUN-08 2VR8 1 JRNL
REVDAT 2 29-APR-08 2VR8 1 JRNL
REVDAT 1 08-APR-08 2VR8 0
JRNL AUTH X.CAO,S.ANTONYUK,S.V.SEETHARAMAN,L.J.WHITSON,
JRNL AUTH 2 A.B.TAYLOR,S.P.HOLLOWAY,R.W.STRANGE,P.A.DOUCETTE,
JRNL AUTH 3 A.TIWARI,L.J.HAYWARD,S.PADUA,J.A.COHLBERG,
JRNL AUTH 4 J.SELVERSTONE VALENTINE,S.S.HASNAIN,P.J.HART
JRNL TITL STRUCTURES OF THE G85R VARIANT OF SOD1 IN FAMILIAL
JRNL TITL 2 AMYOTROPHIC LATERAL SCLEROSIS.
JRNL REF J.BIOL.CHEM. V. 283 16169 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18378676
JRNL DOI 10.1074/JBC.M801522200
REMARK 2
REMARK 2 RESOLUTION. 1.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.9999
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) : 1.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 52158
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) : 0.115
REMARK 3 R VALUE (WORKING SET) : 0.113
REMARK 3 FREE R VALUE : 0.153
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2789
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) : 1.36
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.40
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2313
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2287
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.053
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.051
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.776
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2366 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2069 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3190 ; 1.770 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4877 ; 1.977 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 321 ;12.729 ; 5.125
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 398 ;10.992 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;18.641 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 347 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2700 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 424 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 498 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2189 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1489 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 391 ; 0.251 ; 0.200
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): 75 ; 0.600 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 124 ; 0.513 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 49 ; 0.270 ; 0.200
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): 1530 ; 1.712 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2444 ; 2.498 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 836 ; 3.524 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 741 ; 4.562 ; 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 : BABINET MODEL WITH 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 2VR8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-08.
REMARK 100 THE PDBE ID CODE IS EBI-35801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 1.28
REMARK 200 MONOCHROMATOR : NULL
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 : 55091
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.36
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.2
REMARK 200 R MERGE FOR SHELL (I) : 0.33
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.40
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 2C9S
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): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M SODIUM
REMARK 280 THIOCYANATE
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 28.32350
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1510 ANGSTROM**2
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 17510 ANGSTROM**2
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -15.5 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 86 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, GLY 86 TO ARG
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 2003 - O HOH A 2012 2.04
REMARK 500 O HOH A 2011 - O HOH A 2039 2.20
REMARK 500 O HOH A 2027 - O HOH A 2208 2.19
REMARK 500 O HOH A 2089 - O HOH A 2100 2.10
REMARK 500 O HOH A 2104 - O HOH A 2219 2.16
REMARK 500 O HOH A 2148 - O HOH A 2193 1.88
REMARK 500 O HOH A 2242 - O HOH A 2244 2.09
REMARK 500 O HOH F 2027 - O HOH F 2076 2.14
REMARK 500 O HOH F 2150 - O HOH F 2180 1.85
REMARK 500 O HOH F 2150 - O HOH F 2177 2.09
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 A 96 CB - CG - OD2 ANGL. DEV. = 6.4 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 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 ASN A 65 65.57 -155.15
REMARK 500 ASN F 65 64.42 -157.61
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 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 A1156 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 137.2
REMARK 620 3 HIS A 120 NE2 100.2 114.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU F1156 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 120 NE2
REMARK 620 2 HIS F 46 ND1 97.8
