HEADER OXIDOREDUCTASE 03-OCT-01 1GN6
TITLE G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE
TITLE 2 DISMUTASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 EXPRESSION_SYSTEM: MYCOBACTERIUM VACCAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1810
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.BUNTING,J.B.COOPER,S.SAWARD,P.T.ERSKINE,M.O.BADASSO,
AUTHOR 2 S.P.WOOD,Y.ZHANG,D.B.YOUNG
REVDAT 2 24-FEB-09 1GN6 1 VERSN
REVDAT 1 05-OCT-01 1GN6 0
JRNL AUTH J.B.COOPER,S.SAWARD,P.T.ERSKINE,M.O.BADASSO,
JRNL AUTH 2 S.P.WOOD,Y.ZHANG,D.B.YOUNG
JRNL TITL X-RAY STRUCTURE ANALYSIS OF AN ENGINEERED
JRNL TITL 2 FE-SUPEROXIDE DISMUTASE GLY-ALA MUTANT WITH
JRNL TITL 3 SIGNIFICANTLY REDUCED STABILITY TO DENATURANT
JRNL REF FEBS LETT. V. 387 105 1996
JRNL REFN ISSN 0014-5793
JRNL PMID 8674528
JRNL DOI 10.1016/0014-5793(96)00490-5
REMARK 2
REMARK 2 RESOLUTION. 2.9 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CCP4
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.9
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 3 NUMBER OF REFLECTIONS : 14468
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6276
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 360
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.013 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.030 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.011 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GN6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-01.
REMARK 100 THE PDBE ID CODE IS EBI-8657.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60000
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.15400
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: OTHER
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 7.0,
REMARK 280 25% PEG 6000, PROTEIN CONCENTRATION = 3 MG/ML,
REMARK 280 4 DEGREES CENTIGRADE.
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 42.80000
REMARK 290 SMTRY3 2 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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 1
REMARK 465 GLN A 200
REMARK 465 THR A 201
REMARK 465 LYS A 202
REMARK 465 GLY A 203
REMARK 465 LEU A 204
REMARK 465 ILE A 205
REMARK 465 PHE A 206
REMARK 465 GLY A 207
REMARK 465 MET B 1
REMARK 465 GLN B 200
REMARK 465 THR B 201
REMARK 465 LYS B 202
REMARK 465 GLY B 203
REMARK 465 LEU B 204
REMARK 465 ILE B 205
REMARK 465 PHE B 206
REMARK 465 GLY B 207
REMARK 465 MET C 1
REMARK 465 GLN C 200
REMARK 465 THR C 201
REMARK 465 LYS C 202
REMARK 465 GLY C 203
REMARK 465 LEU C 204
REMARK 465 ILE C 205
REMARK 465 PHE C 206
REMARK 465 GLY C 207
REMARK 465 MET D 1
REMARK 465 GLN D 200
REMARK 465 THR D 201
REMARK 465 LYS D 202
REMARK 465 GLY D 203
REMARK 465 LEU D 204
REMARK 465 ILE D 205
REMARK 465 PHE D 206
REMARK 465 GLY D 207
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 NZ LYS C 38 - O HOH C 2020 1.96
REMARK 500 O HOH A 2063 - O HOH B 2065 0.49
REMARK 500 O HOH A 2068 - O HOH C 2070 1.54
REMARK 500 O HOH B 2070 - O HOH D 2073 1.54
REMARK 500 O HOH C 2066 - O HOH D 2068 0.42
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
REMARK 500 OE1 GLU B 3 O GLY C 104 1556 1.65
REMARK 500 CG ASP B 12 OE2 GLU C 54 1557 1.99
REMARK 500 OD1 ASP B 12 CD GLU C 54 1557 2.00
REMARK 500 OD1 ASP B 12 OE2 GLU C 54 1557 1.08
REMARK 500 CD GLU C 54 OD1 ASP B 12 1547 2.00
REMARK 500 OE2 GLU C 54 CG ASP B 12 1547 1.99
REMARK 500 OE2 GLU C 54 OD1 ASP B 12 1547 1.08
REMARK 500 CA ASN C 86 CD GLU D 3 1646 2.18
REMARK 500 CA ASN C 86 OE1 GLU D 3 1646 1.76
REMARK 500 CA ASN C 86 OE2 GLU D 3 1646 2.13
REMARK 500 CB ASN C 86 OE1 GLU D 3 1646 1.99
REMARK 500 CB ASN C 86 OE2 GLU D 3 1646 2.15
REMARK 500 CG ASN C 86 OE2 GLU D 3 1646 1.94
REMARK 500 OD1 ASN C 86 OE2 GLU D 3 1646 1.37
REMARK 500 O GLY C 104 OE1 GLU B 3 1554 1.65
