| 4WCV-pdb | HEADER HYDROLASE 05-SEP-14 4WCV
TITLE HALOALKANE DEHALOGENASE DHAA MUTANT FROM RHODOCOCCUS RHODOCHROUS
TITLE 2 (T148L+G171Q+A172V+C176G)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PAQN
KEYWDS HYDROLASE, MUTATION IN TUNNEL ACCESS
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HOLUBEVA,T.PRUDNIKOVA,I.KUTA-SMATANOVA,P.REZACOVA
REVDAT 1 15-OCT-14 4WCV 0
JRNL AUTH V.LISKOVA,D.BEDNAR,T.PRUDNIKOVA,P.REZACOVA,T.KOUDELAKOVA,
JRNL AUTH 2 E.SEBESTOVA,I.KUTA-SMATANOVA,J.BREZOVSKY,R.CHALOUPKOVA,
JRNL AUTH 3 J.DAMBORSKY
JRNL TITL BALANCING THE STABILITY-ACTIVITY TRADE-OFF BY FINE-TUNING
JRNL TITL 2 DEHALOGENASE ACCESS TUNNELS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 26995
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) : 0.123
REMARK 3 R VALUE (WORKING SET) : 0.120
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1421
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) : 1.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.73
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1882
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.1140
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.1850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2365
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 477
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : -0.01000
REMARK 3 B13 (A**2) : 0.01000
REMARK 3 B23 (A**2) : 0.01000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.208
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.179
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2557 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3510 ; 1.846 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 314 ; 5.774 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 129 ;30.920 ;23.566
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 386 ;12.812 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;20.548 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 363 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2061 ; 0.013 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1210 ; 1.103 ; 0.695
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1520 ; 1.408 ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1347 ; 2.244 ; 0.798
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4567 ; 3.449 ; 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): 2531 ; 4.112 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2436 ;10.696 ; 5.000
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 : 9
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 132
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0760 1.4900 -6.6560
REMARK 3 T TENSOR
REMARK 3 T11: 0.0146 T22: 0.0049
REMARK 3 T33: 0.0088 T12: -0.0075
REMARK 3 T13: -0.0107 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.0941 L22: 0.0728
REMARK 3 L33: 0.0877 L12: -0.0263
REMARK 3 L13: -0.0414 L23: 0.0127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0025 S12: 0.0065 S13: -0.0028
REMARK 3 S21: -0.0024 S22: -0.0038 S23: 0.0099
REMARK 3 S31: -0.0005 S32: -0.0077 S33: 0.0013
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 133 A 144
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5120 -8.9670 14.4840
REMARK 3 T TENSOR
REMARK 3 T11: 0.0260 T22: 0.0178
REMARK 3 T33: 0.0130 T12: -0.0077
REMARK 3 T13: 0.0056 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.2545 L22: 0.5393
REMARK 3 L33: 0.4698 L12: 0.3681
REMARK 3 L13: 0.3436 L23: 0.4913
REMARK 3 S TENSOR
REMARK 3 S11: -0.0265 S12: 0.0105 S13: -0.0039
REMARK 3 S21: -0.0517 S22: 0.0252 S23: -0.0091
REMARK 3 S31: -0.0276 S32: 0.0102 S33: 0.0014
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 145 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3500 -0.4640 20.1430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0197 T22: 0.0174
REMARK 3 T33: 0.0106 T12: -0.0032
REMARK 3 T13: -0.0097 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.2300 L22: 0.5915
REMARK 3 L33: 0.2655 L12: -0.3543
REMARK 3 L13: -0.2384 L23: 0.3545
REMARK 3 S TENSOR
REMARK 3 S11: -0.0149 S12: -0.0132 S13: -0.0022
REMARK 3 S21: 0.0269 S22: 0.0072 S23: 0.0078
REMARK 3 S31: 0.0085 S32: 0.0087 S33: 0.0077
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 159 A 167
