HEADER OXIDOREDUCTASE 26-JAN-10 3LJF
TITLE THE X-RAY STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM
TITLE 2 PSEUDOALTEROMONAS HALOPLANKTIS (CRYSTAL FORM II)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IRON SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, C, B, D;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOALTEROMONAS HALOPLANKTIS;
SOURCE 3 ORGANISM_TAXID: 326442;
SOURCE 4 STRAIN: TAC 125;
SOURCE 5 GENE: SODB, PSHAA1215;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COLD ADAPTATION, SUPEROXIDE DISMUTASE, FLEXIBILITY, THERMAL
KEYWDS 2 STABILITY, PSYCHROPHILIC PROTEIN, METAL-BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MERLINO,I.RUSSO KRAUSS,B.ROSSI,M.CONTE,A.VERGARA,F.SICA
REVDAT 2 24-NOV-10 3LJF 1 JRNL
REVDAT 1 08-SEP-10 3LJF 0
JRNL AUTH A.MERLINO,I.RUSSO KRAUSS,I.CASTELLANO,E.DE VENDITTIS,
JRNL AUTH 2 B.ROSSI,M.CONTE,A.VERGARA,F.SICA
JRNL TITL STRUCTURE AND FLEXIBILITY IN COLD-ADAPTED IRON SUPEROXIDE
JRNL TITL 2 DISMUTASES: THE CASE OF THE ENZYME ISOLATED FROM
JRNL TITL 3 PSEUDOALTEROMONAS HALOPLANKTIS.
JRNL REF J.STRUCT.BIOL. V. 172 343 2010
JRNL REFN ISSN 1047-8477
JRNL PMID 20732427
JRNL DOI 10.1016/J.JSB.2010.08.008
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.MERLINO,I.RUSSO KRAUSS,I.CASTELLANO,E.DE VENDITTIS,
REMARK 1 AUTH 2 A.VERGARA,F.SICA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK 1 TITL 2 A PSYCHROPHILIC IRON SUPEROXIDE DISMUTASE FROM
REMARK 1 TITL 3 PSEUDOALTEROMONAS HALOPLANKTIS
REMARK 1 REF PROTEIN AND PEPTIDE LETTERS V. 15 415 2008
REMARK 1 REFN ISSN 0929-8665
REMARK 1 PMID 18473957
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 47141
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 SET) : 0.192
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4727
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6044
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 532
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LJF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057351.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51958
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.09200
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1ISA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF PROTEIN WERE OBTAINED
REMARK 280 USING 2.3-2.5M AMMONIUM SULPHATE, 10 MM FECL3, 100 MM HEPES PH
REMARK 280 7.0, 3% (V/V) ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP
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 51.89250
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 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: 1900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 5292 O HOH B 5330 2.13
REMARK 500 O HOH B 5411 O HOH B 5459 2.15
REMARK 500 O LYS D 46 O HOH D 5178 2.17
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 GLU C 108 CG GLU C 108 CD 0.103
