HEADER OXIDOREDUCTASE 14-DEC-05 2C9U
TITLE 1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-ISOLATED CU-ZN
TITLE 2 HUMAN SUPEROXIDE DISMUTASE
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
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BLOOD;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS ACETYLATION, AMYOTROPHIC LATERAL SCLEROSIS, ZINC,
KEYWDS 2 ANTIOXIDANT, COPPER, DISEASE MUTATION, HUMAN CU, METAL-
KEYWDS 3 BINDING, OXIDOREDUCTASE, ZN SUPEROXIDE DISMUTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.STRANGE,S.V.ANTONYUK,M.A.HOUGH,P.A.DOUCETTE,
AUTHOR 2 J.S.VALENTINE S,S.HASNAIN
REVDAT 3 24-FEB-09 2C9U 1 VERSN
REVDAT 2 15-FEB-06 2C9U 1 AUTHOR JRNL
REVDAT 1 16-DEC-05 2C9U 0
JRNL AUTH R.W.STRANGE,S.V.ANTONYUK,M.A.HOUGH,P.A.DOUCETTE,
JRNL AUTH 2 J.S.VALENTINE,S.S.HASNAIN
JRNL TITL VARIABLE METALLATION OF HUMAN SUPEROXIDE
JRNL TITL 2 DISMUTASE: ATOMIC RESOLUTION CRYSTAL STRUCTURES OF
JRNL TITL 3 CU-ZN, ZN-ZN AND AS-ISOLATED WILD-TYPE ENZYMES.
JRNL REF J.MOL.BIOL. V. 356 1152 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16406071
JRNL DOI 10.1016/J.JMB.2005.11.081
REMARK 2
REMARK 2 RESOLUTION. 1.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 66500
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) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3501
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) : 1.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.27
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3900
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 203
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2273
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 389
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : -0.36000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.045
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.045
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.025
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.271
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2328 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2055 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3138 ; 1.841 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4845 ; 2.495 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 306 ; 6.798 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 101 ;39.028 ;25.644
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 397 ;11.843 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;13.630 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 346 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2641 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 414 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 474 ; 0.253 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2074 ; 0.203 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1121 ; 0.169 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1335 ; 0.095 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 301 ; 0.302 ; 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): 24 ; 0.193 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 50 ; 0.182 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 47 ; 0.297 ; 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): 1916 ; 2.417 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2408 ; 3.041 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 898 ; 3.718 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 730 ; 4.618 ; 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 2C9U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-05.
REMARK 100 THE PDBE ID CODE IS EBI-26849.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-03
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 : PX10.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.074
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70045
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.240
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 (%): 39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0 M AMMONIUM SULPHATE, 100 MM
REMARK 280 SODIUM CHLORITE, 50MM SODIUM ACETATE BUFFER
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 33.77650
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 GENERATING THE BIOMOLECULE
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: 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 ELIMINATES RADICALS WHICH ARE PRODUCED BY CELLS
REMARK 400 AND WHICH ARE TOXIC TO BIOLOGICAL SYSTEMS.
