HEADER HYDROLASE 28-NOV-03 1RMQ
TITLE CRYSTAL STRUCTURE OF APHA CLASS B ACID PHOSPHATASE/PHOSPHOTRANSFERASE
TITLE 2 WITH OSMIATE MIMICKING THE CATALYTIC INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLASS B ACID PHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.3.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: APHA, NAPA, B4055, SF4149, S3580;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PATAC
KEYWDS CLASS B ACID PHOSPHATASE, DDDD ACID PHOSPHATASE, METALLO-ENZYME,
KEYWDS 2 OSMIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CALDERONE,C.FORLEO,M.BENVENUTI,G.M.ROSSOLINI,M.C.THALLER,S.MANGANI
REVDAT 4 23-AUG-23 1RMQ 1 REMARK LINK
REVDAT 3 13-JUL-11 1RMQ 1 VERSN
REVDAT 2 24-FEB-09 1RMQ 1 VERSN
REVDAT 1 14-DEC-04 1RMQ 0
JRNL AUTH V.CALDERONE,C.FORLEO,M.BENVENUTI,G.M.ROSSOLINI,M.C.THALLER,
JRNL AUTH 2 S.MANGANI
JRNL TITL INSIGHTS IN THE CATALYTIC MECHANISM OF APHA FROM ESCHERICHIA
JRNL TITL 2 COLI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.C.THALLER,S.SCHIPPA,A.BONCI,S.CRESTI,G.M.ROSSOLINI
REMARK 1 TITL IDENTIFICATION OF THE GENE (APHA) ENCODING THE CLASS B ACID
REMARK 1 TITL 2 PHOSPHATASE/PHOSPHOTRANSFERASE OF ESCHERICHIA COLI MG1655
REMARK 1 TITL 3 AND CHARACTERIZATION OF ITS PRODUCT
REMARK 1 REF FEMS MICROBIOL.LETT. V. 146 191 1997
REMARK 1 REFN ISSN 0378-1097
REMARK 1 DOI 10.1016/S0378-1097(96)00474-0
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.FORLEO,M.BENVENUTI,V.CALDERONE,S.SCHIPPA,J.D.DOCQUIER,
REMARK 1 AUTH 2 M.C.THALLER,G.M ROSSOLINI,S.MANGANI
REMARK 1 TITL EXPRESSION, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY
REMARK 1 TITL 2 X-RAY CHARACTERIZATION OF THE CLASS B ACID PHOSPHATASE
REMARK 1 TITL 3 (APHA) FROM ESCHERICHIA COLI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 59 1058 2003
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444903006826
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 29421
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 + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2265
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2101
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 163
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3282
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.58000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.183
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.040
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3353 ; 0.026 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4548 ; 1.943 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 415 ; 8.202 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 483 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2616 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1640 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 284 ; 0.213 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.324 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 116 ; 0.252 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.250 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2082 ; 1.135 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3365 ; 1.853 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1271 ; 3.316 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1183 ; 5.066 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020888.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.13980, 1.14057, 1.13800
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 31710
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40200
REMARK 200 R SYM FOR SHELL (I) : 0.40200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1N8N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: APHA 6MG/ML, 50MM NA ACETATE, 25% PEG
REMARK 280 6000, 10MM OSMIATE, PH 7.2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 45.86600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.22350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.86600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.22350
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER, BUT THERE IS A DIMER
REMARK 300 IN THE ASYMMETRIC UNIT.