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2890 9.0380 18.0270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0179 T22: 0.0079
REMARK 3 T33: 0.0070 T12: -0.0050
REMARK 3 T13: -0.0064 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.8467 L22: 0.1587
REMARK 3 L33: 0.2509 L12: -0.3209
REMARK 3 L13: -0.4356 L23: 0.1336
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: -0.0330 S13: 0.0231
REMARK 3 S21: 0.0035 S22: 0.0105 S23: -0.0195
REMARK 3 S31: -0.0011 S32: 0.0173 S33: -0.0042
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 168 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2970 11.6440 7.6700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0175 T22: 0.0089
REMARK 3 T33: 0.0163 T12: -0.0101
REMARK 3 T13: -0.0121 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.3429 L22: 0.1439
REMARK 3 L33: 0.1033 L12: -0.1738
REMARK 3 L13: -0.0734 L23: 0.1066
REMARK 3 S TENSOR
REMARK 3 S11: -0.0070 S12: -0.0159 S13: 0.0154
REMARK 3 S21: 0.0029 S22: 0.0106 S23: -0.0113
REMARK 3 S31: -0.0042 S32: 0.0087 S33: -0.0037
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 186 A 196
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2980 15.6270 5.7300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0195 T22: 0.0094
REMARK 3 T33: 0.0100 T12: -0.0041
REMARK 3 T13: -0.0098 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.4548 L22: 0.6742
REMARK 3 L33: 0.5109 L12: 0.0982
REMARK 3 L13: -0.4538 L23: -0.0386
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: 0.0245 S13: 0.0314
REMARK 3 S21: 0.0091 S22: 0.0082 S23: 0.0147
REMARK 3 S31: -0.0104 S32: -0.0065 S33: -0.0237
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 197 A 230
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7930 -7.6330 7.7960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0159 T22: 0.0068
REMARK 3 T33: 0.0123 T12: -0.0074
REMARK 3 T13: -0.0099 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.0590 L22: 0.2971
REMARK 3 L33: 0.0915 L12: -0.0146
REMARK 3 L13: -0.0473 L23: 0.0486
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: 0.0034 S13: -0.0120
REMARK 3 S21: 0.0065 S22: -0.0081 S23: 0.0181
REMARK 3 S31: 0.0056 S32: -0.0021 S33: 0.0092
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 231 A 263
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4000 -11.1430 -1.9720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0200 T22: 0.0175
REMARK 3 T33: 0.0126 T12: 0.0010
REMARK 3 T13: -0.0079 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.0117 L22: 0.3266
REMARK 3 L33: 0.1324 L12: 0.0471
REMARK 3 L13: 0.0132 L23: 0.1181
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: -0.0065 S13: -0.0026
REMARK 3 S21: 0.0150 S22: 0.0070 S23: -0.0061
REMARK 3 S31: 0.0227 S32: 0.0092 S33: -0.0022
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 264 A 295
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2010 -0.5740 -7.9940
REMARK 3 T TENSOR
REMARK 3 T11: 0.0167 T22: 0.0049
REMARK 3 T33: 0.0117 T12: -0.0060
REMARK 3 T13: -0.0094 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.1278 L22: 0.0874
REMARK 3 L33: 0.2371 L12: 0.0108
REMARK 3 L13: -0.0120 L23: 0.1034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: -0.0047 S13: -0.0060
REMARK 3 S21: -0.0077 S22: 0.0028 S23: -0.0151
REMARK 3 S31: -0.0037 S32: 0.0081 S33: -0.0081
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4WCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000202749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
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 : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28416
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 39.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.17000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 9.160
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3G9X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE TRIHYDRATE, AMMONIUM
REMARK 280 ACETATE, PEG 4000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SER A 2
REMARK 465 GLU A 3
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
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 O HOH A 1008 O HOH A 1020 1.92
REMARK 500 O HOH A 701 O HOH A 1008 1.98
REMARK 500 O4 PGE A 502 O HOH A 1076 2.09
REMARK 500 OE2 GLU A 183 O HOH A 601 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 653 O HOH A 665 1565 2.08
