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HEADER OXIDOREDUCTASE 06-AUG-08 3E3A
TITLE THE STRUCTURE OF RV0554 FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POSSIBLE PEROXIDASE BPOC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NON-HAEM PEROXIDASE, PUTATIVE BROMOPEROXIDASE;
COMPND 5 EC: 1.11.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37 RV;
SOURCE 5 GENE: BPOC, MT0580, RV0554;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX
KEYWDS ALPHA/BETA HYDROLASE, OXIDOREDUCTASE, PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.JOHNSTON,E.N.BAKER
REVDAT 1 23-JUN-09 3E3A 0
JRNL AUTH J.M.JOHNSTON,E.N.BAKER
JRNL TITL THE STRUCTURE OF RV0554 FROM M. TUBERCULOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0078
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 26997
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2703
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1378
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 156
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4211
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.95000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : 1.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.360
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.256
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.191
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.869
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4327 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5893 ; 1.680 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 547 ; 6.049 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 200 ;35.127 ;23.200
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 645 ;17.730 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;18.790 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 652 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3394 ; 0.008 ; 0.021
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): 2745 ; 0.731 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4395 ; 1.337 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1582 ; 2.443 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1498 ; 3.785 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 260 6
REMARK 3 1 B 1 B 260 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 1982 ; 0.310 ; 5.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 1982 ; 2.430 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
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 -11 A 9
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1280 11.9250 -0.7580
REMARK 3 T TENSOR
REMARK 3 T11: 0.9917 T22: 0.2869
REMARK 3 T33: 0.0050 T12: -0.0158
REMARK 3 T13: 0.0317 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 8.6742 L22: 1.8879
REMARK 3 L33: 5.4229 L12: 3.9286
REMARK 3 L13: 2.8323 L23: 0.5837
REMARK 3 S TENSOR
REMARK 3 S11: 0.4600 S12: 0.1304 S13: 0.3491
REMARK 3 S21: 0.2169 S22: -0.3874 S23: 0.0036
REMARK 3 S31: 0.1934 S32: 0.3724 S33: -0.0727
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 10 A 126
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6640 1.0020 -8.0320
REMARK 3 T TENSOR
REMARK 3 T11: 0.7435 T22: 0.2276
REMARK 3 T33: 0.0395 T12: -0.0381
REMARK 3 T13: 0.0078 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.8506 L22: 1.7503
REMARK 3 L33: 1.9846 L12: 0.0120
REMARK 3 L13: 0.0528 L23: -0.1753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: -0.0365 S13: 0.0323
REMARK 3 S21: 0.3537 S22: 0.0005 S23: 0.1134
REMARK 3 S31: 0.0570 S32: 0.0239 S33: 0.0033
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 127 A 187
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4520 3.1510 -26.6360
REMARK 3 T TENSOR
REMARK 3 T11: 0.7219 T22: 0.2160
REMARK 3 T33: 0.0467 T12: 0.0168
REMARK 3 T13: 0.0031 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.5549 L22: 1.1766
REMARK 3 L33: 2.3461 L12: -0.1599
REMARK 3 L13: 0.1195 L23: 0.9271
REMARK 3 S TENSOR
REMARK 3 S11: 0.1534 S12: 0.0335 S13: -0.1084
REMARK 3 S21: -0.0289 S22: -0.0220 S23: -0.1055
REMARK 3 S31: 0.0184 S32: 0.1663 S33: -0.1315
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 188 A 262
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3140 -9.6260 -13.3950
REMARK 3 T TENSOR
REMARK 3 T11: 0.7535 T22: 0.1967
REMARK 3 T33: 0.0925 T12: -0.0951
REMARK 3 T13: 0.0238 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.8933 L22: 2.4806
REMARK 3 L33: 3.0408 L12: -0.6812
REMARK 3 L13: 0.1415 L23: 0.0669
REMARK 3 S TENSOR
REMARK 3 S11: 0.1121 S12: 0.0253 S13: -0.1603
REMARK 3 S21: 0.1145 S22: -0.0095 S23: 0.1957
REMARK 3 S31: 0.4959 S32: -0.2463 S33: -0.1026