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 ASP A 11 OD1 OD2
REMARK 470 SER A 25 OG
REMARK 470 GLN F 153 O
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 GLY F 10 - O HOH F 2011 1.85
REMARK 500 O GLY F 10 - O HOH F 2012 1.96
REMARK 500 C ASP F 11 - O HOH F 2011 2.18
REMARK 500 N GLY F 12 - O HOH F 2011 1.95
REMARK 500 O GLU F 77 - O HOH F 2109 1.80
REMARK 500 O HOH A 2005 - O HOH A 2013 1.91
REMARK 500 O HOH A 2066 - O HOH F 2184 2.19
REMARK 500 O HOH A 2084 - O HOH F 2184 2.12
REMARK 500 O HOH A 2100 - O HOH A 2114 2.17
REMARK 500 O HOH A 2130 - O HOH A 2134 2.19
REMARK 500 O HOH F 2010 - O HOH A 2064 2.02
REMARK 500 O HOH F 2089 - O HOH F 2177 2.17
REMARK 500 O HOH F 2120 - O HOH F 2129 2.10
REMARK 500 O HOH F 2122 - O HOH F 2129 2.16
REMARK 500 O HOH F 2173 - O HOH F 2187 2.19
REMARK 500 O HOH F 2186 - O HOH F 2188 2.17
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
REMARK 500 O HOH A 2058 O HOH F 2124 1645 2.08
REMARK 500 O HOH F 2067 O HOH A 2110 1756 1.96
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 SER A 59 CA SER A 59 CB 0.099
REMARK 500 GLU F 49 CG GLU F 49 CD -0.106
REMARK 500 SER F 59 CA SER F 59 CB 0.105
REMARK 500 GLU F 78 CD GLU F 78 OE1 0.075
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 ARG A 115 NE - CZ - NH1 ANGL. DEV. = 3.0 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 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 A1157 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 48 NE2
REMARK 620 2 HIS A 120 NE2 112.5
REMARK 620 3 HIS A 46 ND1 136.1 98.3
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 48 NE2
REMARK 620 2 HIS F 46 ND1 133.6
REMARK 620 3 HIS F 120 NE2 123.9 101.6
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 HIS A 71 ND1
REMARK 620 2 HIS A 63 ND1 104.5
REMARK 620 3 HIS A 80 ND1 119.8 109.3
REMARK 620 4 ASP A 83 OD1 99.5 106.3 116.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1159 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 48 NE2
REMARK 620 2 HIS A 120 NE2 124.0
REMARK 620 3 SO4 A1154 O1 112.2 104.5
REMARK 620 4 HOH A2193 O 102.8 109.8 9.5
REMARK 620 5 HIS A 46 ND1 113.2 94.8 105.8 112.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F1155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 48 NE2
REMARK 620 2 HIS F 46 ND1 111.2
REMARK 620 3 HIS F 120 NE2 123.3 95.5
REMARK 620 4 SO4 F1154 O1 112.6 111.0 101.7
REMARK 620 5 HOH F2190 O 111.1 109.0 105.2 3.7
REMARK 620 N 1 2 3 4
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 63 ND1
REMARK 620 2 HIS F 71 ND1 105.2
REMARK 620 3 ASP F 83 OD1 105.5 99.1
REMARK 620 4 HIS F 80 ND1 108.3 121.9 115.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A1157
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F1155
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 ACT F1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F1159
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: 1OEZ RELATED DB: PDB
REMARK 900 ZN HIS46ARG MUTANT OF HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE
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: 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: 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: 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: 1PU0 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN CU,ZN SUPEROXIDE
REMARK 900 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: 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: 1UXL RELATED DB: PDB
REMARK 900 I113T MUTANT OF HUMAN SOD1
REMARK 900 RELATED ID: 1UXM RELATED DB: PDB
REMARK 900 A4V MUTANT OF HUMAN SOD1
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: 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: 2C9S RELATED DB: PDB
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-
REMARK 900 ZN HUMAN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2C9V RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN
