HEADER OXIDOREDUCTASE 28-MAR-01 1IBB
TITLE X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT W83F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CU,ZN SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHOTOBACTERIUM LEIOGNATHI;
SOURCE 3 ORGANISM_TAXID: 658;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROKARYOTIC SUPEROXIDE DISMUTASE, SUBUNIT INTERACTION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.STROPPOLO,A.PESCE,M.D'ORAZIO,P.O'NEILL,D.BORDO,C.ROSANO,M.MILANI,
AUTHOR 2 A.BATTISTONI,M.BOLOGNESI,A.DESIDERI
REVDAT 5 03-APR-24 1IBB 1 REMARK
REVDAT 4 27-OCT-21 1IBB 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1IBB 1 VERSN
REVDAT 2 01-APR-03 1IBB 1 JRNL
REVDAT 1 09-MAY-01 1IBB 0
JRNL AUTH M.E.STROPPOLO,A.PESCE,M.D'ORAZIO,P.O'NEILL,D.BORDO,C.ROSANO,
JRNL AUTH 2 M.MILANI,A.BATTISTONI,M.BOLOGNESI,A.DESIDERI
JRNL TITL SINGLE MUTATIONS AT THE SUBUNIT INTERFACE MODULATE COPPER
JRNL TITL 2 REACTIVITY IN PHOTOBACTERIUM LEIOGNATHI CU,ZN SUPEROXIDE
JRNL TITL 3 DISMUTASE.
JRNL REF J.MOL.BIOL. V. 308 555 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11327787
JRNL DOI 10.1006/JMBI.2001.4606
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 7985
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 790
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 : 1107
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.00
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.220
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 1IBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013123.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-99
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 4.5
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7985
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : 0.17000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: P.LEIOGNATHI CU,ZN SOD WILD TYPE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8K, NACL, PH 4.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 301K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 43.56000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 25.14938
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 32.79733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 43.56000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 25.14938
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 32.79733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 43.56000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 25.14938
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 32.79733
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 43.56000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 25.14938
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 32.79733
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 43.56000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 25.14938
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 32.79733
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 43.56000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 25.14938
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 32.79733
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 50.29876
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 65.59467
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 50.29876
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 65.59467
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 50.29876
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 65.59467
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 50.29876
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 65.59467
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 50.29876
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 65.59467
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 50.29876
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 65.59467
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 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 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 100.59751