REMARK 500 CD GLU D 3 CA ASN C 86 1656 2.18
REMARK 500 OE1 GLU D 3 CA ASN C 86 1656 1.76
REMARK 500 OE1 GLU D 3 CB ASN C 86 1656 1.99
REMARK 500 OE2 GLU D 3 CA ASN C 86 1656 2.13
REMARK 500 OE2 GLU D 3 CB ASN C 86 1656 2.15
REMARK 500 OE2 GLU D 3 CG ASN C 86 1656 1.94
REMARK 500 OE2 GLU D 3 OD1 ASN C 86 1656 1.37
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 GLU A 94 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 ALA A 126 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 ALA A 152 N - CA - CB ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 GLU B 94 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 ALA B 126 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 ALA B 152 N - CA - CB ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG B 193 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 GLU C 94 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 ALA C 126 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 ALA C 152 N - CA - CB ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG C 193 NE - CZ - NH1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 GLU D 94 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 ALA D 126 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 ALA D 152 N - CA - CB ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG D 193 NE - CZ - NH1 ANGL. DEV. = -5.0 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 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 89 -150.99 73.15
REMARK 500 ASP A 144 -113.87 56.42
REMARK 500 ASN A 148 46.55 79.02
REMARK 500 PHE A 166 -14.53 -141.03
REMARK 500 LYS A 171 -133.07 54.86
REMARK 500 ASP B 89 -150.98 73.17
REMARK 500 ASP B 144 -113.83 56.39
REMARK 500 ASN B 148 46.61 78.95
REMARK 500 PHE B 166 -14.50 -141.03
REMARK 500 LYS B 171 -133.02 54.83
REMARK 500 ASP C 89 -150.97 73.10
REMARK 500 ASP C 144 -113.89 56.44
REMARK 500 ASN C 148 46.62 78.95
REMARK 500 PHE C 166 -14.54 -141.03
REMARK 500 LYS C 171 -133.06 54.84
REMARK 500 ASP D 89 -150.98 73.10
REMARK 500 ASP D 144 -113.84 56.44
REMARK 500 ASN D 148 46.54 79.01
REMARK 500 PHE D 166 -14.50 -141.04
REMARK 500 LYS D 171 -133.09 54.87
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 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 TYR A 167 21.6 L L OUTSIDE RANGE
REMARK 500 TYR B 167 21.7 L L OUTSIDE RANGE
REMARK 500 TYR C 167 21.7 L L OUTSIDE RANGE
REMARK 500 TYR D 167 21.6 L L OUTSIDE RANGE
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 FE A 999 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 76 NE2
REMARK 620 2 HIS A 28 NE2 87.2
REMARK 620 3 ASP A 160 OD2 102.3 82.1
REMARK 620 4 HIS A 164 NE2 137.9 94.1 119.5
REMARK 620 5 HOH A2037 O 84.0 168.4 92.4 97.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 999 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 28 NE2
REMARK 620 2 HIS B 76 NE2 87.2
REMARK 620 3 ASP B 160 OD2 82.1 102.3
REMARK 620 4 HIS B 164 NE2 94.1 137.9 119.5
REMARK 620 5 HOH B2038 O 168.4 84.0 92.4 97.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 999 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 76 NE2
REMARK 620 2 HOH C2038 O 84.0
REMARK 620 3 HIS C 28 NE2 87.2 168.4
REMARK 620 4 ASP C 160 OD2 102.3 92.3 82.1
REMARK 620 5 HIS C 164 NE2 137.9 97.5 94.1 119.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D 999 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 160 OD2
REMARK 620 2 HIS D 164 NE2 119.5
REMARK 620 3 HOH D2039 O 92.3 97.5
REMARK 620 4 HIS D 76 NE2 102.3 137.9 84.0
REMARK 620 5 HIS D 28 NE2 82.0 94.1 168.4 87.2
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 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GN2 RELATED DB: PDB
REMARK 900 S123C MUTANT OF THE IRON-SUPEROXIDE
REMARK 900 DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.