REMARK 620 3 HIS F 48 NE2 113.5 140.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1157 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 110.5
REMARK 620 3 HIS A 120 NE2 90.3 124.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1158 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 83 OD1
REMARK 620 2 HIS A 71 ND1 98.6
REMARK 620 3 HIS A 63 ND1 107.1 106.0
REMARK 620 4 HIS A 80 ND1 115.1 120.7 108.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 24 OE1
REMARK 620 2 SCN A1161 N 116.0
REMARK 620 3 SCN A1162 N 104.3 108.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F1157 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 120 NE2
REMARK 620 2 HIS F 46 ND1 91.4
REMARK 620 3 HIS F 48 NE2 125.6 111.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F1158 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 80 ND1
REMARK 620 2 HIS F 63 ND1 109.2
REMARK 620 3 HIS F 71 ND1 119.9 106.5
REMARK 620 4 ASP F 83 OD1 115.0 106.3 98.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F1160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 24 OE1
REMARK 620 2 SCN F1161 N 102.7
REMARK 620 3 SCN F1162 N 116.3 110.4
REMARK 620 N 1 2
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A1156
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1157
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F1156
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F1157
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN F1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN F1162
REMARK 900
REMARK 900 RELATED ENTRIES
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: 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: 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: 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: 1HL4 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF APO TYPE 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: 2V0A RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN
REMARK 900 SUPEROXIDE DISMUTASE
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: 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: 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: 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: 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: 2C9V RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN
REMARK 900 SUPEROXIDE DISMUTASE
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: 1PU0 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN CU,ZN SUPEROXIDE
REMARK 900 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: 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: 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: 1HL5 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE
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: 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: 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 999
REMARK 999 SEQUENCE
REMARK 999 G85R MUTANT
DBREF 2VR8 A 0 0 PDB 2VR8 2VR8 0 0
DBREF 2VR8 A 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 2VR8 F 0 0 PDB 2VR8 2VR8 0 0
DBREF 2VR8 F 1 153 UNP P00441 SODC_HUMAN 2 154
SEQADV 2VR8 ARG A 85 UNP P00441 GLY 86 ENGINEERED MUTATION
SEQADV 2VR8 ARG F 85 UNP P00441 GLY 86 ENGINEERED MUTATION
SEQRES 1 A 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 A 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 A 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 A 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 A 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 A 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 A 154 GLU ARG HIS VAL GLY ASP LEU ARG ASN VAL THR ALA ASP
SEQRES 8 A 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 A 154 ILE SER LEU SER GLY ASP HIS CSO ILE ILE GLY ARG THR
SEQRES 10 A 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 A 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 A 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 F 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 F 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 F 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 F 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 F 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 F 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 F 154 GLU ARG HIS VAL GLY ASP LEU ARG ASN VAL THR ALA ASP
SEQRES 8 F 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 F 154 ILE SER LEU SER GLY ASP HIS CSO ILE ILE GLY ARG THR
SEQRES 10 F 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 F 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 F 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
MODRES 2VR8 CSO F 111 CYS S-HYDROXYCYSTEINE
MODRES 2VR8 CSO A 111 CYS S-HYDROXYCYSTEINE
HET ACE A 0 3
HET CSO A 111 7
HET CU A1156 1 MICROHETEROGENEITY
HET ZN A1157 1 MICROHETEROGENEITY
HET ZN A1158 1
HET SO4 A1159 5
HET ZN A1160 1
HET SCN A1161 3
HET SCN A1162 3
HET ACE F 0 3
HET CSO F 111 7
HET CU F1156 1 MICROHETEROGENEITY
HET ZN F1157 1 MICROHETEROGENEITY