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 32.79733
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 1 N CB CG CD OE1 NE2
REMARK 480 ASP A 2 OD2
REMARK 480 LEU A 3 CD1 CD2
REMARK 480 LYS A 6 CD CE NZ
REMARK 480 GLN A 11 CD OE1 NE2
REMARK 480 LYS A 14 CD CE NZ
REMARK 480 ASP A 58 OD2
REMARK 480 LYS A 60 CE NZ
REMARK 480 ASN A 100 OD1 ND2
REMARK 480 LYS A 115 CE NZ
REMARK 480 LYS A 136 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
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 ASP A 86 44.66 -92.20
REMARK 500 HIS A 88 124.80 -38.42
REMARK 500 ASP A 129 107.99 -162.45
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 202 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 45 ND1
REMARK 620 2 HIS A 47 NE2 146.8
REMARK 620 3 HIS A 70 NE2 77.1 94.6
REMARK 620 4 HIS A 125 NE2 98.3 112.0 126.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 70 ND1
REMARK 620 2 HIS A 79 ND1 106.0
REMARK 620 3 HIS A 88 ND1 103.7 119.5
REMARK 620 4 ASP A 91 OD1 110.5 92.3 123.8
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 ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BZO RELATED DB: PDB
REMARK 900 P.LEIOGNATHI CU,ZN SOD WILD TYPE
REMARK 900 RELATED ID: 1IB5 RELATED DB: PDB
REMARK 900 P.LEIOGNATHI CU,ZN SOD W83Y MUTATION
REMARK 900 RELATED ID: 1IBD RELATED DB: PDB
REMARK 900 P.LEIOGNATHI CU,ZN SOD V29A MUTATION
REMARK 900 RELATED ID: 1IBF RELATED DB: PDB
REMARK 900 P.LEIOGNATHI CU,ZN SOD V29G MUTATION
REMARK 900 RELATED ID: 1IBH RELATED DB: PDB
REMARK 900 P.LEIOGNATHI CU,ZN SOD M41I MUTATION
DBREF 1IBB A 1 151 UNP P00446 SODC_PHOLE 23 173
SEQADV 1IBB ILE A 31 UNP P00446 THR 53 CONFLICT
SEQADV 1IBB PHE A 83 UNP P00446 TRP 105 ENGINEERED MUTATION
SEQRES 1 A 151 GLN ASP LEU THR VAL LYS MET THR ASP LEU GLN THR GLY
SEQRES 2 A 151 LYS PRO VAL GLY THR ILE GLU LEU SER GLN ASN LYS TYR
SEQRES 3 A 151 GLY VAL VAL PHE ILE PRO GLU LEU ALA ASP LEU THR PRO
SEQRES 4 A 151 GLY MET HIS GLY PHE HIS ILE HIS GLN ASN GLY SER CYS
SEQRES 5 A 151 ALA SER SER GLU LYS ASP GLY LYS VAL VAL LEU GLY GLY
SEQRES 6 A 151 ALA ALA GLY GLY HIS TYR ASP PRO GLU HIS THR ASN LYS
SEQRES 7 A 151 HIS GLY PHE PRO PHE THR ASP ASP ASN HIS LYS GLY ASP
SEQRES 8 A 151 LEU PRO ALA LEU PHE VAL SER ALA ASN GLY LEU ALA THR
SEQRES 9 A 151 ASN PRO VAL LEU ALA PRO ARG LEU THR LEU LYS GLU LEU
SEQRES 10 A 151 LYS GLY HIS ALA ILE MET ILE HIS ALA GLY GLY ASP ASN
SEQRES 11 A 151 HIS SER ASP MET PRO LYS ALA LEU GLY GLY GLY GLY ALA
SEQRES 12 A 151 ARG VAL ALA CYS GLY VAL ILE GLN
HET ZN A 201 1
HET CU A 202 1
HETNAM ZN ZINC ION
HETNAM CU COPPER (II) ION
FORMUL 2 ZN ZN 2+
FORMUL 3 CU CU 2+
FORMUL 4 HOH *49(H2 O)
HELIX 1 1 GLY A 64 GLY A 68 5 5
HELIX 2 2 THR A 113 LYS A 118 1 6
HELIX 3 3 LYS A 136 GLY A 141 5 6
SHEET 1 A 7 PHE A 44 HIS A 47 0
SHEET 2 A 7 ALA A 121 HIS A 125 -1 O ALA A 121 N HIS A 47
SHEET 3 A 7 ARG A 144 VAL A 149 -1 N VAL A 145 O ILE A 124
SHEET 4 A 7 ASP A 2 ASP A 9 -1 N THR A 8 O CYS A 147
SHEET 5 A 7 PRO A 15 ASN A 24 -1 N VAL A 16 O MET A 7
SHEET 6 A 7 GLY A 27 LEU A 34 -1 O GLY A 27 N ASN A 24
SHEET 7 A 7 VAL A 107 ALA A 109 -1 O VAL A 107 N PHE A 30
SHEET 1 B 2 GLY A 40 HIS A 42 0
SHEET 2 B 2 LEU A 95 VAL A 97 -1 O LEU A 95 N HIS A 42
SHEET 1 C 2 SER A 55 LYS A 57 0
SHEET 2 C 2 LYS A 60 VAL A 62 -1 O LYS A 60 N LYS A 57
SSBOND 1 CYS A 52 CYS A 147 1555 1555 2.03
LINK ND1 HIS A 45 CU CU A 202 1555 1555 2.12
LINK NE2 HIS A 47 CU CU A 202 1555 1555 2.24
LINK ND1 HIS A 70 ZN ZN A 201 1555 1555 2.08
LINK NE2 HIS A 70 CU CU A 202 1555 1555 2.70
LINK ND1 HIS A 79 ZN ZN A 201 1555 1555 2.22
LINK ND1 HIS A 88 ZN ZN A 201 1555 1555 2.16
LINK OD1 ASP A 91 ZN ZN A 201 1555 1555 1.88
LINK NE2 HIS A 125 CU CU A 202 1555 1555 2.14
CISPEP 1 MET A 134 PRO A 135 0 -0.12
SITE 1 AC1 4 HIS A 70 HIS A 79 HIS A 88 ASP A 91
SITE 1 AC2 4 HIS A 45 HIS A 47 HIS A 70 HIS A 125
CRYST1 87.120 87.120 98.392 90.00 90.00 120.00 H 3 2 18
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 0.011478 0.006627 0.000000 0.00000
SCALE2 0.000000 0.013254 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010163 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