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 21 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 133 NE - CZ - NH1 ANGL. DEV. = -3.0 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
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 42 51.00 -107.80
REMARK 500 THR A 43 -158.68 -105.26
REMARK 500 GLU A 98 -92.24 -107.96
REMARK 500 GLU A 98 -88.28 -111.07
REMARK 500 ASP A 106 -130.44 50.16
REMARK 500 ARG A 153 46.14 -91.23
REMARK 500 ASP A 156 -71.73 -102.85
REMARK 500 GLN A 171 -63.95 -107.22
REMARK 500 VAL A 245 -77.22 -134.67
REMARK 500 LEU A 271 -92.65 -120.35
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 875 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A 938 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A1041 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH A1042 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH A1052 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A1053 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A1056 DISTANCE = 7.25 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F5Z RELATED DB: PDB
REMARK 900 4F5Z CONTAINS L95V, A172V MUTATIONS IN ACCESS TUNNEL
REMARK 900 RELATED ID: 4F60 RELATED DB: PDB
REMARK 900 4F60 CONTAINS T148L, G171Q, A172V, C176F MUTATIOSN IN ACCESS TUNNEL
DBREF 4WCV A 1 293 UNP P0A3G3 DHAA_RHOSO 1 293
SEQADV 4WCV LEU A 148 UNP P0A3G3 THR 148 ENGINEERED MUTATION
SEQADV 4WCV GLN A 171 UNP P0A3G3 GLY 171 ENGINEERED MUTATION
SEQADV 4WCV VAL A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 4WCV GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 4WCV HIS A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 4WCV HIS A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 4WCV HIS A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 4WCV HIS A 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 4WCV HIS A 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 4WCV HIS A 299 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 299 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 299 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR ALA ASP
SEQRES 13 A 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 A 299 GLU GLN VAL LEU PRO LYS GLY VAL VAL ARG PRO LEU THR
SEQRES 15 A 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 299 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 299 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
HET CL A 501 1
HET PGE A 502 10
HET ACT A 503 4
HET ACT A 504 4
HETNAM CL CHLORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM ACT ACETATE ION
FORMUL 2 CL CL 1-
FORMUL 3 PGE C6 H14 O4
FORMUL 4 ACT 2(C2 H3 O2 1-)
FORMUL 6 HOH *477(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 PHE A 144 5 3
HELIX 7 AA7 ALA A 145 ARG A 153 1 9
HELIX 8 AA8 ASP A 156 ILE A 163 1 8
HELIX 9 AA9 ASN A 166 GLN A 171 1 6
HELIX 10 AB1 GLN A 171 GLY A 176 1 6
HELIX 11 AB2 THR A 182 GLU A 191 1 10
HELIX 12 AB3 PRO A 192 LEU A 194 5 3
HELIX 13 AB4 LYS A 195 ASP A 198 5 4
HELIX 14 AB5 ARG A 199 LEU A 209 1 11
HELIX 15 AB6 PRO A 215 SER A 232 1 18
HELIX 16 AB7 PRO A 248 LEU A 259 1 12
HELIX 17 AB8 TYR A 273 ASN A 278 1 6
HELIX 18 AB9 ASN A 278 LEU A 290 1 13
HELIX 19 AC1 PRO A 291 HIS A 294 5 4
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O MET A 22 N VAL A 15
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N CYS A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O LYS A 263 N LEU A 238
CISPEP 1 ASN A 41 PRO A 42 0 -3.19
CISPEP 2 GLU A 214 PRO A 215 0 -2.86
CISPEP 3 GLU A 214 PRO A 215 0 -7.75
CISPEP 4 THR A 242 PRO A 243 0 5.00
SITE 1 AC1 5 ASN A 41 TRP A 107 PRO A 206 PGE A 502
SITE 2 AC1 5 HOH A1076
SITE 1 AC2 6 ASP A 106 PHE A 144 PHE A 168 LYS A 175
SITE 2 AC2 6 CL A 501 HOH A1076
SITE 1 AC3 8 PRO A 12 GLN A 231 PRO A 233 PRO A 260
SITE 2 AC3 8 HOH A 603 HOH A 628 HOH A 663 HOH A 689
SITE 1 AC4 7 THR A 33 HIS A 59 LYS A 124 LEU A 290
SITE 2 AC4 7 HIS A 294 HOH A 823 HOH A 982
CRYST1 42.585 44.477 46.508 115.47 98.79 109.12 P 1 1
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 0.023482 0.008142 0.009113 0.00000
SCALE2 0.000000 0.023797 0.014263 0.00000
SCALE3 0.000000 0.000000 0.025366 0.00000
TER 2450 HIS A 296
MASTER 522 0 4 19 8 0 8 6 2861 1 18 23
END
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