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: 13870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 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 -47.54795
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 78.20264
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 513 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 540 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 SER A 2
REMARK 465 PRO A 3
REMARK 465 SER B 1
REMARK 465 SER B 2
REMARK 465 PRO B 3
REMARK 465 SER B 4
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 ASN A 170 OD1
REMARK 480 PRO B 5 CD
REMARK 480 LEU B 6 CD1
REMARK 480 PRO B 8 CB
REMARK 480 GLU B 17 OE2
REMARK 480 ASP B 69 CB CG OD2
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 THR A 151 C THR A 151 O -0.155
REMARK 500 PRO B 5 CD PRO B 5 N -0.095
REMARK 500 GLU B 17 CD GLU B 17 OE2 -0.152
REMARK 500 ALA B 27 CA ALA B 27 CB 0.129
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 ARG A 14 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 44 CB - CG - OD2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP A 106 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 145 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG A 181 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 181 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 GLU B 17 OE1 - CD - OE2 ANGL. DEV. = -16.2 DEGREES
REMARK 500 GLU B 17 CG - CD - OE2 ANGL. DEV. = 12.8 DEGREES
REMARK 500 ASP B 44 CB - CG - OD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP B 47 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 69 N - CA - CB ANGL. DEV. = 12.1 DEGREES
REMARK 500 ASP B 69 OD1 - CG - OD2 ANGL. DEV. = 15.6 DEGREES
REMARK 500 ASP B 69 CB - CG - OD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500 ASP B 69 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 GLU B 78 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 MET B 100 CG - SD - CE ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG B 103 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ASP B 158 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 171 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 181 NE - CZ - NH1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG B 181 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG B 184 NE - CZ - NH2 ANGL. DEV. = -3.2 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 PRO A 38 137.34 -39.37
REMARK 500 SER A 64 63.13 -160.64
REMARK 500 SER A 67 -173.07 -174.60
REMARK 500 LYS A 146 90.13 -167.42
REMARK 500 ALA B 34 120.93 -32.24
REMARK 500 ILE B 45 -61.24 -90.26
REMARK 500 SER B 64 66.26 -165.83
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 GLY A 144 ASP A 145 103.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH A 546
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 CO A 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 44 OD2
REMARK 620 2 ASP A 46 O 90.7
REMARK 620 3 ASP A 167 OD1 85.9 88.2
REMARK 620 4 HOH A 408 O 84.8 172.2 85.2
REMARK 620 5 HOH A 428 O 179.6 89.6 94.2 94.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO B 403 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 44 OD2
REMARK 620 2 ASP B 46 O 87.6
REMARK 620 3 ASP B 167 OD1 85.8 88.5
REMARK 620 4 HOH B 495 O 88.8 168.5 80.3
REMARK 620 5 HOH B 551 O 174.4 87.5 91.4 95.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OS B 404 OS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 44 OD1