REMARK 900 SUPEROXIDE DISMUTASE
DBREF 2C9U A 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 2C9U F 1 153 UNP P00441 SODC_HUMAN 1 153
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 GLY 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 GLY 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 SO4 A1154 5
HET SO4 A1155 5
HET CU A1157 1
HET ZN A1158 1
HET ZN A1159 1
HET SO4 F1154 5
HET ZN F1155 1
HET CU F1156 1
HET ZN F1157 1
HET ACT F1158 4
HET ACT F1159 4
HETNAM SO4 SULFATE ION
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 5 CU 2(CU 2+)
FORMUL 6 ZN 4(ZN 2+)
FORMUL 12 ACT 2(C2 H3 O2 1-)
FORMUL 14 HOH *389(H2 O1)
HELIX 1 1 ALA A 55 GLY A 61 5 7
HELIX 2 2 SER A 107 HIS A 110 5 4
HELIX 3 3 ASN A 131 LYS A 136 5 6
HELIX 4 4 ALA F 55 GLY F 61 5 7
HELIX 5 5 ASN F 131 LYS F 136 5 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 GLU A 21 -1 O GLN A 15 N LYS A 36
SHEET 4 AA 5 LYS A 3 LYS A 9 -1 O ALA A 4 N PHE A 20
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 VAL F 14 GLN F 22 -1 O GLN F 15 N LYS F 36
SHEET 4 FA 5 THR F 2 GLY F 10 -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 F 57 CYS F 146 1555 1555 2.58
SSBOND 2 CYS F 57 CYS F 146 1555 1555 2.00
LINK O1 SO4 A1154 ZN ZN A1159 1555 1555 1.98
LINK CU CU A1157 NE2 HIS A 48 1555 1555 2.04
LINK CU CU A1157 NE2 HIS A 120 1555 1555 2.23
LINK CU CU A1157 ND1 HIS A 46 1555 1555 1.82
LINK ZN ZN A1158 ND1 HIS A 71 1555 1555 2.08
LINK ZN ZN A1158 ND1 HIS A 63 1555 1555 2.03
LINK ZN ZN A1158 ND1 HIS A 80 1555 1555 2.02
LINK ZN ZN A1158 OD1 ASP A 83 1555 1555 1.97
LINK ZN ZN A1159 NE2 HIS A 48 1555 1555 2.07
LINK ZN ZN A1159 NE2 HIS A 120 1555 1555 1.95
LINK ZN ZN A1159 O HOH A2193 1555 1555 2.31
LINK ZN ZN A1159 ND1 HIS A 46 1555 1555 2.22
LINK OD1 ASP F 11 OXT ACT F1159 1555 1555 1.65
LINK CG ASP F 11 OXT ACT F1159 1555 1555 1.93
LINK ZN ZN F1155 NE2 HIS F 48 1555 1555 2.16
LINK ZN ZN F1155 ND1 HIS F 46 1555 1555 2.28
LINK ZN ZN F1155 NE2 HIS F 120 1555 1555 1.85
LINK ZN ZN F1155 O1 SO4 F1154 1555 1555 2.06
LINK ZN ZN F1155 O HOH F2190 1555 1555 2.08
LINK CU CU F1156 NE2 HIS F 120 1555 1555 2.00
LINK CU CU F1156 ND1 HIS F 46 1555 1555 1.98
LINK CU CU F1156 NE2 HIS F 48 1555 1555 2.01
LINK ZN ZN F1157 ND1 HIS F 80 1555 1555 1.99
LINK ZN ZN F1157 OD1 ASP F 83 1555 1555 1.96
LINK ZN ZN F1157 ND1 HIS F 71 1555 1555 2.07
LINK ZN ZN F1157 ND1 HIS F 63 1555 1555 2.06
CISPEP 1 GLY F 12 PRO F 13 0 1.50
SITE 1 AC1 15 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC1 15 THR A 137 ARG A 143 CU A1157 ZN A1159
SITE 3 AC1 15 HOH A2177 HOH A2178 HOH A2191 HOH A2192
SITE 4 AC1 15 HOH A2193 HOH A2194 HOH A2196
SITE 1 AC2 6 THR A 58 ARG A 143 HOH A2080 HOH A2195
SITE 2 AC2 6 HOH A2196 HOH A2197
SITE 1 AC3 5 HIS A 46 HIS A 48 HIS A 120 SO4 A1154
SITE 2 AC3 5 ZN A1159
SITE 1 AC4 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC5 8 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC5 8 SO4 A1154 CU A1157 HOH A2191 HOH A2193
SITE 1 AC6 16 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 2 AC6 16 THR F 137 ARG F 143 ZN F1155 CU F1156
SITE 3 AC6 16 HOH F2172 HOH F2173 HOH F2185 HOH F2186
SITE 4 AC6 16 HOH F2187 HOH F2188 HOH F2189 HOH F2190
SITE 1 AC7 8 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 2 AC7 8 SO4 F1154 CU F1156 HOH F2189 HOH F2190
SITE 1 AC8 7 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 2 AC8 7 SO4 F1154 ZN F1155 HOH F2190
SITE 1 AC9 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 BC1 6 GLY F 85 ASN F 86 LEU F 126 HOH F2041
SITE 2 BC1 6 HOH F2191 HOH F2192
SITE 1 BC2 3 GLY F 10 ASP F 11 HOH F2175
CRYST1 38.638 67.553 52.320 90.00 106.48 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 0.025881 0.000000 0.007657 0.00000
SCALE2 0.000000 0.014803 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
