| content |
HEADER HYDROLASE 17-MAR-11 3R41
TITLE CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 -
TITLE 2 HIS280ASN/APO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 1076;
SOURCE 4 STRAIN: CGA009;
SOURCE 5 GENE: RPA1163;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P15TV-L
KEYWDS FACD, DEFLUORINASE, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.W.Y.CHAN,A.F.YAKUNIN,E.A.EDWARDS,E.F.PAI
REVDAT 1 04-MAY-11 3R41 0
JRNL AUTH P.W.CHAN,A.F.YAKUNIN,E.A.EDWARDS,E.F.PAI
JRNL TITL MAPPING THE REACTION COORDINATES OF ENZYMATIC
JRNL TITL 2 DEFLUORINATION.
JRNL REF J.AM.CHEM.SOC. 2011
JRNL REFN ESSN 1520-5126
JRNL PMID 21510690
JRNL DOI 10.1021/JA200277D
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 238331
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) : 0.143
REMARK 3 R VALUE (WORKING SET) : 0.142
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11952
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) : 1.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15308
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 847
REMARK 3 BIN FREE R VALUE : 0.2400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4729
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 455
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.65000
REMARK 3 B33 (A**2) : -0.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.028
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.018
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.782
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5202 ; 0.026 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3553 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7123 ; 2.189 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8588 ; 1.176 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 659 ; 6.621 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 251 ;36.658 ;22.869
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 792 ;13.972 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;19.585 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 714 ; 0.159 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6053 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1169 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 3183 ; 2.563 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1260 ; 0.923 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5124 ; 3.498 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2019 ; 4.844 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1999 ; 6.547 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 8755 ; 2.222 ; 3.000
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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3R41 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064461.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978700
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 238333
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050
REMARK 200 RESOLUTION RANGE LOW (A) : 82.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.420
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-24% PEG3350, 0.1-0.2M CACL2 AND
REMARK 280 0.1M TRIS-HCL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 39.05000
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 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: 2970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 ALA A 301
REMARK 465 PRO A 302
REMARK 465 GLY A 303
REMARK 465 SER A 304
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ASP B 3
REMARK 465 ALA B 301
REMARK 465 PRO B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
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 OH TYR B 141 O ILE B 253 1.85
REMARK 500 OH TYR B 149 O HOH B 452 1.87
REMARK 500 O HOH B 364 O HOH B 403 1.89
REMARK 500 CE2 TYR A 141 CE MET A 145 1.96
REMARK 500 CE2 PHE A 176 O HOH B 399 2.00
REMARK 500 O MET B 145 O HOH B 450 2.11
REMARK 500 O HOH A 513 O HOH A 551 2.12
REMARK 500 OD1 ASN A 280 O HOH A 551 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 145 N MET A 145 CA 0.124
REMARK 500 TYR A 149 CB TYR A 149 CG -0.101
REMARK 500 TRP B 15 CB TRP B 15 CG 0.220
REMARK 500 VAL B 45 CB VAL B 45 CG2 -0.159
REMARK 500 VAL B 50 CB VAL B 50 CG2 -0.181
REMARK 500 ARG B 144 CZ ARG B 144 NH1 -0.092
REMARK 500 VAL B 271 CB VAL B 271 CG1 -0.145
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 49 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 VAL A 50 CA - CB - CG1 ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG A 86 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 TYR A 149 CG - CD1 - CE1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TYR A 149 CD1 - CE1 - CZ ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 MET A 244 CG - SD - CE ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP A 288 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 VAL B 45 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG B 49 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR B 149 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 MET B 244 CG - SD - CE ANGL. DEV. = -17.1 DEGREES