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 : B -12 B 26
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1040 33.7230 -15.8770
REMARK 3 T TENSOR
REMARK 3 T11: 0.7408 T22: 0.2836
REMARK 3 T33: 0.1319 T12: 0.0140
REMARK 3 T13: -0.0025 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.1845 L22: 2.2557
REMARK 3 L33: 4.1792 L12: -0.2528
REMARK 3 L13: -0.8576 L23: 0.5697
REMARK 3 S TENSOR
REMARK 3 S11: 0.0943 S12: 0.1121 S13: -0.0459
REMARK 3 S21: 0.0601 S22: -0.1409 S23: 0.3526
REMARK 3 S31: -0.3112 S32: -0.2645 S33: 0.0467
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 : B 27 B 126
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9260 35.0200 -19.4250
REMARK 3 T TENSOR
REMARK 3 T11: 0.7542 T22: 0.2287
REMARK 3 T33: 0.0534 T12: -0.0119
REMARK 3 T13: -0.0043 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.4815 L22: 1.7712
REMARK 3 L33: 1.6027 L12: 0.4348
REMARK 3 L13: -0.2860 L23: -0.2746
REMARK 3 S TENSOR
REMARK 3 S11: 0.0778 S12: -0.0499 S13: 0.0602
REMARK 3 S21: 0.3079 S22: -0.0861 S23: 0.0702
REMARK 3 S31: -0.2472 S32: 0.0282 S33: 0.0084
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 : B 127 B 187
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9500 40.1580 -38.1880
REMARK 3 T TENSOR
REMARK 3 T11: 0.7036 T22: 0.2192
REMARK 3 T33: 0.0789 T12: 0.0065
REMARK 3 T13: -0.0265 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 0.5758 L22: 2.2940
REMARK 3 L33: 5.4401 L12: -0.2403
REMARK 3 L13: -1.7539 L23: 1.1958
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: 0.0590 S13: 0.0128
REMARK 3 S21: 0.0944 S22: -0.0895 S23: 0.2908
REMARK 3 S31: 0.0986 S32: -0.4083 S33: 0.0841
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 : B 188 B 261
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3020 31.7890 -24.8000
REMARK 3 T TENSOR
REMARK 3 T11: 0.6564 T22: 0.2574
REMARK 3 T33: 0.0732 T12: -0.0320
REMARK 3 T13: -0.0266 T23: 0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 1.5495 L22: 3.2620
REMARK 3 L33: 2.8729 L12: 0.5670
REMARK 3 L13: -0.2797 L23: -1.0646
REMARK 3 S TENSOR
REMARK 3 S11: 0.0549 S12: -0.0519 S13: -0.0426
REMARK 3 S21: -0.0089 S22: -0.1780 S23: -0.3822
REMARK 3 S31: 0.0465 S32: 0.3689 S33: 0.1231
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 ADDED IN THE
REMARK 4
REMARK 4 3E3A COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048820.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.92
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97907
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29742
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.74800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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 (%): 57.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH 4.92, 7.5%
REMARK 280 MPD, VAPOR DIFFUSION, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.35200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.08250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.94500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.08250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.35200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.94500
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 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: 4630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 MET A -30
REMARK 465 SER A -29
REMARK 465 TYR A -28
REMARK 465 TYR A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 ASP A -20
REMARK 465 TYR A -19
REMARK 465 ASP A -18
REMARK 465 ILE A -17
REMARK 465 PRO A -16
REMARK 465 THR A -15
REMARK 465 THR A -14
REMARK 465 GLU A -13
REMARK 465 ASN A -12
REMARK 465 MET B -30
REMARK 465 SER B -29
REMARK 465 TYR B -28
REMARK 465 TYR B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 HIS B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 ASP B -20
REMARK 465 TYR B -19
REMARK 465 ASP B -18
REMARK 465 ILE B -17
REMARK 465 PRO B -16
REMARK 465 THR B -15
REMARK 465 THR B -14
REMARK 465 ALA B 262
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 B 368 O HOH B 370 2.15
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 ASP A 8 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU A 148 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG B 21 NE - CZ - NH1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG B 21 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP B 117 CB - CG - OD1 ANGL. DEV. = 5.9 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 -3 -19.12 -43.94
REMARK 500 ASN A 48 143.56 -37.45
REMARK 500 SER A 87 -118.35 53.72
REMARK 500 ASP A 117 -179.44 -65.85
REMARK 500 HIS B 31 -46.34 -130.79
REMARK 500 SER B 87 -116.32 59.84
REMARK 500 PRO B 188 90.79 -61.13
