HEADER OXIDOREDUCTASE 11-MAR-06 2GBT
TITLE C6A/C111A CUZN SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CU/ZN SUPEROXIDE DISMUTASE;
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 GENE: SOD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21/DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PACA
KEYWDS OXIDOREDUCTASE, HUMAN CU/ZN SUPEROXIDE DISMUTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HORNBERG,D.T.LOGAN,S.L.MARKLUND,M.OLIVEBERG
REVDAT 3 13-JUL-11 2GBT 1 VERSN
REVDAT 2 24-FEB-09 2GBT 1 VERSN
REVDAT 1 02-JAN-07 2GBT 0
JRNL AUTH A.HORNBERG,D.T.LOGAN,S.L.MARKLUND,M.OLIVEBERG
JRNL TITL THE COUPLING BETWEEN DISULPHIDE STATUS, METALLATION AND
JRNL TITL 2 DIMER INTERFACE STRENGTH IN CU/ZN SUPEROXIDE DISMUTASE
JRNL REF J.MOL.BIOL. V. 365 333 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17070542
JRNL DOI 10.1016/J.JMB.2006.09.048
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 64189
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3249
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4458
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 235
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4026
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 537
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) : 31.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.50000
REMARK 3 B22 (A**2) : 2.16000
REMARK 3 B33 (A**2) : -1.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.73000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.115
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.109
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.979
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4094 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3650 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5532 ; 1.031 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8533 ; 0.673 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 546 ; 5.687 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;37.789 ;25.491
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 657 ;10.404 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;10.324 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 621 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4694 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 744 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 637 ; 0.181 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3563 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1962 ; 0.156 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2344 ; 0.079 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 438 ; 0.113 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.174 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.080 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 36 ; 0.182 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.104 ; 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): 3547 ; 0.569 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1184 ; 0.090 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4289 ; 0.677 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1678 ; 1.201 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1243 ; 1.604 ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0429 -2.8992 20.8128
REMARK 3 T TENSOR
REMARK 3 T11: -0.2331 T22: -0.0400
REMARK 3 T33: -0.2186 T12: -0.0682
REMARK 3 T13: 0.0042 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 2.2893 L22: 1.5362
REMARK 3 L33: 4.6842 L12: 0.1841
REMARK 3 L13: 1.2149 L23: 0.2009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0610 S12: 0.1605 S13: -0.1477
REMARK 3 S21: -0.0523 S22: -0.0820 S23: -0.0500
REMARK 3 S31: 0.1859 S32: -0.2844 S33: 0.0210
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7538 3.0887 46.3614
REMARK 3 T TENSOR
REMARK 3 T11: -0.2364 T22: -0.0033
REMARK 3 T33: -0.2220 T12: -0.0204
REMARK 3 T13: -0.0023 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 2.2868 L22: 1.2758
REMARK 3 L33: 3.6776 L12: 0.0207
REMARK 3 L13: 0.1002 L23: 0.1389
REMARK 3 S TENSOR
REMARK 3 S11: 0.0247 S12: -0.3395 S13: 0.0131
REMARK 3 S21: 0.1457 S22: 0.0641 S23: -0.0042
REMARK 3 S31: 0.1141 S32: -0.0202 S33: -0.0888
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 153
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1570 11.8112 30.5120
REMARK 3 T TENSOR
REMARK 3 T11: -0.2413 T22: -0.1314
REMARK 3 T33: -0.2148 T12: -0.0402
REMARK 3 T13: -0.0042 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 4.0533 L22: 1.3111
REMARK 3 L33: 4.5178 L12: 0.3474
REMARK 3 L13: -0.0847 L23: -0.0112
REMARK 3 S TENSOR
REMARK 3 S11: 0.0669 S12: -0.3993 S13: 0.2244
REMARK 3 S21: -0.0139 S22: 0.0191 S23: 0.0109
REMARK 3 S31: -0.2011 S32: 0.1988 S33: -0.0860
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 153
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0501 5.0422 8.3858
REMARK 3 T TENSOR
REMARK 3 T11: -0.1985 T22: -0.1429
REMARK 3 T33: -0.2157 T12: -0.0352
REMARK 3 T13: -0.0102 T23: 0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 2.8302 L22: 2.2032
REMARK 3 L33: 5.6411 L12: -0.0465
REMARK 3 L13: 0.3766 L23: 0.1322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0162 S12: 0.4500 S13: -0.0564
REMARK 3 S21: -0.1130 S22: 0.0013 S23: 0.0169
REMARK 3 S31: 0.0903 S32: 0.0209 S33: -0.0175
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2GBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB036930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.092
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64389
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.37800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1HL4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG8000, 50MM TRIS-HCL, 50MM NAAC,
REMARK 280 1MM EDTA, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 78.30900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 17.62850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.30900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 17.62850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 1440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 273 LIES ON A SPECIAL POSITION.
