HEADER OXIDOREDUCTASE, METAL BINDING PROTEIN 14-JUL-03 1PZS
TITLE CRYSTAL STRUCTURE OF A CU-ZN SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS AT 1.63 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 33-240;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: SODC OR RV0432 OR MT0447 OR MTCY22G10.29;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: QC871;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS CU-PROTEIN, BETA CORE, ANTIOXIDANT, METAL BINDING, GREEK KEY BETA
KEYWDS 2 BARREL, OXIDOREDUCTASE, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.DJINOVIC-CARUGO,L.SPAGNOLO,I.TORO
REVDAT 7 16-AUG-23 1PZS 1 REMARK LINK
REVDAT 6 31-JAN-18 1PZS 1 REMARK
REVDAT 5 11-OCT-17 1PZS 1 REMARK
REVDAT 4 13-JUL-11 1PZS 1 VERSN
REVDAT 3 24-FEB-09 1PZS 1 VERSN
REVDAT 2 17-AUG-04 1PZS 1 JRNL
REVDAT 1 27-JUL-04 1PZS 0
JRNL AUTH L.SPAGNOLO,I.TORO,M.D'ORAZIO,P.O'NEILL,J.Z.PEDERSEN,
JRNL AUTH 2 O.CARUGO,G.ROTILIO,A.BATTISTONI,K.DJINOVIC-CARUGO
JRNL TITL UNIQUE FEATURES OF THE SODC-ENCODED SUPEROXIDE DISMUTASE
JRNL TITL 2 FROM MYCOBACTERIUM TUBERCULOSIS, A FULLY FUNCTIONAL
JRNL TITL 3 COPPER-CONTAINING ENZYME LACKING ZINC IN THE ACTIVE SITE.
JRNL REF J.BIOL.CHEM. V. 279 33447 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15155722
JRNL DOI 10.1074/JBC.M404699200
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 19233
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1013
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) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1146
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1204
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 252
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.82000
REMARK 3 B22 (A**2) : -0.52000
REMARK 3 B33 (A**2) : 1.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.19000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.561
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1248 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1108 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1695 ; 1.356 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2593 ; 1.858 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 170 ; 6.233 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 198 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1420 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 227 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 208 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1242 ; 0.253 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 648 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 158 ; 0.154 ; 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): 12 ; 0.132 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 69 ; 0.328 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.119 ; 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): 841 ; 0.831 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1348 ; 1.484 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 407 ; 2.123 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 347 ; 3.475 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1PZS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019736.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-02
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 : ESRF
REMARK 200 BEAMLINE : ID13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9755
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20248
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.634
REMARK 200 RESOLUTION RANGE LOW (A) : 27.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 3.620
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.27
REMARK 200 R MERGE FOR SHELL (I) : 0.27300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.170
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 1JCV.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM SULFATE, ZINC
REMARK 280 CHLORIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 20K,
REMARK 280 TEMPERATURE 293.0K
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 35.02000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.21000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.02000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.21000
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED BY THE TWO
REMARK 300 FOLD AXIS: -X, Y, -Z
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 A 215 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 CYS A -36
REMARK 465 SER A -35
REMARK 465 SER A -34
REMARK 465 PRO A -33
REMARK 465 GLN A -32
REMARK 465 HIS A -31
REMARK 465 ALA A -30
REMARK 465 SER A -29
REMARK 465 THR A -28
REMARK 465 VAL A -27
REMARK 465 PRO A -26
REMARK 465 GLY A -25
REMARK 465 THR A -24
REMARK 465 THR A -23
REMARK 465 PRO A -22
REMARK 465 SER A -21
REMARK 465 ILE A -20
REMARK 465 TRP A -19
REMARK 465 THR A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 PRO A -15
REMARK 465 ALA A -14
REMARK 465 PRO A -13
REMARK 465 SER A -12
REMARK 465 GLY A -11
REMARK 465 LEU A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 HIS A -7
REMARK 465 ASP A -6
REMARK 465 GLU A -5
REMARK 465 GLU A -4
REMARK 465 SER A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 ALA A 0
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 NE2 HIS A 75 O HOH A 448 1.98
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 LYS A 120 -170.33 67.50
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 CU A 172 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 47 ND1
REMARK 620 2 HIS A 49 NE2 151.0
REMARK 620 3 HIS A 126 NE2 95.8 113.1
REMARK 620 4 HOH A 448 O 81.8 102.1 86.8
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 CU A 172
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JCV RELATED DB: PDB
REMARK 900 REDUCED BRIDGE-BROKEN YEAST CU/ZN SUPEROXIDE DISMUTASE LOW
REMARK 900 TEMPERATURE (-180C) STRUCTURE
REMARK 900 RELATED ID: 1BZO RELATED DB: PDB
REMARK 900 THREE-DIMENSIONAL STRUCTURE OF PROKARYOTIC CU, ZN SUPEROXIDE
REMARK 900 DISMUTASE FROM P. LEIOGNATHI, SOLVED BY X-RAY CRYSTALLOGRAPHY.
