HEADER METAL BINDING PROTEIN, HYDROLASE 20-MAR-07 2P7O
TITLE CRYSTAL STRUCTURE OF GENOMICALLY ENCODED FOSFOMYCIN RESISTANCE
TITLE 2 PROTEIN, FOSX, FROM LISTERIA MONOCYTOGENES (TETRAGONAL FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYOXALASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 3 ORGANISM_TAXID: 169963;
SOURCE 4 STRAIN: EGD-E;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET20B(+)
KEYWDS FOSFOMYCIN RESISTANCE PROTEIN, MN BINDING, ANTIBIOTIC RESISTANCE,
KEYWDS 2 METAL BINDING PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.FILLGROVE,S.PAKHOMOVA,M.SCHAAB,M.E.NEWCOMER,R.N.ARMSTRONG
REVDAT 4 30-AUG-23 2P7O 1 REMARK LINK
REVDAT 3 13-JUL-11 2P7O 1 VERSN
REVDAT 2 24-FEB-09 2P7O 1 VERSN
REVDAT 1 17-JUL-07 2P7O 0
JRNL AUTH K.L.FILLGROVE,S.PAKHOMOVA,M.R.SCHAAB,M.E.NEWCOMER,
JRNL AUTH 2 R.N.ARMSTRONG
JRNL TITL STRUCTURE AND MECHANISM OF THE GENOMICALLY ENCODED
JRNL TITL 2 FOSFOMYCIN RESISTANCE PROTEIN, FOSX, FROM LISTERIA
JRNL TITL 3 MONOCYTOGENES.
JRNL REF BIOCHEMISTRY V. 46 8110 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17567049
JRNL DOI 10.1021/BI700625P
REMARK 2
REMARK 2 RESOLUTION. 1.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.5
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.126
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.124
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.800
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1453
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 38298
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.117
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.116
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.157
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 3.700
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1192
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 31792
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2050
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 168
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2223.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 7
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 20274
REMARK 3 NUMBER OF RESTRAINTS : 25273
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.034
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.034
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.133
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.156
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.011
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.072
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.075
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT
REMARK 4
REMARK 4 2P7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042069.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41281
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.440
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 2P7K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 3350, 0.1 M TRIS-HCL, 0.2 M
REMARK 280 MGCL2, 5% ISOPROPANOL, PH 8.1, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 28.41750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.62625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.20875
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 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 SER A 33
REMARK 465 SER A 34
REMARK 465 GLY A 35
REMARK 465 ASP A 36
REMARK 465 LYS A 37
REMARK 465 GLU A 133
REMARK 465 SER B 33
REMARK 465 SER B 34
REMARK 465 GLY B 35
REMARK 465 ASP B 36
REMARK 465 LYS B 37
REMARK 465 HIS B 132