REMARK 620 2 HOH B 549 O 76.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OS B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OS A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OS B 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1N8N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE AU3+ COMPLEX OF APHA CLASS B ACID
REMARK 900 PHOSPHATASE/PHOSPHOTRANSFERASE FROM E. COLI AT 1.7 A RESOLUTION
REMARK 900 RELATED ID: 1N9K RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BROMIDE ADDUCT OF APHA CLASS B ACID
REMARK 900 PHOSPHATASE/PHOSPHOTRANSFERASE FROM E. COLI AT 2.2 A RESOLUTION
REMARK 900 RELATED ID: 1RM7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APHA CLASS B ACID PHOSPHATASE/
REMARK 900 PHOSPHOTRANSFERASE TERNARY COMPLEX WITH ADENOSINE AND PHOSPHATE AT
REMARK 900 2 A RESOLUTION
REMARK 900 RELATED ID: 1RMT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APHA CLASS B ACID PHOSPHATASE/
REMARK 900 PHOSPHOTRANSFERASE COMPLEXED WITH ADENOSINE
REMARK 900 RELATED ID: 1RMW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APHA CLASS B ACID PHOSPHATASE/
REMARK 900 PHOSPHOTRANSFERASE TERNARY COMPLEX WITH ADENOSINE AND PHOSPHATE
REMARK 900 BOUND TO THE CATALYTIC METAL AT 1.2 A RESOLUTION
REMARK 900 RELATED ID: 1RMY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APHA CLASS B ACID PHOSPHATASE/
REMARK 900 PHOSPHOTRANSFERASE TERNARY COMPLEX WITH DEOXYCYTOSINE AND PHOSPHATE
REMARK 900 BOUND TO THE CATALYTIC METAL
DBREF 1RMQ A 1 212 UNP P32697 APHA_ECOLI 26 237
DBREF 1RMQ B 1 212 UNP P32697 APHA_ECOLI 26 237
SEQRES 1 A 212 SER SER PRO SER PRO LEU ASN PRO GLY THR ASN VAL ALA
SEQRES 2 A 212 ARG LEU ALA GLU GLN ALA PRO ILE HIS TRP VAL SER VAL
SEQRES 3 A 212 ALA GLN ILE GLU ASN SER LEU ALA GLY ARG PRO PRO MET
SEQRES 4 A 212 ALA VAL GLY PHE ASP ILE ASP ASP THR VAL LEU PHE SER
SEQRES 5 A 212 SER PRO GLY PHE TRP ARG GLY LYS LYS THR PHE SER PRO
SEQRES 6 A 212 GLU SER GLU ASP TYR LEU LYS ASN PRO VAL PHE TRP GLU
SEQRES 7 A 212 LYS MET ASN ASN GLY TRP ASP GLU PHE SER ILE PRO LYS
SEQRES 8 A 212 GLU VAL ALA ARG GLN LEU ILE ASP MET HIS VAL ARG ARG
SEQRES 9 A 212 GLY ASP ALA ILE PHE PHE VAL THR GLY ARG SER PRO THR
SEQRES 10 A 212 LYS THR GLU THR VAL SER LYS THR LEU ALA ASP ASN PHE
SEQRES 11 A 212 HIS ILE PRO ALA THR ASN MET ASN PRO VAL ILE PHE ALA
SEQRES 12 A 212 GLY ASP LYS PRO GLY GLN ASN THR LYS SER GLN TRP LEU
SEQRES 13 A 212 GLN ASP LYS ASN ILE ARG ILE PHE TYR GLY ASP SER ASP
SEQRES 14 A 212 ASN ASP ILE THR ALA ALA ARG ASP VAL GLY ALA ARG GLY
SEQRES 15 A 212 ILE ARG ILE LEU ARG ALA SER ASN SER THR TYR LYS PRO
SEQRES 16 A 212 LEU PRO GLN ALA GLY ALA PHE GLY GLU GLU VAL ILE VAL
SEQRES 17 A 212 ASN SER GLU TYR
SEQRES 1 B 212 SER SER PRO SER PRO LEU ASN PRO GLY THR ASN VAL ALA
SEQRES 2 B 212 ARG LEU ALA GLU GLN ALA PRO ILE HIS TRP VAL SER VAL
SEQRES 3 B 212 ALA GLN ILE GLU ASN SER LEU ALA GLY ARG PRO PRO MET
SEQRES 4 B 212 ALA VAL GLY PHE ASP ILE ASP ASP THR VAL LEU PHE SER
SEQRES 5 B 212 SER PRO GLY PHE TRP ARG GLY LYS LYS THR PHE SER PRO
SEQRES 6 B 212 GLU SER GLU ASP TYR LEU LYS ASN PRO VAL PHE TRP GLU
SEQRES 7 B 212 LYS MET ASN ASN GLY TRP ASP GLU PHE SER ILE PRO LYS
SEQRES 8 B 212 GLU VAL ALA ARG GLN LEU ILE ASP MET HIS VAL ARG ARG
SEQRES 9 B 212 GLY ASP ALA ILE PHE PHE VAL THR GLY ARG SER PRO THR
SEQRES 10 B 212 LYS THR GLU THR VAL SER LYS THR LEU ALA ASP ASN PHE
SEQRES 11 B 212 HIS ILE PRO ALA THR ASN MET ASN PRO VAL ILE PHE ALA