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 LEU A 110 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 LEU A 154 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 ASP B 60 CB - CG - OD1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 VAL B 182 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 LEU D 154 CA - CB - CG ANGL. DEV. = 15.6 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 ASN A 140 -106.02 56.19
REMARK 500 ARG A 168 -124.24 49.31
REMARK 500 LYS C 29 -65.03 -105.62
REMARK 500 PHE C 47 -39.07 -32.17
REMARK 500 SER C 81 143.91 -176.86
REMARK 500 ASN C 83 25.24 49.00
REMARK 500 ASN C 140 -103.13 53.41
REMARK 500 TYR C 163 -3.56 -141.48
REMARK 500 ARG C 168 -125.62 49.46
REMARK 500 LYS B 29 -65.59 -105.07
REMARK 500 ASN B 140 -107.67 60.83
REMARK 500 TYR B 163 -5.79 -141.76
REMARK 500 ARG B 168 -128.61 48.96
REMARK 500 ASN D 140 -109.83 54.31
REMARK 500 ARG D 168 -131.61 51.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PRO C 82 45.9 L L OUTSIDE RANGE
REMARK 500 ASN C 83 24.5 L L OUTSIDE RANGE
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 FE A5000 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 157 OD2
REMARK 620 2 HIS A 73 NE2 110.9
REMARK 620 3 HIS A 26 NE2 98.4 91.1
REMARK 620 4 HIS A 161 NE2 124.5 124.1 88.2
REMARK 620 5 HOH A5004 O 79.0 90.5 177.3 92.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D5003 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 157 OD2
REMARK 620 2 HIS D 73 NE2 110.4
REMARK 620 3 HIS D 26 NE2 87.5 100.2
REMARK 620 4 HIS D 161 NE2 121.3 126.6 94.8
REMARK 620 5 HOH D1699 O 85.0 87.9 170.5 84.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C5002 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 157 OD2
REMARK 620 2 HIS C 161 NE2 123.4
REMARK 620 3 HIS C 73 NE2 112.5 124.0
REMARK 620 4 HIS C 26 NE2 90.7 87.6 95.8
REMARK 620 5 HOH C5006 O 84.9 95.4 85.3 175.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B5001 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 157 OD2
REMARK 620 2 HIS B 161 NE2 116.8
REMARK 620 3 HIS B 73 NE2 120.6 121.5
REMARK 620 4 HIS B 26 NE2 87.8 95.3 97.3
REMARK 620 5 HOH B5005 O 83.5 91.5 84.5 170.7
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 FE A 5000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE A 193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 5002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE C 195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE B 194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 5003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE D 196
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LIO RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE IRON SUPEROXIDE DISMUTASE FROM
REMARK 900 PSEUDOALTEROMONAS HALOPLANKTIS (CRYSTAL FORM I)
REMARK 900 RELATED ID: 3LJ9 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE IRON SUPEROXIDE DISMUTASE FROM
REMARK 900 PSEUDOALTEROMONAS HALOPLANKTIS IN COMPLEX WITH SODIUM AZIDE
DBREF 3LJF A 1 192 UNP P84612 SODF_PSEHT 1 192
DBREF 3LJF C 1 192 UNP P84612 SODF_PSEHT 1 192
DBREF 3LJF B 1 192 UNP P84612 SODF_PSEHT 1 192
DBREF 3LJF D 1 192 UNP P84612 SODF_PSEHT 1 192