REMARK 900 RELATED ID: 1GN3 RELATED DB: PDB
REMARK 900 H145Q MUTANT OF MYCOBACTERIUM TUBERCULOSIS
REMARK 900 IRON-SUPEROXIDE DISMUTASE.
REMARK 900 RELATED ID: 1GN4 RELATED DB: PDB
REMARK 900 H145E MUTANT OF MYCOBACTERIUM TUBERCULOSIS
REMARK 900 IRON-SUPEROXIDE DISMUTASE.
REMARK 900 RELATED ID: 1IDS RELATED DB: PDB
REMARK 900 IRON-DEPENDENT SUPEROXIDE DISMUTASE (FE-SUPEROXIDE
REMARK 900 DISMUTASE, FE-SOD)
DBREF 1GN6 A 1 207 UNP P17670 SODF_MYCTU 1 207
DBREF 1GN6 B 1 207 UNP P17670 SODF_MYCTU 1 207
DBREF 1GN6 C 1 207 UNP P17670 SODF_MYCTU 1 207
DBREF 1GN6 D 1 207 UNP P17670 SODF_MYCTU 1 207
SEQADV 1GN6 ALA A 152 UNP P17670 GLY 152 ENGINEERED MUTATION
SEQADV 1GN6 ALA B 152 UNP P17670 GLY 152 ENGINEERED MUTATION
SEQADV 1GN6 ALA C 152 UNP P17670 GLY 152 ENGINEERED MUTATION
SEQADV 1GN6 ALA D 152 UNP P17670 GLY 152 ENGINEERED MUTATION
SEQRES 1 A 207 MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR
SEQRES 2 A 207 GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU
SEQRES 3 A 207 LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY
SEQRES 4 A 207 ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA
SEQRES 5 A 207 LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN
SEQRES 6 A 207 LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE
SEQRES 7 A 207 TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO
SEQRES 8 A 207 THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY
SEQRES 9 A 207 SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA
SEQRES 10 A 207 THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP
SEQRES 11 A 207 ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR
SEQRES 12 A 207 ASP HIS GLN THR ASN PHE PRO LEU ALA ILE VAL PRO LEU
SEQRES 13 A 207 LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN
SEQRES 14 A 207 TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP
SEQRES 15 A 207 ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA
SEQRES 16 A 207 ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY
SEQRES 1 B 207 MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR
SEQRES 2 B 207 GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU
SEQRES 3 B 207 LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY
SEQRES 4 B 207 ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA
SEQRES 5 B 207 LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN
SEQRES 6 B 207 LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE
SEQRES 7 B 207 TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO
SEQRES 8 B 207 THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY
SEQRES 9 B 207 SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA
SEQRES 10 B 207 THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP
SEQRES 11 B 207 ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR
SEQRES 12 B 207 ASP HIS GLN THR ASN PHE PRO LEU ALA ILE VAL PRO LEU
SEQRES 13 B 207 LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN
SEQRES 14 B 207 TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP
SEQRES 15 B 207 ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA
SEQRES 16 B 207 ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY
SEQRES 1 C 207 MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR
SEQRES 2 C 207 GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU
