HEADER OXIDOREDUCTASE 31-AUG-98 1BS3
TITLE P.SHERMANII SOD(FE+3) FLUORIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SOD;
COMPND 5 EC: 1.15.1.1;
COMPND 6 OTHER_DETAILS: COMPETITIVELY INHIBITED BY FLOURIDE. FLUORIDE OCCUPIES
COMPND 7 SUBSTRATE BINDING SITE.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROPIONIBACTERIUM FREUDENREICHII SUBSP.
SOURCE 3 SHERMANII;
SOURCE 4 ORGANISM_TAXID: 1752;
SOURCE 5 STRAIN: PZ3;
SOURCE 6 ATCC: GERMAN COLLECTION OF MICROORGANISMS (DSM) 4902;
SOURCE 7 COLLECTION: GERMAN COLLECTION OF MICROORGANISMS (DSM) 4902;
SOURCE 8 CELLULAR_LOCATION: CYTOPLASM
KEYWDS SUPEROXIDE DISMUTASE, FLUORIDE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SCHMIDT
REVDAT 6 09-AUG-23 1BS3 1 REMARK
REVDAT 5 28-JUN-23 1BS3 1 REMARK LINK
REVDAT 4 13-JUL-11 1BS3 1 VERSN
REVDAT 3 24-FEB-09 1BS3 1 VERSN
REVDAT 2 01-APR-03 1BS3 1 JRNL
REVDAT 1 15-JUN-99 1BS3 0
JRNL AUTH M.SCHMIDT
JRNL TITL MANIPULATING THE COORDINATION MUMBER OF THE FERRIC IRON
JRNL TITL 2 WITHIN THE CAMBIALISTIC SUPEROXIDE DISMUTASE OF
JRNL TITL 3 PROPIONIBACTERIUM SHERMANII BY CHANGING THE PH-VALUE A
JRNL TITL 4 CRYSTALLOGRAPHIC ANALYSIS
JRNL REF EUR.J.BIOCHEM. V. 262 117 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10231372
JRNL DOI 10.1046/J.1432-1327.1999.00359.X
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.500
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 78.2
REMARK 3 NUMBER OF REFLECTIONS : 41693
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) : 0.174
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4178
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3691
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 439
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 : 3208
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 478
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.10
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) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.250
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.500 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.200 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.300 ; 2.500
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.PEP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IRON AND FLUORIDE REFINED UNRESTRAINED
REMARK 4
REMARK 4 1BS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172045.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-97
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 6.1
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 : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45799
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 39.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.1
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.14800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 1AR5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.1
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 54.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 39.71000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.64000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.71000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.64000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.20000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.71000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.64000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.20000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.71000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.64000