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 ALA A 1
REMARK 465 ALA B 1
REMARK 465 ARG C 69
REMARK 465 LYS C 70
REMARK 465 HIS C 71
REMARK 465 GLY C 72
REMARK 465 GLY C 73
REMARK 465 PRO C 74
REMARK 465 LYS C 75
REMARK 465 ASP C 76
REMARK 465 GLU C 77
REMARK 465 GLU C 78
REMARK 465 ASP C 125
REMARK 465 LEU C 126
REMARK 465 GLY C 127
REMARK 465 LYS C 128
REMARK 465 GLY C 129
REMARK 465 GLY C 130
REMARK 465 ASN C 131
REMARK 465 GLU C 132
REMARK 465 GLU C 133
REMARK 465 SER C 134
REMARK 465 THR C 135
REMARK 465 LYS C 136
REMARK 465 THR C 137
REMARK 465 GLY C 138
REMARK 465 ASN C 139
REMARK 465 ALA C 140
REMARK 465 GLY C 141
REMARK 465 ALA D 1
REMARK 465 LEU D 67
REMARK 465 SER D 68
REMARK 465 ARG D 69
REMARK 465 LYS D 70
REMARK 465 HIS D 71
REMARK 465 GLY D 72
REMARK 465 GLY D 73
REMARK 465 PRO D 74
REMARK 465 LYS D 75
REMARK 465 ASP D 76
REMARK 465 GLU D 77
REMARK 465 ASP D 125
REMARK 465 LEU D 126
REMARK 465 GLY D 127
REMARK 465 LYS D 128
REMARK 465 GLY D 129
REMARK 465 GLY D 130
REMARK 465 ASN D 131
REMARK 465 GLU D 132
REMARK 465 GLU D 133
REMARK 465 SER D 134
REMARK 465 THR D 135
REMARK 465 LYS D 136
REMARK 465 THR D 137
REMARK 465 GLY D 138
REMARK 465 ASN D 139
REMARK 465 ALA D 140
REMARK 465 GLY D 141
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 B 79 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 79 NE - CZ - NH2 ANGL. DEV. = -4.2 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 SER A 98 69.61 -156.73
REMARK 500 ASN C 65 84.99 -156.53
REMARK 500 ALA C 111 151.15 -48.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 266 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH B 277 DISTANCE = 5.03 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 141.2
REMARK 620 3 HIS A 120 NE2 96.1 115.9
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 63 ND1
REMARK 620 2 HIS A 71 ND1 113.2
REMARK 620 3 HIS A 80 ND1 104.7 124.4
REMARK 620 4 ASP A 83 OD1 110.6 85.0 118.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 B 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 ND1
REMARK 620 2 HIS B 48 NE2 139.1
REMARK 620 3 HIS B 120 NE2 102.1 117.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 63 ND1
REMARK 620 2 HIS B 71 ND1 121.7
REMARK 620 3 HIS B 80 ND1 105.9 119.0
REMARK 620 4 ASP B 83 OD1 111.2 85.8 111.6
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 CU1 A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HL4 RELATED DB: PDB
REMARK 900 APO CUZN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2GBU RELATED DB: PDB
REMARK 900 C6A/C111A/C57A/C146A APO CUZN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2GBV RELATED DB: PDB
REMARK 900 C6A/C111A/C57A/C146A HOLO CUZN SUPEROXIDE DISMUTASE
DBREF 2GBT A 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 2GBT B 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 2GBT C 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 2GBT D 1 153 UNP P00441 SODC_HUMAN 1 153
SEQADV 2GBT ALA A 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 2GBT ALA A 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 2GBT ALA B 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 2GBT ALA B 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 2GBT ALA C 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 2GBT ALA C 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 2GBT ALA D 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 2GBT ALA D 111 UNP P00441 CYS 111 ENGINEERED
SEQRES 1 A 153 ALA THR LYS ALA VAL ALA 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 ALA 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 B 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 B 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 B 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 B 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 B 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 B 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 B 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 B 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 B 153 SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU
SEQRES 10 B 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 B 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 B 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 C 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 C 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 C 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 C 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 C 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 C 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 C 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 C 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 C 153 SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU
SEQRES 10 C 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 C 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 C 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 D 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 D 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 D 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 D 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 D 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 D 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 D 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 D 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 D 153 SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU
SEQRES 10 D 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 D 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 D 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET CU1 A 154 1
HET ZN A 155 1
HET CU1 B 154 1
HET ZN B 155 1
HETNAM CU1 COPPER (I) ION
HETNAM ZN ZINC ION
FORMUL 5 CU1 2(CU 1+)
FORMUL 6 ZN 2(ZN 2+)
FORMUL 9 HOH *537(H2 O)
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 B 55 GLY B 61 5 7
HELIX 4 4 GLU B 133 GLY B 138 1 6
HELIX 5 5 ALA C 55 GLY C 61 5 7
HELIX 6 6 ALA D 55 GLY D 61 5 7
SHEET 1 A 5 ALA A 95 ASP A 101 0
SHEET 2 A 5 VAL A 29 LYS A 36 -1 N VAL A 29 O ASP A 101
SHEET 3 A 5 GLN A 15 GLU A 21 -1 N ASN A 19 O TRP A 32
SHEET 4 A 5 LYS A 3 LEU A 8 -1 N ALA A 6 O ILE A 18
SHEET 5 A 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5
SHEET 1 B 4 ASP A 83 ALA A 89 0
SHEET 2 B 4 GLY A 41 HIS A 48 -1 N GLY A 41 O ALA A 89
SHEET 3 B 4 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 4 B 4 ARG A 143 VAL A 148 -1 O GLY A 147 N LEU A 117
SHEET 1 C 5 ALA B 95 ASP B 101 0
SHEET 2 C 5 VAL B 29 LYS B 36 -1 N ILE B 35 O ALA B 95
SHEET 3 C 5 GLN B 15 GLU B 21 -1 N ASN B 19 O TRP B 32
SHEET 4 C 5 LYS B 3 LEU B 8 -1 N ALA B 4 O PHE B 20
SHEET 5 C 5 GLY B 150 ILE B 151 -1 O GLY B 150 N VAL B 5
SHEET 1 D 4 ASP B 83 ALA B 89 0
SHEET 2 D 4 GLY B 41 HIS B 48 -1 N GLY B 41 O ALA B 89
SHEET 3 D 4 THR B 116 HIS B 120 -1 O THR B 116 N HIS B 48
SHEET 4 D 4 ARG B 143 VAL B 148 -1 O GLY B 147 N LEU B 117
SHEET 1 E 5 ALA C 95 ASP C 101 0
SHEET 2 E 5 VAL C 29 LYS C 36 -1 N GLY C 33 O VAL C 97
SHEET 3 E 5 GLN C 15 GLN C 22 -1 N ASN C 19 O TRP C 32
SHEET 4 E 5 THR C 2 LEU C 8 -1 N THR C 2 O GLN C 22
SHEET 5 E 5 GLY C 150 ILE C 151 -1 O GLY C 150 N VAL C 5
SHEET 1 F 4 ASP C 83 ALA C 89 0
SHEET 2 F 4 GLY C 41 HIS C 48 -1 N GLY C 41 O ALA C 89
SHEET 3 F 4 THR C 116 HIS C 120 -1 O THR C 116 N HIS C 48
SHEET 4 F 4 ARG C 143 VAL C 148 -1 O GLY C 147 N LEU C 117
SHEET 1 G 5 ALA D 95 ASP D 101 0
SHEET 2 G 5 VAL D 29 LYS D 36 -1 N VAL D 31 O ILE D 99
SHEET 3 G 5 GLN D 15 GLN D 22 -1 N ASN D 19 O TRP D 32
SHEET 4 G 5 LYS D 3 LEU D 8 -1 N ALA D 6 O ILE D 18
SHEET 5 G 5 GLY D 150 ILE D 151 -1 O GLY D 150 N VAL D 5
SHEET 1 H 4 ASP D 83 ALA D 89 0
SHEET 2 H 4 GLY D 41 HIS D 48 -1 N GLY D 41 O ALA D 89
SHEET 3 H 4 THR D 116 HIS D 120 -1 O THR D 116 N HIS D 48
SHEET 4 H 4 ARG D 143 VAL D 148 -1 O GLY D 147 N LEU D 117
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.07
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.08
SSBOND 3 CYS C 57 CYS C 146 1555 1555 2.10
SSBOND 4 CYS D 57 CYS D 146 1555 1555 2.08
LINK CU CU1 A 154 ND1 HIS A 46 1555 1555 2.41
LINK CU CU1 A 154 NE2 HIS A 48 1555 1555 2.05
LINK CU CU1 A 154 NE2 HIS A 120 1555 1555 1.83
LINK ZN ZN A 155 ND1 HIS A 63 1555 1555 2.10
LINK ZN ZN A 155 ND1 HIS A 71 1555 1555 2.32
LINK ZN ZN A 155 ND1 HIS A 80 1555 1555 2.05
LINK ZN ZN A 155 OD1 ASP A 83 1555 1555 1.79
LINK CU CU1 B 154 ND1 HIS B 46 1555 1555 2.25
LINK CU CU1 B 154 NE2 HIS B 48 1555 1555 2.05
LINK CU CU1 B 154 NE2 HIS B 120 1555 1555 1.81
LINK ZN ZN B 155 ND1 HIS B 63 1555 1555 1.89
LINK ZN ZN B 155 ND1 HIS B 71 1555 1555 2.25
LINK ZN ZN B 155 ND1 HIS B 80 1555 1555 2.28
LINK ZN ZN B 155 OD1 ASP B 83 1555 1555 1.91
SITE 1 AC1 4 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 1 AC2 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC3 4 HIS B 46 HIS B 48 HIS B 63 HIS B 120
SITE 1 AC4 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
CRYST1 156.618 35.257 114.971 90.00 112.17 90.00 C 1 2 1 16
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 0.006380 0.000000 0.002600 0.00000
SCALE2 0.000000 0.028360 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009390 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