SEQRES 1 A 192 ALA PHE GLU LEU PRO SER LEU PRO TYR ALA ILE ASP ALA
SEQRES 2 A 192 LEU GLU PRO HIS ILE SER LYS GLU THR LEU GLU PHE HIS
SEQRES 3 A 192 HIS GLY LYS HIS HIS ASN THR TYR VAL VAL LYS LEU ASN
SEQRES 4 A 192 GLY LEU ILE PRO GLY THR LYS PHE GLU ASN LYS SER LEU
SEQRES 5 A 192 GLU GLU ILE VAL CYS SER SER ASP GLY GLY VAL PHE ASN
SEQRES 6 A 192 ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASN
SEQRES 7 A 192 SER LEU SER PRO ASN GLY GLY GLY ALA PRO THR GLY ALA
SEQRES 8 A 192 VAL ALA ASP ALA ILE ASN ALA LYS TRP GLY SER PHE ASP
SEQRES 9 A 192 ALA PHE LYS GLU ALA LEU ASN ASP LYS ALA VAL ASN ASN
SEQRES 10 A 192 PHE GLY SER SER TRP THR TRP LEU VAL LYS LEU ALA ASP
SEQRES 11 A 192 GLY SER LEU ASP ILE VAL ASN THR SER ASN ALA ALA THR
SEQRES 12 A 192 PRO LEU THR ASP ASP GLY VAL THR PRO ILE LEU THR VAL
SEQRES 13 A 192 ASP LEU TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN
SEQRES 14 A 192 VAL ARG PRO ASP TYR LEU LYS GLY PHE TRP SER LEU VAL
SEQRES 15 A 192 ASN TRP GLU PHE ALA ASN ALA ASN PHE ALA
SEQRES 1 C 192 ALA PHE GLU LEU PRO SER LEU PRO TYR ALA ILE ASP ALA
SEQRES 2 C 192 LEU GLU PRO HIS ILE SER LYS GLU THR LEU GLU PHE HIS
SEQRES 3 C 192 HIS GLY LYS HIS HIS ASN THR TYR VAL VAL LYS LEU ASN
SEQRES 4 C 192 GLY LEU ILE PRO GLY THR LYS PHE GLU ASN LYS SER LEU
SEQRES 5 C 192 GLU GLU ILE VAL CYS SER SER ASP GLY GLY VAL PHE ASN
SEQRES 6 C 192 ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASN
SEQRES 7 C 192 SER LEU SER PRO ASN GLY GLY GLY ALA PRO THR GLY ALA
SEQRES 8 C 192 VAL ALA ASP ALA ILE ASN ALA LYS TRP GLY SER PHE ASP
SEQRES 9 C 192 ALA PHE LYS GLU ALA LEU ASN ASP LYS ALA VAL ASN ASN
SEQRES 10 C 192 PHE GLY SER SER TRP THR TRP LEU VAL LYS LEU ALA ASP
SEQRES 11 C 192 GLY SER LEU ASP ILE VAL ASN THR SER ASN ALA ALA THR
SEQRES 12 C 192 PRO LEU THR ASP ASP GLY VAL THR PRO ILE LEU THR VAL
SEQRES 13 C 192 ASP LEU TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN
SEQRES 14 C 192 VAL ARG PRO ASP TYR LEU LYS GLY PHE TRP SER LEU VAL
SEQRES 15 C 192 ASN TRP GLU PHE ALA ASN ALA ASN PHE ALA
SEQRES 1 B 192 ALA PHE GLU LEU PRO SER LEU PRO TYR ALA ILE ASP ALA
SEQRES 2 B 192 LEU GLU PRO HIS ILE SER LYS GLU THR LEU GLU PHE HIS
SEQRES 3 B 192 HIS GLY LYS HIS HIS ASN THR TYR VAL VAL LYS LEU ASN
SEQRES 4 B 192 GLY LEU ILE PRO GLY THR LYS PHE GLU ASN LYS SER LEU
SEQRES 5 B 192 GLU GLU ILE VAL CYS SER SER ASP GLY GLY VAL PHE ASN
SEQRES 6 B 192 ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASN
SEQRES 7 B 192 SER LEU SER PRO ASN GLY GLY GLY ALA PRO THR GLY ALA
SEQRES 8 B 192 VAL ALA ASP ALA ILE ASN ALA LYS TRP GLY SER PHE ASP
SEQRES 9 B 192 ALA PHE LYS GLU ALA LEU ASN ASP LYS ALA VAL ASN ASN
SEQRES 10 B 192 PHE GLY SER SER TRP THR TRP LEU VAL LYS LEU ALA ASP
SEQRES 11 B 192 GLY SER LEU ASP ILE VAL ASN THR SER ASN ALA ALA THR
SEQRES 12 B 192 PRO LEU THR ASP ASP GLY VAL THR PRO ILE LEU THR VAL
SEQRES 13 B 192 ASP LEU TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN
SEQRES 14 B 192 VAL ARG PRO ASP TYR LEU LYS GLY PHE TRP SER LEU VAL