REMARK 290 SMTRY3 8 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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 12490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 BIOMT1 2 -1.000000 0.000000 0.000000 79.42000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 54.20000
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 FE FE B 202 F F B 203 1.80
REMARK 500 FE FE A 202 F F A 203 1.89
REMARK 500 NE2 HIS A 75 F F A 203 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 433 O HOH B 433 3655 0.66
REMARK 500 O HOH A 334 O HOH A 334 3655 1.13
REMARK 500 O HOH B 347 O HOH B 347 3555 1.33
REMARK 500 O HOH A 343 O HOH A 343 4566 1.97
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 30 -60.11 -105.80
REMARK 500 ASP A 94 -134.43 55.98
REMARK 500 ASP A 145 -119.82 57.56
REMARK 500 LYS A 172 -133.36 56.78
REMARK 500 LYS B 30 -60.88 -104.06
REMARK 500 ASP B 94 -140.87 53.43
REMARK 500 ASP B 145 -116.41 57.31
REMARK 500 ASN B 149 45.92 70.21
REMARK 500 PHE B 167 -13.95 -144.92
REMARK 500 LYS B 172 -132.78 57.32
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 357 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH A 405 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH B 336 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 394 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH B 448 DISTANCE = 5.95 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 FE A 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 27 NE2
REMARK 620 2 HIS A 75 NE2 89.1
REMARK 620 3 ASP A 161 OD2 85.6 101.5
REMARK 620 4 HIS A 165 NE2 89.8 145.3 113.0
REMARK 620 5 HOH A 204 O 176.6 91.5 90.9 91.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 27 NE2
REMARK 620 2 HIS B 75 NE2 92.2
REMARK 620 3 ASP B 161 OD2 84.3 104.7
REMARK 620 4 HIS B 165 NE2 92.4 144.1 111.2
REMARK 620 5 HOH B 204 O 176.3 90.2 92.4 87.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FEA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: FERRIC IRON (FE(III)), SIX FOLD COORDINATED
REMARK 800 FLUORIDE AT THE POSSIBLE SUBSTRATE BINDING SITE ACTIVITY
REMARK 800 COMPETITIVELY HAMPERED
REMARK 800
REMARK 800 SITE_IDENTIFIER: FEB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: FERRIC IRON (FE(III)), SIX FOLD COORDINATED
REMARK 800 FLUORIDE AT THE POSSIBLE SUBSTRATE BINDING SITE ACTIVITY
REMARK 800 COMPETITIVELY HAMPERED
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F B 203
DBREF 1BS3 A 1 201 UNP P80293 SODM_PROFR 1 201
DBREF 1BS3 B 1 201 UNP P80293 SODM_PROFR 1 201
SEQRES 1 A 201 ALA VAL TYR THR LEU PRO GLU LEU PRO TYR ASP TYR SER
SEQRES 2 A 201 ALA LEU GLU PRO TYR ILE SER GLY GLU ILE MET GLU LEU
SEQRES 3 A 201 HIS HIS ASP LYS HIS HIS LYS ALA TYR VAL ASP GLY ALA
SEQRES 4 A 201 ASN THR ALA LEU ASP LYS LEU ALA GLU ALA ARG ASP LYS
SEQRES 5 A 201 ALA ASP PHE GLY ALA ILE ASN LYS LEU GLU LYS ASP LEU
SEQRES 6 A 201 ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS SER VAL PHE
SEQRES 7 A 201 TRP LYS ASN MET ALA PRO LYS GLY SER ALA PRO GLU ARG
SEQRES 8 A 201 PRO THR ASP GLU LEU GLY ALA ALA ILE ASP GLU PHE PHE
SEQRES 9 A 201 GLY SER PHE ASP ASN MET LYS ALA GLN PHE THR ALA ALA
SEQRES 10 A 201 ALA THR GLY ILE GLN GLY SER GLY TRP ALA SER LEU VAL
SEQRES 11 A 201 TRP ASP PRO LEU GLY LYS ARG ILE ASN THR LEU GLN PHE
SEQRES 12 A 201 TYR ASP HIS GLN ASN ASN LEU PRO ALA GLY SER ILE PRO
SEQRES 13 A 201 LEU LEU GLN LEU ASP MET TRP GLU HIS ALA PHE TYR LEU
SEQRES 14 A 201 GLN TYR LYS ASN VAL LYS GLY ASP TYR VAL LYS SER TRP
SEQRES 15 A 201 TRP ASN VAL VAL ASN TRP ASP ASP VAL ALA LEU ARG PHE
SEQRES 16 A 201 SER GLU ALA ARG VAL ALA
SEQRES 1 B 201 ALA VAL TYR THR LEU PRO GLU LEU PRO TYR ASP TYR SER
