HEADER OXIDOREDUCTASE 03-FEB-06 2CE4
TITLE MANGANESE SUPEROXIDE DISMUTASE (MN-SOD) FROM DEINOCOCCUS
TITLE 2 RADIODURANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [MN];
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MNSOD;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 STRAIN: R1;
SOURCE 5 ATCC: 13939;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: GATEWAY PDEST17
KEYWDS MANGANESE SUPEROXIDE DISMUTASE, DEINOCOCCUS RADIODURANS,
KEYWDS 2 RADIATION RESISTANCE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.DENNIS,E.MICOSSI,J.MCCARTHY,E.MOE,E.GORDON,G.LEONARD,
AUTHOR 2 S.MCSWEENEY
REVDAT 3 24-FEB-09 2CE4 1 VERSN
REVDAT 2 05-APR-06 2CE4 1 JRNL
REVDAT 1 13-FEB-06 2CE4 0
JRNL AUTH R.DENNIS,E.MICOSSI,J.MCCARTHY,E.MOE,E.GORDON,
JRNL AUTH 2 G.LEONARD,S.MCSWEENEY
JRNL TITL STRUCTURE OF THE MANGANESE SUPEROXIDE DISMUTASE
JRNL TITL 2 FROM DEINOCOCCUS RADIODURANS IN TWO CRYSTAL FORMS.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 62 325 2006
JRNL REFN ISSN 1744-3091
JRNL PMID 16582477
JRNL DOI 10.1107/S1744309106008402
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19553
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 996
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1391
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3217
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 365
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.58000
REMARK 3 B22 (A**2) : 2.34000
REMARK 3 B33 (A**2) : -2.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.28000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.312
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.227
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.154
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.144
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3305 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2816 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4497 ; 1.308 ; 1.908
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6539 ; 0.846 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 404 ; 6.007 ; 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): 467 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3781 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 690 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 718 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3308 ; 0.233 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1765 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 269 ; 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): 8 ; 0.128 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 23 ; 0.267 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.214 ; 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): 2028 ; 0.642 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3225 ; 1.160 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1277 ; 1.624 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1272 ; 2.628 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 45 6
REMARK 3 1 B 1 B 45 6
REMARK 3 2 A 46 A 90 6
REMARK 3 2 B 46 B 90 6
REMARK 3 3 A 97 A 210 6
REMARK 3 3 B 97 B 210 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 2942 ; 0.38 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 2942 ; 2.46 ; 10.00
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
REMARK 3 RIDING POSITIONS. ELECTRON DENSITY FOR RESIDUES A90-A95 AND
REMARK 3 B91-B95 IS POOR. THEY ARE NOT INCLUDED IN THE MODEL.
REMARK 4
REMARK 4 2CE4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-06.
REMARK 100 THE PDBE ID CODE IS EBI-27551.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20567
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 29.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.16000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1VEW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM TRIS-HCL PH 8.5, 20MM
REMARK 280 MNCL2, 30% PEG 4000
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 41.60500
REMARK 290 SMTRY3 2 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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 MET A -21
REMARK 465 SER A -20
REMARK 465 TYR A -19
REMARK 465 TYR A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 LEU A -11
REMARK 465 GLU A -10
REMARK 465 SER A -9
REMARK 465 THR A -8
REMARK 465 SER A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 LYS A -4
REMARK 465 LYS A -3
REMARK 465 ALA A -2
REMARK 465 LEU A -1
REMARK 465 GLY A 44
REMARK 465 GLY A 90
REMARK 465 GLN A 91
REMARK 465 GLY A 92
REMARK 465 GLN A 93
REMARK 465 ASN A 94
REMARK 465 GLY A 95
REMARK 465 MET B -21
REMARK 465 SER B -20
REMARK 465 TYR B -19
REMARK 465 TYR B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 LEU B -11
REMARK 465 GLU B -10
REMARK 465 SER B -9
REMARK 465 THR B -8
REMARK 465 SER B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 LYS B -4
REMARK 465 LYS B -3
REMARK 465 ALA B -2
REMARK 465 GLN B 91
REMARK 465 GLY B 92
REMARK 465 GLN B 93
REMARK 465 ASN B 94
REMARK 465 GLY B 95
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 LYS A 40 CD CE NZ
REMARK 470 THR A 45 O
REMARK 470 ALA A 64 CB
REMARK 470 LEU A 104 CD1 CD2
REMARK 470 LYS A 126 CE NZ
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 LEU B -1 CD1 CD2
REMARK 470 LYS B 40 CD CE NZ
REMARK 470 GLU B 43 CD OE1 OE2
REMARK 470 LYS B 66 CE NZ
REMARK 470 LYS B 120 CE NZ
REMARK 470 LYS B 142 CG CD CE NZ
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 ARG A 61 -46.25 168.61
REMARK 500 ASN A 150 -128.03 57.51
REMARK 500 GLN A 183 -128.70 43.36
REMARK 500 SER B 109 -72.01 -65.41
REMARK 500 ASN B 150 -125.57 54.76
REMARK 500 TYR B 178 -5.25 -146.54
REMARK 500 GLN B 183 -125.37 50.73
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 MN A1211 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 26 NE2
REMARK 620 2 HIS A 80 NE2 92.9
REMARK 620 3 ASP A 172 OD2 86.2 110.0
REMARK 620 4 HIS A 176 NE2 94.7 139.1 110.6
REMARK 620 5 HOH A2198 O 167.7 94.3 82.0 86.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1211 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 172 OD2
REMARK 620 2 HIS B 26 NE2 85.1
REMARK 620 3 HIS B 176 NE2 115.3 93.8
REMARK 620 4 HOH B2167 O 83.8 168.9 90.6
REMARK 620 5 HIS B 80 NE2 105.2 86.9 139.4 96.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B1211
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y67 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MANGANESE SUPEROXIDE
REMARK 900 DISMUTASE FROMDEINOCOCCUS RADIODURANS
REMARK 900 RELATED ID: 2CDY RELATED DB: PDB
REMARK 900 MANGANESE SUPEROXIDE DISMUTASE (MN-SOD) FROM
REMARK 900 DEINOCOCCUS RADIODURANS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE CRYSTALLISED CONTAINS AN N-TERMINAL
REMARK 999 PURIFICATION TAG. WHERE RESIDUES FROM THIS ARE SEEN IN THE
REMARK 999 CRYSTAL THE NUMBERING IS -1, -2 ETC...