SEQRES 15 B 192 ASN TRP GLU PHE ALA ASN ALA ASN PHE ALA
SEQRES 1 D 192 ALA PHE GLU LEU PRO SER LEU PRO TYR ALA ILE ASP ALA
SEQRES 2 D 192 LEU GLU PRO HIS ILE SER LYS GLU THR LEU GLU PHE HIS
SEQRES 3 D 192 HIS GLY LYS HIS HIS ASN THR TYR VAL VAL LYS LEU ASN
SEQRES 4 D 192 GLY LEU ILE PRO GLY THR LYS PHE GLU ASN LYS SER LEU
SEQRES 5 D 192 GLU GLU ILE VAL CYS SER SER ASP GLY GLY VAL PHE ASN
SEQRES 6 D 192 ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASN
SEQRES 7 D 192 SER LEU SER PRO ASN GLY GLY GLY ALA PRO THR GLY ALA
SEQRES 8 D 192 VAL ALA ASP ALA ILE ASN ALA LYS TRP GLY SER PHE ASP
SEQRES 9 D 192 ALA PHE LYS GLU ALA LEU ASN ASP LYS ALA VAL ASN ASN
SEQRES 10 D 192 PHE GLY SER SER TRP THR TRP LEU VAL LYS LEU ALA ASP
SEQRES 11 D 192 GLY SER LEU ASP ILE VAL ASN THR SER ASN ALA ALA THR
SEQRES 12 D 192 PRO LEU THR ASP ASP GLY VAL THR PRO ILE LEU THR VAL
SEQRES 13 D 192 ASP LEU TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN
SEQRES 14 D 192 VAL ARG PRO ASP TYR LEU LYS GLY PHE TRP SER LEU VAL
SEQRES 15 D 192 ASN TRP GLU PHE ALA ASN ALA ASN PHE ALA
HET FE A5000 1
HET TRE A 193 23
HET FE C5002 1
HET TRE C 195 23
HET FE B5001 1
HET TRE B 194 23
HET FE D5003 1
HET TRE D 196 23
HETNAM FE FE (III) ION
HETNAM TRE TREHALOSE
HETSYN TRE ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-GLUCOPYRANOSIDE
FORMUL 5 FE 4(FE 3+)
FORMUL 6 TRE 4(C12 H22 O11)
FORMUL 13 HOH *532(H2 O)
HELIX 1 1 SER A 19 HIS A 27 1 9
HELIX 2 2 LYS A 29 ILE A 42 1 14
HELIX 3 3 THR A 45 ASN A 49 5 5
HELIX 4 4 SER A 51 SER A 59 1 9
HELIX 5 5 ASP A 60 SER A 79 1 20
HELIX 6 6 THR A 89 GLY A 101 1 13
HELIX 7 7 SER A 102 ASN A 116 1 15
HELIX 8 8 THR A 143 ASP A 147 5 5
HELIX 9 9 TRP A 159 ALA A 162 5 4
HELIX 10 10 TYR A 163 ARG A 168 1 6
HELIX 11 11 VAL A 170 VAL A 182 1 13
HELIX 12 12 ASN A 183 ALA A 192 1 10
HELIX 13 13 SER C 19 HIS C 27 1 9
HELIX 14 14 LYS C 29 ILE C 42 1 14
HELIX 15 15 THR C 45 ASN C 49 5 5
HELIX 16 16 SER C 51 SER C 59 1 9
HELIX 17 17 ASP C 60 SER C 79 1 20
HELIX 18 18 THR C 89 GLY C 101 1 13
HELIX 19 19 SER C 102 ASN C 116 1 15
HELIX 20 20 THR C 143 ASP C 147 5 5
HELIX 21 21 TRP C 159 ALA C 162 5 4
HELIX 22 22 TYR C 163 ARG C 168 1 6
HELIX 23 23 VAL C 170 VAL C 182 1 13
HELIX 24 24 ASN C 183 ALA C 192 1 10
HELIX 25 25 SER B 19 HIS B 27 1 9
HELIX 26 26 LYS B 29 ILE B 42 1 14
HELIX 27 27 THR B 45 LYS B 50 5 6
HELIX 28 28 SER B 51 CYS B 57 1 7
HELIX 29 29 ASP B 60 SER B 79 1 20
HELIX 30 30 THR B 89 GLY B 101 1 13
HELIX 31 31 SER B 102 ASN B 116 1 15
HELIX 32 32 THR B 143 ASP B 147 5 5
HELIX 33 33 TRP B 159 ALA B 162 5 4
HELIX 34 34 TYR B 163 ARG B 168 1 6
HELIX 35 35 VAL B 170 VAL B 182 1 13
HELIX 36 36 ASN B 183 ALA B 192 1 10
HELIX 37 37 SER D 19 HIS D 27 1 9
HELIX 38 38 LYS D 29 ILE D 42 1 14
HELIX 39 39 THR D 45 LYS D 50 5 6
HELIX 40 40 SER D 51 SER D 58 1 8
HELIX 41 41 ASP D 60 SER D 79 1 20
HELIX 42 42 THR D 89 GLY D 101 1 13
HELIX 43 43 SER D 102 ASN D 116 1 15
HELIX 44 44 THR D 143 ASP D 147 5 5
HELIX 45 45 TRP D 159 ALA D 162 5 4
HELIX 46 46 TYR D 163 ARG D 168 1 6