SEQRES 12 B 212 GLY ASP LYS PRO GLY GLN ASN THR LYS SER GLN TRP LEU
SEQRES 13 B 212 GLN ASP LYS ASN ILE ARG ILE PHE TYR GLY ASP SER ASP
SEQRES 14 B 212 ASN ASP ILE THR ALA ALA ARG ASP VAL GLY ALA ARG GLY
SEQRES 15 B 212 ILE ARG ILE LEU ARG ALA SER ASN SER THR TYR LYS PRO
SEQRES 16 B 212 LEU PRO GLN ALA GLY ALA PHE GLY GLU GLU VAL ILE VAL
SEQRES 17 B 212 ASN SER GLU TYR
HET CO A 401 1
HET OS A 402 1
HET OS A 405 1
HET CO B 403 1
HET OS B 404 1
HET OS B 406 1
HETNAM CO COBALT (II) ION
HETNAM OS OSMIUM ION
FORMUL 3 CO 2(CO 2+)
FORMUL 4 OS 4(OS 3+)
FORMUL 9 HOH *296(H2 O)
HELIX 1 1 ASN A 11 GLU A 17 1 7
HELIX 2 2 SER A 25 LEU A 33 1 9
HELIX 3 3 SER A 52 SER A 64 1 13
HELIX 4 4 GLU A 68 LYS A 72 5 5
HELIX 5 5 ASN A 73 ASN A 81 1 9
HELIX 6 6 GLY A 83 SER A 88 5 6
HELIX 7 7 LYS A 91 GLY A 105 1 15
HELIX 8 8 THR A 121 HIS A 131 1 11
HELIX 9 9 LYS A 152 ASN A 160 1 9
HELIX 10 10 SER A 168 VAL A 178 1 11
HELIX 11 11 ASN B 11 GLU B 17 1 7
HELIX 12 12 SER B 25 ALA B 34 1 10
HELIX 13 13 SER B 52 SER B 64 1 13
HELIX 14 14 GLU B 68 LYS B 72 5 5
HELIX 15 15 ASN B 73 ASN B 81 1 9
HELIX 16 16 GLY B 83 SER B 88 5 6
HELIX 17 17 LYS B 91 ARG B 104 1 14
HELIX 18 18 THR B 121 HIS B 131 1 11
HELIX 19 19 THR B 151 ASN B 160 1 10
HELIX 20 20 SER B 168 VAL B 178 1 11
SHEET 1 A 7 HIS A 22 VAL A 24 0
SHEET 2 A 7 GLU A 205 ILE A 207 1 O VAL A 206 N HIS A 22
SHEET 3 A 7 ARG A 181 ARG A 184 1 N ARG A 184 O ILE A 207
SHEET 4 A 7 ILE A 161 GLY A 166 1 N PHE A 164 O ILE A 183
SHEET 5 A 7 ALA A 40 PHE A 43 1 N GLY A 42 O ILE A 163
SHEET 6 A 7 ALA A 107 THR A 112 1 O ALA A 107 N VAL A 41
SHEET 7 A 7 ILE A 141 PHE A 142 1 O ILE A 141 N THR A 112
SHEET 1 B 2 LEU A 50 PHE A 51 0
SHEET 2 B 2 ILE A 89 PRO A 90 -1 O ILE A 89 N PHE A 51
SHEET 1 C 2 HIS B 22 VAL B 24 0
SHEET 2 C 2 GLU B 205 ILE B 207 1 O VAL B 206 N HIS B 22
SHEET 1 D 5 ILE B 141 PHE B 142 0
SHEET 2 D 5 ALA B 107 THR B 112 1 N THR B 112 O ILE B 141
SHEET 3 D 5 ALA B 40 PHE B 43 1 N VAL B 41 O ALA B 107
SHEET 4 D 5 ILE B 161 GLY B 166 1 O ILE B 163 N GLY B 42
SHEET 5 D 5 ARG B 181 ARG B 184 1 O ILE B 183 N PHE B 164
SHEET 1 E 2 LEU B 50 PHE B 51 0
SHEET 2 E 2 ILE B 89 PRO B 90 -1 O ILE B 89 N PHE B 51
LINK NE2 HIS A 22 OS OS A 405 1555 1555 2.24
LINK OD2 ASP A 44 CO CO A 401 1555 1555 2.07
LINK O ASP A 46 CO CO A 401 1555 1555 2.19
LINK OD1 ASP A 167 CO CO A 401 1555 1555 2.13
LINK CO CO A 401 O HOH A 408 1555 1555 2.11
LINK CO CO A 401 O HOH A 428 1555 1555 2.20
LINK OD2 ASP B 44 CO CO B 403 1555 1555 1.96
LINK OD1 ASP B 44 OS OS B 404 1555 1555 2.32
LINK O ASP B 46 CO CO B 403 1555 1555 2.17
LINK OD1 ASP B 167 CO CO B 403 1555 1555 2.11
LINK CO CO B 403 O HOH B 495 1555 1555 2.04
LINK CO CO B 403 O HOH B 551 1555 1555 2.12
LINK OS OS B 404 O HOH B 549 1555 1555 2.35
CISPEP 1 PRO A 147 GLY A 148 0 -15.02
CISPEP 2 LYS A 194 PRO A 195 0 3.75
CISPEP 3 LYS B 194 PRO B 195 0 -1.26
SITE 1 AC1 6 ASP A 44 ASP A 46 ASP A 167 OS A 402
SITE 2 AC1 6 HOH A 408 HOH A 428
SITE 1 AC2 3 ASP A 44 CO A 401 HOH A 442
SITE 1 AC3 6 ASP B 44 ASP B 46 ASP B 167 OS B 404
SITE 2 AC3 6 HOH B 495 HOH B 551
SITE 1 AC4 5 ASP B 44 CO B 403 HOH B 442 HOH B 548
SITE 2 AC4 5 HOH B 549
SITE 1 AC5 1 HIS A 22
SITE 1 AC6 1 HIS B 22
CRYST1 91.732 66.447 91.523 90.00 121.30 90.00 C 1 2 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 0.010901 0.000000 0.006628 0.00000
SCALE2 0.000000 0.015050 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012787 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