HET ZN F1158 1
HET SO4 F1159 5
HET ZN F1160 1
HET SCN F1161 3
HET SCN F1162 3
HETNAM CU COPPER (II) ION
HETNAM ACE ACETYL GROUP
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM SCN THIOCYANATE ION
FORMUL 3 CU 2(CU 2+)
FORMUL 4 ACE 2(C2 H4 O)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 6 ZN 6(ZN 2+)
FORMUL 7 CSO 2(C3 H7 N O3 S)
FORMUL 8 SCN 4(C N S 1-)
FORMUL 9 HOH *520(H2 O1)
HELIX 1 1 ALA A 55 GLY A 61 5 7
HELIX 2 2 GLU A 133 GLY A 138 1 6
HELIX 3 3 ALA F 55 GLY F 61 5 7
HELIX 4 4 GLU F 133 GLY F 138 1 6
SHEET 1 AA 5 ALA A 95 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 GLN A 15 GLN A 22 -1 O GLN A 15 N LYS A 36
SHEET 4 AA 5 THR A 2 LEU A 8 -1 O THR A 2 N GLN A 22
SHEET 5 AA 5 GLY A 150 ALA A 152 -1 O GLY A 150 N VAL A 5
SHEET 1 AB 2 GLY A 41 HIS A 43 0
SHEET 2 AB 2 VAL A 87 ALA A 89 -1 O VAL A 87 N HIS A 43
SHEET 1 AC 3 PHE A 45 HIS A 48 0
SHEET 2 AC 3 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 3 AC 3 ARG A 143 VAL A 148 -1 N LEU A 144 O VAL A 119
SHEET 1 FA 7 PHE F 45 HIS F 48 0
SHEET 2 FA 7 THR F 116 HIS F 120 -1 O THR F 116 N HIS F 48
SHEET 3 FA 7 ARG F 143 VAL F 148 -1 N LEU F 144 O VAL F 119
SHEET 4 FA 7 THR F 2 GLY F 10 -1 O LYS F 9 N CYS F 146
SHEET 5 FA 7 GLN F 15 GLN F 22 -1 O GLY F 16 N LEU F 8
SHEET 6 FA 7 VAL F 29 LYS F 36 -1 O LYS F 30 N GLU F 21
SHEET 7 FA 7 ALA F 95 ASP F 101 -1 O ALA F 95 N ILE F 35
SHEET 1 FB 5 PHE F 45 HIS F 48 0
SHEET 2 FB 5 THR F 116 HIS F 120 -1 O THR F 116 N HIS F 48
SHEET 3 FB 5 ARG F 143 VAL F 148 -1 N LEU F 144 O VAL F 119
SHEET 4 FB 5 THR F 2 GLY F 10 -1 O LYS F 9 N CYS F 146
SHEET 5 FB 5 GLY F 150 ALA F 152 -1 O GLY F 150 N VAL F 5
SHEET 1 FC 2 GLY F 41 HIS F 43 0
SHEET 2 FC 2 VAL F 87 ALA F 89 -1 O VAL F 87 N HIS F 43
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.10
SSBOND 2 CYS F 57 CYS F 146 1555 1555 2.09
LINK N ALA A 1 C ACE A 0 1555 1555 1.31
LINK C HIS A 110 N CSO A 111 1555 1555 1.33
LINK C CSO A 111 N ILE A 112 1555 1555 1.32
LINK CU B CU A1156 ND1 HIS A 46 1555 1555 1.78
LINK CU B CU A1156 NE2 HIS A 48 1555 1555 2.11
LINK CU B CU A1156 NE2 HIS A 120 1555 1555 2.11
LINK ZN A ZN A1157 ND1 HIS A 46 1555 1555 2.30
LINK ZN A ZN A1157 NE2 HIS A 48 1555 1555 2.10
LINK ZN A ZN A1157 NE2 HIS A 120 1555 1555 1.90
LINK ZN ZN A1158 OD1 ASP A 83 1555 1555 1.96
LINK ZN ZN A1158 ND1 HIS A 71 1555 1555 2.05
LINK ZN ZN A1158 ND1 HIS A 63 1555 1555 2.02
LINK ZN ZN A1158 ND1 HIS A 80 1555 1555 2.05
LINK ZN ZN A1160 OE1 GLU A 24 1555 1555 1.99
LINK ZN ZN A1160 N SCN A1161 1555 1555 1.94
LINK ZN ZN A1160 N SCN A1162 1555 1555 1.91
LINK N ALA F 1 C ACE F 0 1555 1555 1.33
LINK C HIS F 110 N CSO F 111 1555 1555 1.33
LINK C CSO F 111 N ILE F 112 1555 1555 1.34
LINK CU B CU F1156 NE2 HIS F 48 1555 1555 2.07
LINK CU B CU F1156 ND1 HIS F 46 1555 1555 1.75
LINK CU B CU F1156 NE2 HIS F 120 1555 1555 2.23
LINK ZN A ZN F1157 NE2 HIS F 48 1555 1555 2.10
LINK ZN A ZN F1157 ND1 HIS F 46 1555 1555 2.26
LINK ZN A ZN F1157 NE2 HIS F 120 1555 1555 1.94
LINK ZN ZN F1158 OD1 ASP F 83 1555 1555 1.96
LINK ZN ZN F1158 ND1 HIS F 71 1555 1555 2.05
LINK ZN ZN F1158 ND1 HIS F 63 1555 1555 2.02
LINK ZN ZN F1158 ND1 HIS F 80 1555 1555 2.05
LINK ZN ZN F1160 N SCN F1162 1555 1555 1.88
LINK ZN ZN F1160 N SCN F1161 1555 1555 1.91
LINK ZN ZN F1160 OE1 GLU F 24 1555 1555 1.95
SITE 1 AC1 6 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC1 6 ZN A1157 SO4 A1159
SITE 1 AC2 7 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC2 7 CU A1156 SO4 A1159 HOH A2265
SITE 1 AC3 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC4 15 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC4 15 THR A 137 ARG A 143 CU A1156 ZN A1157
SITE 3 AC4 15 HOH A2241 HOH A2265 HOH A2266 HOH A2267
SITE 4 AC4 15 HOH A2268 HOH A2269 HOH A2270
SITE 1 AC5 3 GLU A 24 SCN A1161 SCN A1162
SITE 1 AC6 3 GLU A 24 ZN A1160 SCN A1162
SITE 1 AC7 3 GLU A 24 ZN A1160 SCN A1161
SITE 1 AC8 6 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 2 AC8 6 ZN F1157 SO4 F1159
SITE 1 AC9 6 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 2 AC9 6 CU F1156 SO4 F1159
SITE 1 BC1 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 BC2 13 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 2 BC2 13 THR F 137 ARG F 143 CU F1156 ZN F1157
SITE 3 BC2 13 HOH F2224 HOH F2246 HOH F2247 HOH F2248
SITE 4 BC2 13 HOH F2250
SITE 1 BC3 3 GLU F 24 SCN F1161 SCN F1162
SITE 1 BC4 3 GLU F 24 ZN F1160 SCN F1162
SITE 1 BC5 3 GLU F 24 ZN F1160 SCN F1161
CRYST1 34.210 56.647 74.714 90.00 102.14 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 0.029231 0.000000 0.006288 0.00000
SCALE2 0.000000 0.017653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013691 0.00000
HETATM 1 C ACE A 0 -10.988 -8.418 33.075 0.50 19.78 C
ANISOU 1 C ACE A 0 2487 2639 2388 63 222 -42 C
HETATM 2 O ACE A 0 -9.760 -8.544 33.074 0.50 21.05 O
ANISOU 2 O ACE A 0 2713 2851 2434 24 262 -66 O
HETATM 3 CH3 ACE A 0 -11.749 -7.809 34.235 0.50 20.29 C
ANISOU 3 CH3 ACE A 0 2554 2721 2434 40 252 -53 C
(ATOM LINES ARE NOT SHOWN.)
END