HELIX 47 47 VAL D 170 VAL D 182 1 13
HELIX 48 48 ASN D 183 ALA D 192 1 10
SHEET 1 A 3 LEU A 133 SER A 139 0
SHEET 2 A 3 SER A 121 LYS A 127 -1 N TRP A 124 O VAL A 136
SHEET 3 A 3 THR A 151 ASP A 157 -1 O THR A 151 N LYS A 127
SHEET 1 B 3 LEU C 133 SER C 139 0
SHEET 2 B 3 SER C 121 LYS C 127 -1 N TRP C 124 O VAL C 136
SHEET 3 B 3 THR C 151 ASP C 157 -1 O THR C 151 N LYS C 127
SHEET 1 C 3 LEU B 133 SER B 139 0
SHEET 2 C 3 SER B 121 LYS B 127 -1 N TRP B 124 O VAL B 136
SHEET 3 C 3 THR B 151 ASP B 157 -1 O THR B 151 N LYS B 127
SHEET 1 D 3 LEU D 133 SER D 139 0
SHEET 2 D 3 SER D 121 LYS D 127 -1 N TRP D 124 O VAL D 136
SHEET 3 D 3 THR D 151 ASP D 157 -1 O THR D 151 N LYS D 127
LINK OD2 ASP A 157 FE FE A5000 1555 1555 1.87
LINK OD2 ASP D 157 FE FE D5003 1555 1555 1.95
LINK OD2 ASP C 157 FE FE C5002 1555 1555 1.96
LINK NE2 HIS A 73 FE FE A5000 1555 1555 2.01
LINK OD2 ASP B 157 FE FE B5001 1555 1555 2.02
LINK NE2 HIS C 161 FE FE C5002 1555 1555 2.02
LINK NE2 HIS B 161 FE FE B5001 1555 1555 2.03
LINK NE2 HIS A 26 FE FE A5000 1555 1555 2.06
LINK NE2 HIS C 73 FE FE C5002 1555 1555 2.06
LINK NE2 HIS D 73 FE FE D5003 1555 1555 2.08
LINK NE2 HIS D 26 FE FE D5003 1555 1555 2.12
LINK NE2 HIS B 73 FE FE B5001 1555 1555 2.13
LINK NE2 HIS D 161 FE FE D5003 1555 1555 2.14
LINK NE2 HIS B 26 FE FE B5001 1555 1555 2.17
LINK NE2 HIS C 26 FE FE C5002 1555 1555 2.18
LINK NE2 HIS A 161 FE FE A5000 1555 1555 2.21
LINK FE FE B5001 O HOH B5005 1555 1555 2.08
LINK FE FE D5003 O HOH D1699 1555 1555 2.19
LINK FE FE A5000 O HOH A5004 1555 1555 2.20
LINK FE FE C5002 O HOH C5006 1555 1555 2.39
CISPEP 1 GLU A 15 PRO A 16 0 -0.52
CISPEP 2 GLU C 15 PRO C 16 0 -0.84
CISPEP 3 GLU B 15 PRO B 16 0 0.72
CISPEP 4 GLU D 15 PRO D 16 0 -0.31
SITE 1 AC1 5 HIS A 26 HIS A 73 ASP A 157 HIS A 161
SITE 2 AC1 5 HOH A5004
SITE 1 AC2 12 ASN A 116 ASN A 117 PHE A 118 ASN A 137
SITE 2 AC2 12 SER A 139 HOH A5130 HOH A5179 HOH A5340
SITE 3 AC2 12 HOH A5376 GLY B 61 GLY B 62 HOH B5366
SITE 1 AC3 5 HIS C 26 HIS C 73 ASP C 157 HIS C 161
SITE 2 AC3 5 HOH C5006
SITE 1 AC4 10 ASN C 116 ASN C 117 PHE C 118 ASN C 137
SITE 2 AC4 10 SER C 139 HOH C1720 HOH C1727 HOH C5191
SITE 3 AC4 10 GLY D 61 GLY D 62
SITE 1 AC5 5 HIS B 26 HIS B 73 ASP B 157 HIS B 161
SITE 2 AC5 5 HOH B5005
SITE 1 AC6 13 GLY A 61 GLY A 62 LYS B 113 ASN B 116
SITE 2 AC6 13 ASN B 117 PHE B 118 ASN B 137 HOH B1736
SITE 3 AC6 13 HOH B5180 HOH B5252 HOH B5269 HOH B5337
SITE 4 AC6 13 HOH B5379
SITE 1 AC7 5 HIS D 26 HIS D 73 ASP D 157 HIS D 161
SITE 2 AC7 5 HOH D1699
SITE 1 AC8 14 GLY C 61 GLY C 62 ASN C 65 LYS D 113
SITE 2 AC8 14 ASN D 116 ASN D 117 PHE D 118 ASN D 137
SITE 3 AC8 14 HOH D1723 HOH D1745 HOH D5314 HOH D5394
SITE 4 AC8 14 HOH D5408 HOH D5414
CRYST1 50.476 103.785 90.251 90.00 103.81 90.00 P 1 21 1 8
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 0.019811 0.000000 0.004870 0.00000
SCALE2 0.000000 0.009635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011410 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