REMARK 500 LEU B 240 33.95 -96.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 265
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 263
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV0554 RELATED DB: TARGETDB
DBREF 3E3A A -5 262 UNP O06420 O06420_MYCTU 1 262
DBREF 3E3A B -5 262 UNP O06420 O06420_MYCTU 1 262
SEQADV 3E3A MET A -30 UNP O06420 EXPRESSION TAG
SEQADV 3E3A SER A -29 UNP O06420 EXPRESSION TAG
SEQADV 3E3A TYR A -28 UNP O06420 EXPRESSION TAG
SEQADV 3E3A TYR A -27 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS A -26 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS A -25 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS A -24 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS A -23 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS A -22 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS A -21 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ASP A -20 UNP O06420 EXPRESSION TAG
SEQADV 3E3A TYR A -19 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ASP A -18 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ILE A -17 UNP O06420 EXPRESSION TAG
SEQADV 3E3A PRO A -16 UNP O06420 EXPRESSION TAG
SEQADV 3E3A THR A -15 UNP O06420 EXPRESSION TAG
SEQADV 3E3A THR A -14 UNP O06420 EXPRESSION TAG
SEQADV 3E3A GLU A -13 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ASN A -12 UNP O06420 EXPRESSION TAG
SEQADV 3E3A LEU A -11 UNP O06420 EXPRESSION TAG
SEQADV 3E3A TYR A -10 UNP O06420 EXPRESSION TAG
SEQADV 3E3A PHE A -9 UNP O06420 EXPRESSION TAG
SEQADV 3E3A GLN A -8 UNP O06420 EXPRESSION TAG
SEQADV 3E3A GLY A -7 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ALA A -6 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ASP A -4 UNP O06420 EXPRESSION TAG
SEQADV 3E3A PRO A -3 UNP O06420 EXPRESSION TAG
SEQADV 3E3A GLU A -2 UNP O06420 EXPRESSION TAG
SEQADV 3E3A PHE A -1 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ARG A 0 UNP O06420 EXPRESSION TAG
SEQADV 3E3A VAL A 1 UNP O06420 EXPRESSION TAG
SEQADV 3E3A MET B -30 UNP O06420 EXPRESSION TAG
SEQADV 3E3A SER B -29 UNP O06420 EXPRESSION TAG
SEQADV 3E3A TYR B -28 UNP O06420 EXPRESSION TAG
SEQADV 3E3A TYR B -27 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS B -26 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS B -25 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS B -24 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS B -23 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS B -22 UNP O06420 EXPRESSION TAG
SEQADV 3E3A HIS B -21 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ASP B -20 UNP O06420 EXPRESSION TAG
SEQADV 3E3A TYR B -19 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ASP B -18 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ILE B -17 UNP O06420 EXPRESSION TAG
SEQADV 3E3A PRO B -16 UNP O06420 EXPRESSION TAG
SEQADV 3E3A THR B -15 UNP O06420 EXPRESSION TAG
SEQADV 3E3A THR B -14 UNP O06420 EXPRESSION TAG
SEQADV 3E3A GLU B -13 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ASN B -12 UNP O06420 EXPRESSION TAG
SEQADV 3E3A LEU B -11 UNP O06420 EXPRESSION TAG
SEQADV 3E3A TYR B -10 UNP O06420 EXPRESSION TAG
SEQADV 3E3A PHE B -9 UNP O06420 EXPRESSION TAG
SEQADV 3E3A GLN B -8 UNP O06420 EXPRESSION TAG
SEQADV 3E3A GLY B -7 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ALA B -6 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ASP B -4 UNP O06420 EXPRESSION TAG
SEQADV 3E3A PRO B -3 UNP O06420 EXPRESSION TAG
SEQADV 3E3A GLU B -2 UNP O06420 EXPRESSION TAG
SEQADV 3E3A PHE B -1 UNP O06420 EXPRESSION TAG
SEQADV 3E3A ARG B 0 UNP O06420 EXPRESSION TAG
SEQADV 3E3A VAL B 1 UNP O06420 EXPRESSION TAG
SEQRES 1 A 293 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 293 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 293 ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP
SEQRES 4 A 293 ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG
SEQRES 5 A 293 GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO
SEQRES 6 A 293 ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP
SEQRES 7 A 293 ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE
SEQRES 8 A 293 THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE
SEQRES 9 A 293 GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL
SEQRES 10 A 293 SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL
SEQRES 11 A 293 ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR
SEQRES 12 A 293 ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS
SEQRES 13 A 293 ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO
SEQRES 14 A 293 PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE
SEQRES 15 A 293 SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP
SEQRES 16 A 293 TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR
SEQRES 17 A 293 PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR
SEQRES 18 A 293 ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL
SEQRES 19 A 293 LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO
SEQRES 20 A 293 TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY
SEQRES 21 A 293 ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE
SEQRES 22 A 293 PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS
SEQRES 23 A 293 PHE PHE ALA SER VAL LYS ALA
SEQRES 1 B 293 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 293 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 B 293 ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP
SEQRES 4 B 293 ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG
SEQRES 5 B 293 GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO
SEQRES 6 B 293 ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP
SEQRES 7 B 293 ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE
SEQRES 8 B 293 THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE
SEQRES 9 B 293 GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL
SEQRES 10 B 293 SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL
SEQRES 11 B 293 ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR
SEQRES 12 B 293 ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS
SEQRES 13 B 293 ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO
SEQRES 14 B 293 PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE
SEQRES 15 B 293 SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP
SEQRES 16 B 293 TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR
SEQRES 17 B 293 PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR
SEQRES 18 B 293 ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL
SEQRES 19 B 293 LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO
SEQRES 20 B 293 TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY
SEQRES 21 B 293 ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE
SEQRES 22 B 293 PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS
SEQRES 23 B 293 PHE PHE ALA SER VAL LYS ALA
HET ACT A 264 4
HET MPD A 265 8
HET ACT B 263 4
HETNAM ACT ACETATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 MPD C6 H14 O2
FORMUL 6 HOH *215(H2 O)
HELIX 1 1 ALA A 24 HIS A 29 5 6
HELIX 2 2 GLN A 32 ALA A 39 1 8
HELIX 3 3 ILE A 51 GLU A 55 5 5
HELIX 4 4 THR A 61 LEU A 76 1 16
HELIX 5 5 SER A 87 ALA A 100 1 14
HELIX 6 6 ASP A 117 SER A 133 1 17
HELIX 7 7 PRO A 138 PHE A 151 1 14
HELIX 8 8 SER A 152 ASN A 157 1 6
HELIX 9 9 ASP A 158 TRP A 172 1 15
HELIX 10 10 THR A 177 ASP A 185 1 9
HELIX 11 11 ARG A 192 ARG A 197 1 6
HELIX 12 12 PRO A 215 LEU A 226 1 12
HELIX 13 13 LEU A 240 ARG A 245 1 6
HELIX 14 14 ARG A 245 SER A 259 1 15
HELIX 15 15 ALA B 24 HIS B 29 5 6
HELIX 16 16 HIS B 31 ALA B 39 1 9
HELIX 17 17 ILE B 51 GLU B 55 5 5
HELIX 18 18 THR B 61 LEU B 76 1 16
HELIX 19 19 SER B 87 ALA B 100 1 14
HELIX 20 20 ASP B 117 SER B 133 1 17
HELIX 21 21 PRO B 138 PHE B 151 1 14
HELIX 22 22 SER B 152 ASN B 157 1 6
HELIX 23 23 ASP B 158 TRP B 172 1 15
HELIX 24 24 THR B 177 LEU B 184 1 8
HELIX 25 25 ARG B 192 ILE B 199 5 8
HELIX 26 26 PRO B 215 LEU B 226 1 12
HELIX 27 27 LEU B 240 ARG B 245 1 6
HELIX 28 28 ARG B 245 VAL B 260 1 16
SHEET 1 A 8 TYR A -10 GLN A -8 0
SHEET 2 A 8 ASN A 3 ASN A 9 -1 O LEU A 4 N PHE A -9
SHEET 3 A 8 TYR A 41 PHE A 46 -1 O THR A 45 N ASP A 7
SHEET 4 A 8 ASP A 13 ILE A 18 1 N VAL A 15 O ILE A 44
SHEET 5 A 8 ALA A 81 VAL A 86 1 O ARG A 82 N VAL A 16
SHEET 6 A 8 VAL A 104 MET A 110 1 O VAL A 108 N VAL A 83
SHEET 7 A 8 VAL A 203 PHE A 208 1 O ILE A 206 N LEU A 109
SHEET 8 A 8 GLY A 229 ILE A 234 1 O ILE A 234 N GLY A 207
SHEET 1 B 8 LEU B -11 GLN B -8 0
SHEET 2 B 8 ASN B 3 ASN B 9 -1 O TYR B 6 N LEU B -11
SHEET 3 B 8 TYR B 41 PHE B 46 -1 O THR B 45 N ASP B 7
SHEET 4 B 8 ASP B 13 ILE B 18 1 N VAL B 15 O ILE B 44
SHEET 5 B 8 ALA B 81 VAL B 86 1 O VAL B 84 N ILE B 18
SHEET 6 B 8 VAL B 104 MET B 110 1 O VAL B 108 N VAL B 83
SHEET 7 B 8 VAL B 203 PHE B 208 1 O LEU B 204 N LEU B 109
SHEET 8 B 8 GLY B 229 ILE B 234 1 O LEU B 232 N GLY B 207
CISPEP 1 ALA A 79 PRO A 80 0 -3.51
CISPEP 2 ALA B 79 PRO B 80 0 -3.34
SITE 1 AC1 3 ARG A 146 LEU A 240 PHE A 243
SITE 1 AC2 1 MET B -5
CRYST1 48.704 97.890 146.165 90.00 90.00 90.00 P 21 21 21 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 0.020532 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010216 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006842 0.00000
TER 2101 ALA A 262
TER 4213 LYS B 261
MASTER 501 0 3 28 16 0 2 6 4442 2 16 46
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