REMARK 465 GLU B 133
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 SER A 3 OG
REMARK 470 TYR A 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 38 OG1 CG2
REMARK 470 SER A 40 OG
REMARK 470 SER A 61 OG
REMARK 470 LEU A 62 CG CD1 CD2
REMARK 470 HIS A 132 CG ND1 CD2 CE1 NE2
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 TYR B 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 40 OG
REMARK 470 LEU B 62 CG CD1 CD2
REMARK 470 GLN B 63 CG CD OE1 NE2
REMARK 470 GLU B 64 CG CD OE1 OE2
REMARK 470 ARG B 85 CG CD NE CZ NH1 NH2
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 MET A 1 CB - CA - C ANGL. DEV. = 21.3 DEGREES
REMARK 500 MET A 1 CA - CB - CG ANGL. DEV. = 19.4 DEGREES
REMARK 500 MET A 1 CA - C - N ANGL. DEV. = 15.1 DEGREES
REMARK 500 MET A 57 CA - CB - CG ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASP A 60 C - N - CA ANGL. DEV. = 19.6 DEGREES
REMARK 500 ASP A 80 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 PHE B 39 C - N - CA ANGL. DEV. = 19.1 DEGREES
REMARK 500 LEU B 62 C - N - CA ANGL. DEV. = 18.9 DEGREES
REMARK 500 ARG B 65 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 105 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 TYR B 110 CB - CG - CD1 ANGL. DEV. = -3.6 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 ASP A 60 -97.27 24.81
REMARK 500 SER A 61 -36.94 -165.81
REMARK 500 LEU A 62 -156.89 -174.38
REMARK 500 GLN A 63 137.29 -177.13
REMARK 500 ASP A 111 -145.85 -91.37
REMARK 500 PHE B 39 34.21 -65.77
REMARK 500 SER B 42 67.43 -110.14
REMARK 500 GLN B 63 -152.19 -86.20
REMARK 500 ASP B 111 -157.71 -84.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 61 LEU B 62 -40.83
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 MN B4000 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 7 NE2
REMARK 620 2 HIS B 69 NE2 114.2
REMARK 620 3 GLU B 118 OE1 96.6 86.9
REMARK 620 4 GLU B 126 OE1 96.9 90.9 166.0
REMARK 620 5 HOH B7001 O 87.2 156.7 81.2 95.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A6000 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 69 NE2
REMARK 620 2 GLU A 118 OE1 84.0
REMARK 620 3 GLU A 126 OE1 90.7 166.6
REMARK 620 4 HOH A7005 O 149.9 83.3 95.4
REMARK 620 5 HIS B 7 NE2 113.2 95.5 97.9 95.2
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 MN B 4000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 6000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P7K RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GENOMICALLY ENCODED FOSFOMYCIN RESISTANCE
REMARK 900 PROTEIN, FOSX, FROM LISTERIA MONOCYTOGENES (HEXAGONAL FORM)
REMARK 900 RELATED ID: 2P7L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GENOMICALLY ENCODED FOSFOMYCIN RESISTANCE
REMARK 900 PROTEIN, FOSX, FROM LISTERIA MONOCYTOGENES (MONOCLINIC FORM GROWN
REMARK 900 AT PH 5.75)
REMARK 900 RELATED ID: 2P7M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GENOMICALLY ENCODED FOSFOMYCIN RESISTANCE
REMARK 900 PROTEIN, FOSX, FROM LISTERIA MONOCYTOGENES (MONOCLINIC FORM GROWN
REMARK 900 AT PH 6.5)
REMARK 900 RELATED ID: 2P7P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GENOMICALLY ENCODED FOSFOMYCIN RESISTANCE
REMARK 900 PROTEIN, FOSX, FROM LISTERIA MONOCYTOGENES COMPLEXED WITH MN(II)
REMARK 900 AND SULFATE ION
REMARK 900 RELATED ID: 2P7Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E126Q MUTANT OF GENOMICALLY ENCODED FOSFOMYCIN
REMARK 900 RESISTANCE PROTEIN, FOSX, FROM LISTERIA MONOCYTOGENES COMPLEXED
REMARK 900 WITH MN(II) AND 1S,2S-DIHYDROXYPROPYLPHOSPHONIC ACID
DBREF 2P7O A 1 133 UNP Q71YW5 Q71YW5_LISMF 1 133