SEQRES 2 B 201 ALA LEU GLU PRO TYR ILE SER GLY GLU ILE MET GLU LEU
SEQRES 3 B 201 HIS HIS ASP LYS HIS HIS LYS ALA TYR VAL ASP GLY ALA
SEQRES 4 B 201 ASN THR ALA LEU ASP LYS LEU ALA GLU ALA ARG ASP LYS
SEQRES 5 B 201 ALA ASP PHE GLY ALA ILE ASN LYS LEU GLU LYS ASP LEU
SEQRES 6 B 201 ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS SER VAL PHE
SEQRES 7 B 201 TRP LYS ASN MET ALA PRO LYS GLY SER ALA PRO GLU ARG
SEQRES 8 B 201 PRO THR ASP GLU LEU GLY ALA ALA ILE ASP GLU PHE PHE
SEQRES 9 B 201 GLY SER PHE ASP ASN MET LYS ALA GLN PHE THR ALA ALA
SEQRES 10 B 201 ALA THR GLY ILE GLN GLY SER GLY TRP ALA SER LEU VAL
SEQRES 11 B 201 TRP ASP PRO LEU GLY LYS ARG ILE ASN THR LEU GLN PHE
SEQRES 12 B 201 TYR ASP HIS GLN ASN ASN LEU PRO ALA GLY SER ILE PRO
SEQRES 13 B 201 LEU LEU GLN LEU ASP MET TRP GLU HIS ALA PHE TYR LEU
SEQRES 14 B 201 GLN TYR LYS ASN VAL LYS GLY ASP TYR VAL LYS SER TRP
SEQRES 15 B 201 TRP ASN VAL VAL ASN TRP ASP ASP VAL ALA LEU ARG PHE
SEQRES 16 B 201 SER GLU ALA ARG VAL ALA
HET FE A 202 1
HET F A 203 1
HET FE B 202 1
HET F B 203 1
HETNAM FE FE (III) ION
HETNAM F FLUORIDE ION
FORMUL 3 FE 2(FE 3+)
FORMUL 4 F 2(F 1-)
FORMUL 7 HOH *478(H2 O)
HELIX 1 1 GLY A 21 ASP A 29 1 9
HELIX 2 2 HIS A 31 LYS A 52 1 22
HELIX 3 3 ILE A 58 LYS A 80 1 23
HELIX 4 4 ASP A 94 PHE A 104 1 11
HELIX 5 5 PHE A 107 THR A 119 1 13
HELIX 6 6 GLU A 164 ALA A 166 5 3
HELIX 7 7 TYR A 168 TYR A 171 1 4
HELIX 8 8 LYS A 175 VAL A 185 1 11
HELIX 9 9 TRP A 188 ALA A 198 1 11
HELIX 10 10 GLY B 21 ASP B 29 1 9
HELIX 11 11 HIS B 31 LYS B 52 1 22
HELIX 12 12 ILE B 58 LYS B 80 1 23
HELIX 13 13 ASP B 94 PHE B 104 1 11
HELIX 14 14 PHE B 107 THR B 119 1 13
HELIX 15 15 GLU B 164 ALA B 166 5 3
HELIX 16 16 TYR B 168 TYR B 171 1 4
HELIX 17 17 LYS B 175 VAL B 185 1 11
HELIX 18 18 TRP B 188 ARG B 199 1 12
SHEET 1 A 3 ARG A 137 TYR A 144 0
SHEET 2 A 3 GLY A 125 ASP A 132 -1 N ASP A 132 O ARG A 137
SHEET 3 A 3 ILE A 155 ASP A 161 -1 N LEU A 160 O ALA A 127
SHEET 1 B 3 ARG B 137 TYR B 144 0
SHEET 2 B 3 GLY B 125 ASP B 132 -1 N ASP B 132 O ARG B 137
SHEET 3 B 3 ILE B 155 ASP B 161 -1 N LEU B 160 O ALA B 127
LINK NE2 HIS A 27 FE FE A 202 1555 1555 2.17
LINK NE2 HIS A 75 FE FE A 202 1555 1555 2.15
LINK OD2 ASP A 161 FE FE A 202 1555 1555 1.83
LINK NE2 HIS A 165 FE FE A 202 1555 1555 2.09
LINK FE FE A 202 O HOH A 204 1555 1555 2.10
LINK NE2 HIS B 27 FE FE B 202 1555 1555 2.15
LINK NE2 HIS B 75 FE FE B 202 1555 1555 2.18
LINK OD2 ASP B 161 FE FE B 202 1555 1555 1.85
LINK NE2 HIS B 165 FE FE B 202 1555 1555 2.16
LINK FE FE B 202 O HOH B 204 1555 1555 2.10
CISPEP 1 GLU A 16 PRO A 17 0 0.01
CISPEP 2 GLU B 16 PRO B 17 0 -0.07
SITE 1 FEA 7 FE A 202 HIS A 27 HIS A 75 ASP A 161
SITE 2 FEA 7 HIS A 165 F A 203 HOH A 204
SITE 1 FEB 7 FE B 202 HIS B 27 HIS B 75 ASP B 161
SITE 2 FEB 7 HIS B 165 F B 203 HOH B 204
SITE 1 AC1 6 HIS A 27 HIS A 75 ASP A 161 HIS A 165
SITE 2 AC1 6 F A 203 HOH A 204
SITE 1 AC2 7 HIS A 27 TYR A 35 HIS A 75 ASP A 161
SITE 2 AC2 7 HIS A 165 FE A 202 HOH A 204
SITE 1 AC3 6 HIS B 27 HIS B 75 ASP B 161 HIS B 165
SITE 2 AC3 6 F B 203 HOH B 204
SITE 1 AC4 7 HIS B 27 TYR B 35 HIS B 75 ASP B 161
SITE 2 AC4 7 HIS B 165 FE B 202 HOH B 204
CRYST1 79.420 85.280 108.400 90.00 90.00 90.00 C 2 2 21 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 0.012591 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011726 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009225 0.00000
MTRIX1 1 0.202800 -0.001900 -0.979200 58.19220 1
MTRIX2 1 0.003600 -1.000000 0.002700 32.91420 1
MTRIX3 1 -0.979200 -0.004000 -0.202800 71.53430 1
(ATOM LINES ARE NOT SHOWN.)
END