DBREF 2CE4 A -21 -1 PDB 2CE4 2CE4 -21 -1
DBREF 2CE4 A 1 210 UNP Q9RUV2 SODM_DEIRA 1 210
DBREF 2CE4 B -21 -1 PDB 2CE4 2CE4 -21 -1
DBREF 2CE4 B 1 210 UNP Q9RUV2 SODM_DEIRA 1 210
SEQRES 1 A 231 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 A 231 THR SER LEU TYR LYS LYS ALA LEU ALA TYR THR LEU PRO
SEQRES 3 A 231 GLN LEU PRO TYR ALA TYR ASP ALA LEU GLU PRO HIS ILE
SEQRES 4 A 231 ASP ALA ARG THR MET GLU ILE HIS HIS THR LYS HIS HIS
SEQRES 5 A 231 GLN THR TYR VAL ASP ASN ALA ASN LYS ALA LEU GLU GLY
SEQRES 6 A 231 THR GLU PHE ALA ASP LEU PRO VAL GLU GLN LEU ILE GLN
SEQRES 7 A 231 GLN LEU ASP ARG VAL PRO ALA ASP LYS LYS GLY ALA LEU
SEQRES 8 A 231 ARG ASN ASN ALA GLY GLY HIS ALA ASN HIS SER MET PHE
SEQRES 9 A 231 TRP GLN ILE MET GLY GLN GLY GLN GLY GLN ASN GLY ALA
SEQRES 10 A 231 ASN GLN PRO SER GLY GLU LEU LEU ASP ALA ILE ASN SER
SEQRES 11 A 231 ALA PHE GLY SER PHE ASP ALA PHE LYS GLN LYS PHE GLU
SEQRES 12 A 231 ASP ALA ALA LYS THR ARG PHE GLY SER GLY TRP ALA TRP
SEQRES 13 A 231 LEU VAL VAL LYS ASP GLY LYS LEU ASP VAL VAL SER THR
SEQRES 14 A 231 ALA ASN GLN ASP ASN PRO LEU MET GLY GLU ALA ILE ALA
SEQRES 15 A 231 GLY VAL SER GLY THR PRO ILE LEU GLY VAL ASP VAL TRP
SEQRES 16 A 231 GLU HIS ALA TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO
SEQRES 17 A 231 ASP TYR LEU ALA ALA PHE TRP ASN VAL VAL ASN TRP ASP
SEQRES 18 A 231 GLU VAL SER LYS ARG TYR ALA ALA ALA LYS
SEQRES 1 B 231 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 B 231 THR SER LEU TYR LYS LYS ALA LEU ALA TYR THR LEU PRO
SEQRES 3 B 231 GLN LEU PRO TYR ALA TYR ASP ALA LEU GLU PRO HIS ILE
SEQRES 4 B 231 ASP ALA ARG THR MET GLU ILE HIS HIS THR LYS HIS HIS
SEQRES 5 B 231 GLN THR TYR VAL ASP ASN ALA ASN LYS ALA LEU GLU GLY
SEQRES 6 B 231 THR GLU PHE ALA ASP LEU PRO VAL GLU GLN LEU ILE GLN
SEQRES 7 B 231 GLN LEU ASP ARG VAL PRO ALA ASP LYS LYS GLY ALA LEU
SEQRES 8 B 231 ARG ASN ASN ALA GLY GLY HIS ALA ASN HIS SER MET PHE
SEQRES 9 B 231 TRP GLN ILE MET GLY GLN GLY GLN GLY GLN ASN GLY ALA
SEQRES 10 B 231 ASN GLN PRO SER GLY GLU LEU LEU ASP ALA ILE ASN SER
SEQRES 11 B 231 ALA PHE GLY SER PHE ASP ALA PHE LYS GLN LYS PHE GLU
SEQRES 12 B 231 ASP ALA ALA LYS THR ARG PHE GLY SER GLY TRP ALA TRP
SEQRES 13 B 231 LEU VAL VAL LYS ASP GLY LYS LEU ASP VAL VAL SER THR
SEQRES 14 B 231 ALA ASN GLN ASP ASN PRO LEU MET GLY GLU ALA ILE ALA
SEQRES 15 B 231 GLY VAL SER GLY THR PRO ILE LEU GLY VAL ASP VAL TRP
SEQRES 16 B 231 GLU HIS ALA TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO
SEQRES 17 B 231 ASP TYR LEU ALA ALA PHE TRP ASN VAL VAL ASN TRP ASP
SEQRES 18 B 231 GLU VAL SER LYS ARG TYR ALA ALA ALA LYS
HET MN A1211 1
HET MN B1211 1
HETNAM MN MANGANESE (II) ION
FORMUL 3 MN 2(MN 2+)
FORMUL 5 HOH *365(H2 O1)
HELIX 1 1 ASP A 19 LYS A 29 1 11
HELIX 2 2 LYS A 29 GLU A 43 1 15
HELIX 3 3 PRO A 51 ILE A 56 1 6
HELIX 4 4 LYS A 66 ILE A 86 1 21
HELIX 5 5 SER A 100 GLY A 112 1 13
HELIX 6 6 SER A 113 THR A 127 1 15
HELIX 7 7 ASN A 153 MET A 156 5 4
HELIX 8 8 GLY A 157 GLY A 162 1 6
HELIX 9 9 TRP A 174 ALA A 177 5 4
HELIX 10 10 TYR A 178 GLN A 183 1 6
HELIX 11 11 ARG A 185 TRP A 194 1 10
HELIX 12 12 ASN A 198 LYS A 210 1 13
HELIX 13 13 ASP B 19 LYS B 29 1 11
HELIX 14 14 LYS B 29 GLU B 43 1 15
HELIX 15 15 PRO B 51 ILE B 56 1 6
HELIX 16 16 GLN B 57 VAL B 62 5 6
HELIX 17 17 PRO B 63 ILE B 86 1 24
HELIX 18 18 SER B 100 GLY B 112 1 13
HELIX 19 19 SER B 113 THR B 127 1 15
HELIX 20 20 ASN B 153 MET B 156 5 4
HELIX 21 21 GLY B 157 GLY B 162 1 6
HELIX 22 22 TRP B 174 ALA B 177 5 4
HELIX 23 23 TYR B 178 GLN B 183 1 6
HELIX 24 24 ARG B 185 TRP B 194 1 10
HELIX 25 25 ASN B 198 LYS B 210 1 13
SHEET 1 AA 3 LYS A 142 ALA A 149 0
SHEET 2 AA 3 GLY A 132 LYS A 139 -1 O TRP A 133 N THR A 148
SHEET 3 AA 3 THR A 166 ASP A 172 -1 O THR A 166 N VAL A 138
SHEET 1 BA 3 LYS B 142 ALA B 149 0
SHEET 2 BA 3 GLY B 132 LYS B 139 -1 O TRP B 133 N THR B 148
SHEET 3 BA 3 THR B 166 ASP B 172 -1 O THR B 166 N VAL B 138
LINK MN MN A1211 NE2 HIS A 26 1555 1555 2.22
LINK MN MN A1211 NE2 HIS A 80 1555 1555 2.03
LINK MN MN A1211 OD2 ASP A 172 1555 1555 1.90
LINK MN MN A1211 NE2 HIS A 176 1555 1555 2.21
LINK MN MN A1211 O HOH A2198 1555 1555 2.18
LINK MN MN B1211 NE2 HIS B 26 1555 1555 2.15
LINK MN MN B1211 NE2 HIS B 176 1555 1555 2.10
LINK MN MN B1211 O HOH B2167 1555 1555 2.20
LINK MN MN B1211 NE2 HIS B 80 1555 1555 2.16
LINK MN MN B1211 OD2 ASP B 172 1555 1555 1.96
CISPEP 1 GLU A 15 PRO A 16 0 -7.98
CISPEP 2 GLU B 15 PRO B 16 0 -2.08
SITE 1 AC1 5 HIS A 26 HIS A 80 ASP A 172 HIS A 176
SITE 2 AC1 5 HOH A2198
SITE 1 AC2 5 HIS B 26 HIS B 80 ASP B 172 HIS B 176
SITE 2 AC2 5 HOH B2167
CRYST1 44.280 83.210 59.520 90.00 110.18 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 0.022584 0.000000 0.008300 0.00000
SCALE2 0.000000 0.012018 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017900 0.00000
MTRIX1 1 0.995000 -0.091000 -0.043000 42.89740 1
MTRIX2 1 0.088000 0.994000 -0.061000 17.99276 1
MTRIX3 1 0.048000 0.057000 0.997000 56.18528 1
(ATOM LINES ARE NOT SHOWN.)
END