DBREF 2P7O B 1 133 UNP Q71YW5 Q71YW5_LISMF 1 133
SEQRES 1 A 133 MET ILE SER GLY LEU SER HIS ILE THR LEU ILE VAL LYS
SEQRES 2 A 133 ASP LEU ASN LYS THR THR ALA PHE LEU GLN ASN ILE PHE
SEQRES 3 A 133 ASN ALA GLU GLU ILE TYR SER SER GLY ASP LYS THR PHE
SEQRES 4 A 133 SER LEU SER LYS GLU LYS PHE PHE LEU ILE ALA GLY LEU
SEQRES 5 A 133 TRP ILE CYS ILE MET GLU GLY ASP SER LEU GLN GLU ARG
SEQRES 6 A 133 THR TYR ASN HIS ILE ALA PHE GLN ILE GLN SER GLU GLU
SEQRES 7 A 133 VAL ASP GLU TYR THR GLU ARG ILE LYS ALA LEU GLY VAL
SEQRES 8 A 133 GLU MET LYS PRO GLU ARG PRO ARG VAL GLN GLY GLU GLY
SEQRES 9 A 133 ARG SER ILE TYR PHE TYR ASP PHE ASP ASN HIS LEU PHE
SEQRES 10 A 133 GLU LEU HIS ALA GLY THR LEU GLU GLU ARG LEU LYS ARG
SEQRES 11 A 133 TYR HIS GLU
SEQRES 1 B 133 MET ILE SER GLY LEU SER HIS ILE THR LEU ILE VAL LYS
SEQRES 2 B 133 ASP LEU ASN LYS THR THR ALA PHE LEU GLN ASN ILE PHE
SEQRES 3 B 133 ASN ALA GLU GLU ILE TYR SER SER GLY ASP LYS THR PHE
SEQRES 4 B 133 SER LEU SER LYS GLU LYS PHE PHE LEU ILE ALA GLY LEU
SEQRES 5 B 133 TRP ILE CYS ILE MET GLU GLY ASP SER LEU GLN GLU ARG
SEQRES 6 B 133 THR TYR ASN HIS ILE ALA PHE GLN ILE GLN SER GLU GLU
SEQRES 7 B 133 VAL ASP GLU TYR THR GLU ARG ILE LYS ALA LEU GLY VAL
SEQRES 8 B 133 GLU MET LYS PRO GLU ARG PRO ARG VAL GLN GLY GLU GLY
SEQRES 9 B 133 ARG SER ILE TYR PHE TYR ASP PHE ASP ASN HIS LEU PHE
SEQRES 10 B 133 GLU LEU HIS ALA GLY THR LEU GLU GLU ARG LEU LYS ARG
SEQRES 11 B 133 TYR HIS GLU
HET MN A6000 1
HET MN B4000 1
HETNAM MN MANGANESE (II) ION
FORMUL 3 MN 2(MN 2+)
FORMUL 5 HOH *168(H2 O)
HELIX 1 1 ASP A 14 ASN A 27 1 14
HELIX 2 2 GLN A 75 GLU A 77 5 3
HELIX 3 3 GLU A 78 GLY A 90 1 13
HELIX 4 4 ARG A 127 HIS A 132 5 6
HELIX 5 5 ASP B 14 ASN B 27 1 14
HELIX 6 6 GLN B 75 GLU B 77 5 3
HELIX 7 7 GLU B 78 LEU B 89 1 12
HELIX 8 8 ARG B 127 TYR B 131 5 5
SHEET 1 A 7 GLU A 29 GLU A 30 0
SHEET 2 A 7 GLU A 44 ILE A 49 -1 O LEU A 48 N GLU A 29
SHEET 3 A 7 LEU A 52 GLU A 58 -1 O ILE A 54 N PHE A 47
SHEET 4 A 7 GLY A 4 VAL A 12 1 N LEU A 10 O CYS A 55
SHEET 5 A 7 HIS B 69 GLN B 73 -1 O GLN B 73 N GLY A 4
SHEET 6 A 7 LEU B 116 HIS B 120 1 O HIS B 120 N PHE B 72
SHEET 7 A 7 SER B 106 TYR B 110 -1 N PHE B 109 O PHE B 117
SHEET 1 B 8 MET A 93 LYS A 94 0
SHEET 2 B 8 SER A 106 TYR A 110 -1 O TYR A 108 N LYS A 94
SHEET 3 B 8 LEU A 116 HIS A 120 -1 O PHE A 117 N PHE A 109
SHEET 4 B 8 HIS A 69 GLN A 73 1 N PHE A 72 O HIS A 120
SHEET 5 B 8 GLY B 4 VAL B 12 -1 O GLY B 4 N GLN A 73
SHEET 6 B 8 LEU B 52 GLU B 58 1 O CYS B 55 N ILE B 8
SHEET 7 B 8 GLU B 44 ILE B 49 -1 N LYS B 45 O ILE B 56
SHEET 8 B 8 GLU B 29 ILE B 31 -1 N ILE B 31 O PHE B 46
LINK NE2 HIS A 7 MN MN B4000 1555 1555 2.17
LINK NE2 HIS A 69 MN MN A6000 1555 1555 2.12
LINK OE1 GLU A 118 MN MN A6000 1555 1555 2.15
LINK OE1 GLU A 126 MN MN A6000 1555 1555 2.07
LINK MN MN A6000 O HOH A7005 1555 1555 2.19
LINK MN MN A6000 NE2 HIS B 7 1555 1555 2.22
LINK NE2 HIS B 69 MN MN B4000 1555 1555 2.31
LINK OE1 GLU B 118 MN MN B4000 1555 1555 2.04
LINK OE1 GLU B 126 MN MN B4000 1555 1555 2.23
LINK MN MN B4000 O HOH B7001 1555 1555 2.29
CISPEP 1 MET A 1 ILE A 2 0 -22.63
SITE 1 AC1 6 HIS A 7 HIS B 69 TYR B 108 GLU B 118
SITE 2 AC1 6 GLU B 126 HOH B7001
SITE 1 AC2 6 HIS A 69 TYR A 108 GLU A 118 GLU A 126
SITE 2 AC2 6 HOH A7005 HIS B 7
CRYST1 68.579 68.579 56.835 90.00 90.00 90.00 P 43 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 0.014582 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014582 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017595 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