SEQRES 3 C 207 LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY
SEQRES 4 C 207 ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA
SEQRES 5 C 207 LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN
SEQRES 6 C 207 LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE
SEQRES 7 C 207 TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO
SEQRES 8 C 207 THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY
SEQRES 9 C 207 SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA
SEQRES 10 C 207 THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP
SEQRES 11 C 207 ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR
SEQRES 12 C 207 ASP HIS GLN THR ASN PHE PRO LEU ALA ILE VAL PRO LEU
SEQRES 13 C 207 LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN
SEQRES 14 C 207 TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP
SEQRES 15 C 207 ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA
SEQRES 16 C 207 ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY
SEQRES 1 D 207 MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR
SEQRES 2 D 207 GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU
SEQRES 3 D 207 LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY
SEQRES 4 D 207 ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA
SEQRES 5 D 207 LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN
SEQRES 6 D 207 LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE
SEQRES 7 D 207 TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO
SEQRES 8 D 207 THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY
SEQRES 9 D 207 SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA
SEQRES 10 D 207 THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP
SEQRES 11 D 207 ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR
SEQRES 12 D 207 ASP HIS GLN THR ASN PHE PRO LEU ALA ILE VAL PRO LEU
SEQRES 13 D 207 LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN
SEQRES 14 D 207 TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP
SEQRES 15 D 207 ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA
SEQRES 16 D 207 ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY
HET FE A 999 1
HET FE B 999 1
HET FE C 999 1
HET FE D 999 1
HETNAM FE FE (III) ION
FORMUL 5 FE 4(FE 3+)
FORMUL 9 HOH *360(H2 O1)
HELIX 1 1 ASP A 12 GLU A 17 5 6
HELIX 2 2 SER A 21 LYS A 31 1 11
HELIX 3 3 LYS A 31 LYS A 53 1 23
HELIX 4 4 ALA A 58 LEU A 83 1 26
HELIX 5 5 THR A 92 GLY A 104 1 13
HELIX 6 6 SER A 105 THR A 119 1 15
HELIX 7 7 TRP A 162 ALA A 165 5 4
HELIX 8 8 PHE A 166 LYS A 171 1 6
HELIX 9 9 VAL A 173 PHE A 181 1 9
HELIX 10 10 TRP A 182 VAL A 184 5 3
HELIX 11 11 ASN A 186 THR A 198 1 13
HELIX 12 12 ASP B 12 GLU B 17 5 6
HELIX 13 13 SER B 21 LYS B 31 1 11
HELIX 14 14 LYS B 31 LYS B 53 1 23
HELIX 15 15 ALA B 58 LEU B 83 1 26
HELIX 16 16 THR B 92 GLY B 104 1 13
HELIX 17 17 SER B 105 THR B 119 1 15
HELIX 18 18 TRP B 162 ALA B 165 5 4
HELIX 19 19 PHE B 166 LYS B 171 1 6
HELIX 20 20 VAL B 173 PHE B 181 1 9
HELIX 21 21 TRP B 182 VAL B 184 5 3
HELIX 22 22 ASN B 186 THR B 198 1 13
HELIX 23 23 ASP C 12 GLU C 17 5 6
HELIX 24 24 SER C 21 LYS C 31 1 11
HELIX 25 25 LYS C 31 LYS C 53 1 23
HELIX 26 26 ALA C 58 LEU C 83 1 26
HELIX 27 27 THR C 92 GLY C 104 1 13
HELIX 28 28 SER C 105 THR C 119 1 15