REMARK 900 RELATED ID: 1ESO RELATED DB: PDB
REMARK 900 MONOMERIC CU, ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1XSO RELATED DB: PDB
REMARK 900 THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU, ZN SUPEROXIDE
REMARK 900 DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROM
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1EQW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM CU, ZN SUPEROXIDE
REMARK 900 DISMUTASE
DBREF 1PZS A -34 171 UNP P0A608 SODC_MYCTU 33 240
SEQRES 1 A 208 CYS SER SER PRO GLN HIS ALA SER THR VAL PRO GLY THR
SEQRES 2 A 208 THR PRO SER ILE TRP THR GLY SER PRO ALA PRO SER GLY
SEQRES 3 A 208 LEU SER GLY HIS ASP GLU GLU SER PRO GLY ALA GLN SER
SEQRES 4 A 208 LEU THR SER THR LEU THR ALA PRO ASP GLY THR LYS VAL
SEQRES 5 A 208 ALA THR ALA LYS PHE GLU PHE ALA ASN GLY TYR ALA THR
SEQRES 6 A 208 VAL THR ILE ALA THR THR GLY VAL GLY LYS LEU THR PRO
SEQRES 7 A 208 GLY PHE HIS GLY LEU HIS ILE HIS GLN VAL GLY LYS CYS
SEQRES 8 A 208 GLU PRO ASN SER VAL ALA PRO THR GLY GLY ALA PRO GLY
SEQRES 9 A 208 ASN PHE LEU SER ALA GLY GLY HIS TYR HIS VAL PRO GLY
SEQRES 10 A 208 HIS THR GLY THR PRO ALA SER GLY ASP LEU ALA SER LEU
SEQRES 11 A 208 GLN VAL ARG GLY ASP GLY SER ALA MET LEU VAL THR THR
SEQRES 12 A 208 THR ASP ALA PHE THR MET ASP ASP LEU LEU SER GLY ALA
SEQRES 13 A 208 LYS THR ALA ILE ILE ILE HIS ALA GLY ALA ASP ASN PHE
SEQRES 14 A 208 ALA ASN ILE PRO PRO GLU ARG TYR VAL GLN VAL ASN GLY
SEQRES 15 A 208 THR PRO GLY PRO ASP GLU THR THR LEU THR THR GLY ASP
SEQRES 16 A 208 ALA GLY LYS ARG VAL ALA CYS GLY VAL ILE GLY SER GLY
HET CU A 172 1
HETNAM CU COPPER (II) ION
FORMUL 2 CU CU 2+
FORMUL 3 HOH *252(H2 O)
HELIX 1 1 PHE A 69 GLY A 73 5 5
HELIX 2 2 THR A 111 SER A 117 1 7
HELIX 3 3 ASP A 150 GLY A 157 1 8
SHEET 1 A 4 SER A 2 THR A 8 0
SHEET 2 A 4 LYS A 14 ALA A 23 -1 O ALA A 16 N LEU A 7
SHEET 3 A 4 TYR A 26 THR A 33 -1 O THR A 28 N GLU A 21
SHEET 4 A 4 MET A 102 THR A 107 -1 O THR A 107 N ALA A 27
SHEET 1 B 2 GLY A 42 HIS A 44 0
SHEET 2 B 2 LEU A 93 VAL A 95 -1 O VAL A 95 N GLY A 42
SHEET 1 C 3 LEU A 46 HIS A 49 0
SHEET 2 C 3 ALA A 122 HIS A 126 -1 O ALA A 122 N HIS A 49
SHEET 3 C 3 ARG A 162 VAL A 167 -1 O GLY A 166 N ILE A 123
SSBOND 1 CYS A 54 CYS A 165 1555 1555 2.06
LINK ND1 HIS A 47 CU CU A 172 1555 1555 2.07
LINK NE2 HIS A 49 CU CU A 172 1555 1555 2.05
LINK NE2 HIS A 126 CU CU A 172 1555 1555 2.04
LINK CU CU A 172 O HOH A 448 1555 1555 1.93
CISPEP 1 THR A 84 PRO A 85 0 -0.65
SITE 1 AC1 5 HIS A 47 HIS A 49 HIS A 75 HIS A 126
SITE 2 AC1 5 HOH A 448
CRYST1 70.040 58.420 51.390 90.00 126.99 90.00 C 1 2 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 0.014278 0.000000 0.010755 0.00000
SCALE2 0.000000 0.017117 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024362 0.00000
(ATOM LINES ARE NOT SHOWN.)
END