REMARK 500 GLN B 272 CA - CB - CG ANGL. DEV. = 15.8 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 110 -127.27 58.14
REMARK 500 MET A 145 77.32 -47.05
REMARK 500 ASP A 173 67.21 -153.80
REMARK 500 TYR A 224 -100.35 -120.44
REMARK 500 ALA A 257 46.10 -146.09
REMARK 500 SER A 278 159.11 178.16
REMARK 500 ASP B 110 -130.81 55.90
REMARK 500 TYR B 224 -96.97 -122.02
REMARK 500 SER B 278 156.34 175.81
REMARK 500 PHE B 281 61.40 -101.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 114 0.10 SIDE CHAIN
REMARK 500 TYR A 154 0.08 SIDE CHAIN
REMARK 500 ARG B 114 0.10 SIDE CHAIN
REMARK 500 TYR B 154 0.07 SIDE CHAIN
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 349 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH A 461 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH A 487 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH B 423 DISTANCE = 5.04 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 CA A 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 494 O
REMARK 620 2 HOH A 408 O 78.9
REMARK 620 3 HOH A 417 O 76.4 137.3
REMARK 620 4 HOH A 510 O 90.2 73.5 72.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 255 OE1
REMARK 620 2 HOH B 322 O 78.0
REMARK 620 3 HOH B 394 O 107.9 142.0
REMARK 620 4 GLN B 255 O 75.1 142.3 72.6
REMARK 620 5 HOH B 340 O 86.7 73.5 142.8 79.0
REMARK 620 6 HOH B 449 O 75.8 77.0 68.7 120.3 148.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 307
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R3U RELATED DB: PDB
REMARK 900 THE WT/APO CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 3R3V RELATED DB: PDB
REMARK 900 THE ASP110ASN MUTANT IN COMPLEX WITH FLUOROACETATE
REMARK 900 RELATED ID: 3R3W RELATED DB: PDB
REMARK 900 THE ASP110ASN MUTANT IN COMPLEX WITH CHLOROACETATE
REMARK 900 RELATED ID: 3R3X RELATED DB: PDB
REMARK 900 THE ASP110ASN MUTANT IN COMPLEX WITH BROMOACETATE
REMARK 900 RELATED ID: 3R3Y RELATED DB: PDB
REMARK 900 THE HIS280ASN MUTANT IN COVALENT COMPLEX WITH FLUOROACETATE
REMARK 900 RELATED ID: 3R3Z RELATED DB: PDB
REMARK 900 THE WT IN COMPLEX WITH GLYCOLATE
REMARK 900 RELATED ID: 3R40 RELATED DB: PDB
REMARK 900 THE ASP110ASN MUTANT/APO CRYSTAL STRUCTURE
DBREF 3R41 A 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
DBREF 3R41 B 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
SEQADV 3R41 GLY A -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 3R41 HIS A 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 3R41 ASN A 280 UNP Q6NAM1 HIS 280 ENGINEERED MUTATION
SEQADV 3R41 GLY A 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 3R41 SER A 304 UNP Q6NAM1 EXPRESSION TAG
SEQADV 3R41 GLY B -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 3R41 HIS B 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 3R41 ASN B 280 UNP Q6NAM1 HIS 280 ENGINEERED MUTATION
SEQADV 3R41 GLY B 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 3R41 SER B 304 UNP Q6NAM1 EXPRESSION TAG
SEQRES 1 A 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 A 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 A 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 A 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 A 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 A 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 A 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 A 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 A 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 A 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 A 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 A 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 A 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 A 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 A 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 A 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 A 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 A 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 A 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 A 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 A 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 A 306 GLN GLY ALA PRO ILE GLU SER GLY ASN PHE LEU PRO GLU
SEQRES 23 A 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 A 306 PHE SER ALA ALA PRO GLY SER