HELIX 29 29 TRP C 162 ALA C 165 5 4
HELIX 30 30 PHE C 166 LYS C 171 1 6
HELIX 31 31 VAL C 173 PHE C 181 1 9
HELIX 32 32 TRP C 182 VAL C 184 5 3
HELIX 33 33 ASN C 186 THR C 198 1 13
HELIX 34 34 ASP D 12 GLU D 17 5 6
HELIX 35 35 SER D 21 LYS D 31 1 11
HELIX 36 36 LYS D 31 LYS D 53 1 23
HELIX 37 37 ALA D 58 LEU D 83 1 26
HELIX 38 38 THR D 92 GLY D 104 1 13
HELIX 39 39 SER D 105 THR D 119 1 15
HELIX 40 40 TRP D 162 ALA D 165 5 4
HELIX 41 41 PHE D 166 LYS D 171 1 6
HELIX 42 42 VAL D 173 PHE D 181 1 9
HELIX 43 43 TRP D 182 VAL D 184 5 3
HELIX 44 44 ASN D 186 THR D 198 1 13
SHEET 1 AA 3 LYS A 136 TYR A 143 0
SHEET 2 AA 3 GLY A 124 ASP A 131 -1 O TRP A 125 N VAL A 142
SHEET 3 AA 3 VAL A 154 ASP A 160 -1 O VAL A 154 N TRP A 130
SHEET 1 BA 3 LYS B 136 TYR B 143 0
SHEET 2 BA 3 GLY B 124 ASP B 131 -1 O TRP B 125 N VAL B 142
SHEET 3 BA 3 VAL B 154 ASP B 160 -1 O VAL B 154 N TRP B 130
SHEET 1 CA 3 LYS C 136 TYR C 143 0
SHEET 2 CA 3 GLY C 124 ASP C 131 -1 O TRP C 125 N VAL C 142
SHEET 3 CA 3 VAL C 154 ASP C 160 -1 O VAL C 154 N TRP C 130
SHEET 1 DA 3 LYS D 136 TYR D 143 0
SHEET 2 DA 3 GLY D 124 ASP D 131 -1 O TRP D 125 N VAL D 142
SHEET 3 DA 3 VAL D 154 ASP D 160 -1 O VAL D 154 N TRP D 130
LINK FE FE A 999 NE2 HIS A 76 1555 1555 2.19
LINK FE FE A 999 NE2 HIS A 28 1555 1555 2.22
LINK FE FE A 999 OD2 ASP A 160 1555 1555 2.00
LINK FE FE A 999 NE2 HIS A 164 1555 1555 2.10
LINK FE FE A 999 O HOH A2037 1555 1555 1.88
LINK FE FE B 999 NE2 HIS B 28 1555 1555 2.22
LINK FE FE B 999 NE2 HIS B 76 1555 1555 2.19
LINK FE FE B 999 OD2 ASP B 160 1555 1555 2.00
LINK FE FE B 999 NE2 HIS B 164 1555 1555 2.10
LINK FE FE B 999 O HOH B2038 1555 1555 1.88
LINK FE FE C 999 O HOH C2038 1555 1555 1.88
LINK FE FE C 999 NE2 HIS C 28 1555 1555 2.22
LINK FE FE C 999 OD2 ASP C 160 1555 1555 2.00
LINK FE FE C 999 NE2 HIS C 164 1555 1555 2.10
LINK FE FE C 999 NE2 HIS C 76 1555 1555 2.19
LINK FE FE D 999 NE2 HIS D 164 1555 1555 2.10
LINK FE FE D 999 O HOH D2039 1555 1555 1.88
LINK FE FE D 999 NE2 HIS D 76 1555 1555 2.19
LINK FE FE D 999 NE2 HIS D 28 1555 1555 2.22
LINK FE FE D 999 OD2 ASP D 160 1555 1555 2.00
CISPEP 1 GLU A 17 PRO A 18 0 0.23
CISPEP 2 GLU B 17 PRO B 18 0 0.21
CISPEP 3 GLU C 17 PRO C 18 0 0.29
CISPEP 4 GLU D 17 PRO D 18 0 0.21
SITE 1 AC1 5 HIS A 28 HIS A 76 ASP A 160 HIS A 164
SITE 2 AC1 5 HOH A2037
SITE 1 AC2 5 HIS B 28 HIS B 76 ASP B 160 HIS B 164
SITE 2 AC2 5 HOH B2038
SITE 1 AC3 5 HIS C 28 HIS C 76 ASP C 160 HIS C 164
SITE 2 AC3 5 HOH C2038
SITE 1 AC4 5 HIS D 28 HIS D 76 ASP D 160 HIS D 164
SITE 2 AC4 5 HOH D2039
CRYST1 68.700 85.600 66.700 90.00 99.80 90.00 P 1 21 1 2
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 0.014556 0.000000 0.002514 0.00000
SCALE2 0.000000 0.011682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015215 0.00000
MTRIX1 1 0.903500 -0.298300 -0.307600 25.70900 1
MTRIX2 1 -0.298800 -0.953200 0.046900 63.88100 1
MTRIX3 1 -0.307200 0.049500 -0.950300 97.46200 1
MTRIX1 2 -0.903500 0.307700 0.298300 -5.68000 1
MTRIX2 2 0.311400 -0.007000 0.950300 -17.20800 1
MTRIX3 2 0.294400 0.951500 -0.089500 19.80200 1
MTRIX1 3 -0.999900 -0.010100 0.010000 19.74200 1
MTRIX2 3 -0.009600 -0.039000 -0.999200 82.88700 1
MTRIX3 3 0.010400 -0.999200 0.038900 79.61000 1
(ATOM LINES ARE NOT SHOWN.)
END