SEQRES 1 B 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 B 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 B 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 B 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 B 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 B 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 B 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 B 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 B 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 B 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 B 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 B 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 B 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 B 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 B 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 B 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 B 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 B 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 B 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 B 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 B 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 B 306 GLN GLY ALA PRO ILE GLU SER GLY ASN PHE LEU PRO GLU
SEQRES 23 B 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 B 306 PHE SER ALA ALA PRO GLY SER
HET CA A 305 1
HET CL A 306 1
HET CL A 307 1
HET CL A 308 1
HET CA B 305 1
HET CL B 306 1
HET CL B 307 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 CL 5(CL 1-)
FORMUL 10 HOH *455(H2 O)
HELIX 1 1 THR A 43 HIS A 48 5 6
HELIX 2 2 VAL A 50 GLU A 56 1 7
HELIX 3 3 HIS A 80 TYR A 83 5 4
HELIX 4 4 THR A 84 LEU A 99 1 16
HELIX 5 5 ASP A 110 SER A 123 1 14
HELIX 6 6 PRO A 137 ARG A 144 1 8
HELIX 7 7 ASN A 146 ILE A 153 1 8
HELIX 8 8 TYR A 154 ALA A 160 1 7
HELIX 9 9 PRO A 164 GLY A 172 1 9
HELIX 10 10 ASP A 173 TRP A 185 1 13
HELIX 11 11 ASP A 195 ALA A 207 1 13
HELIX 12 12 ASP A 208 TYR A 224 1 17
HELIX 13 13 TYR A 224 GLY A 237 1 14
HELIX 14 14 THR A 259 ALA A 268 1 10
HELIX 15 15 PHE A 281 ALA A 286 1 6
HELIX 16 16 ALA A 286 ALA A 300 1 15
HELIX 17 17 THR B 43 ARG B 49 5 7
HELIX 18 18 VAL B 50 ALA B 55 1 6
HELIX 19 19 HIS B 80 TYR B 83 5 4
HELIX 20 20 THR B 84 LEU B 99 1 16
HELIX 21 21 ASP B 110 SER B 123 1 14
HELIX 22 22 PRO B 137 ARG B 144 1 8
HELIX 23 23 ASN B 146 ILE B 153 1 8
HELIX 24 24 TYR B 154 LEU B 159 1 6
HELIX 25 25 PRO B 164 GLY B 171 1 8
HELIX 26 26 ASP B 173 TRP B 185 1 13
HELIX 27 27 ASP B 195 ALA B 207 1 13
HELIX 28 28 ASP B 208 TYR B 224 1 17
HELIX 29 29 TYR B 224 GLY B 237 1 14
HELIX 30 30 THR B 259 LYS B 266 1 8
HELIX 31 31 PHE B 281 ALA B 286 1 6
HELIX 32 32 ALA B 286 ALA B 300 1 15
SHEET 1 A 8 GLY A 12 ILE A 16 0
SHEET 2 A 8 ILE A 23 GLY A 29 -1 O ILE A 23 N ILE A 16
SHEET 3 A 8 LYS A 59 ALA A 63 -1 O VAL A 62 N ARG A 26
SHEET 4 A 8 PRO A 33 LEU A 37 1 N LEU A 34 O ILE A 61
SHEET 5 A 8 PHE A 104 HIS A 109 1 O ALA A 105 N LEU A 35
SHEET 6 A 8 LEU A 127 LEU A 133 1 O ALA A 131 N LEU A 106
SHEET 7 A 8 MET A 244 GLY A 249 1 O LEU A 245 N VAL A 132
SHEET 8 A 8 VAL A 271 ILE A 276 1 O GLN A 272 N ALA A 246
SHEET 1 B 8 GLY B 12 ILE B 16 0
SHEET 2 B 8 ILE B 23 GLY B 28 -1 O ILE B 23 N ILE B 16
SHEET 3 B 8 LYS B 59 ALA B 63 -1 O VAL B 62 N ARG B 26
SHEET 4 B 8 PRO B 33 LEU B 37 1 N LEU B 34 O ILE B 61
SHEET 5 B 8 PHE B 104 HIS B 109 1 O ALA B 105 N LEU B 35
SHEET 6 B 8 LEU B 127 LEU B 133 1 O ALA B 131 N LEU B 106
SHEET 7 B 8 MET B 244 GLY B 249 1 O LEU B 245 N VAL B 132
SHEET 8 B 8 VAL B 271 ILE B 276 1 O ILE B 276 N TRP B 248
LINK CA CA A 305 O HOH A 494 1555 1555 2.35
LINK CA CA A 305 O HOH A 408 1555 1555 2.36
LINK OE1 GLN B 255 CA CA B 305 1555 1555 2.40
LINK CA CA B 305 O HOH B 322 1555 1555 2.41
LINK CA CA A 305 O HOH A 417 1555 1555 2.41
LINK CA CA A 305 O HOH A 510 1555 1555 2.41
LINK CA CA B 305 O HOH B 394 1555 1555 2.42
LINK O GLN B 255 CA CA B 305 1555 1555 2.47
LINK CA CA B 305 O HOH B 340 1555 1555 2.47
LINK CA CA B 305 O HOH B 449 1555 1555 2.51
CISPEP 1 PHE A 40 PRO A 41 0 -1.59
CISPEP 2 ALA A 163 PRO A 164 0 8.03
CISPEP 3 PHE B 40 PRO B 41 0 -3.58
CISPEP 4 ALA B 163 PRO B 164 0 7.95
SITE 1 AC1 4 HOH A 408 HOH A 417 HOH A 494 HOH A 510
SITE 1 AC2 3 ARG A 114 LEU A 136 HOH A 558
SITE 1 AC3 4 ALA A 286 PRO A 287 ASP A 288 GLN A 289
SITE 1 AC4 2 LYS A 90 HOH A 464
SITE 1 AC5 5 GLN B 255 HOH B 322 HOH B 340 HOH B 394
SITE 2 AC5 5 HOH B 449
SITE 1 AC6 3 ASP B 110 ARG B 111 ARG B 114
SITE 1 AC7 4 ARG B 114 LEU B 136 TYR B 141 HOH B 402
CRYST1 41.690 78.100 85.100 90.00 103.41 90.00 P 1 21 1 4
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 0.023987 0.000000 0.005721 0.00000
SCALE2 0.000000 0.012804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012080 0.00000
TER 2531 ALA A 300
TER 5015 ALA B 300
MASTER 451 0 7 32 16 0 8 6 5191 2 13 48
END |