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HEADER TRANSFERASE 05-SEP-02 1MO2
TITLE THIOESTERASE DOMAIN FROM 6-DEOXYERYTHRONOLIDE SYNTHASE
TITLE 2 (DEBS TE), PH 8.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERYTHRONOLIDE SYNTHASE, MODULES 5 AND 6;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN;
COMPND 5 SYNONYM: 6-DEOXYERYTHRONOLIDE B SYNTHASE III; DEBS 3; DEBS
COMPND 6 TE; ERYTHRONOLIDE SYNTHASE III;
COMPND 7 EC: 2.3.1.94;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: ERYA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21C
KEYWDS THIOESTERASE, POLYKETIDE SYNTHASE, OPEN SUBSTRATE CHANNEL,
KEYWDS 2 TE, PKS, ALPHA BETA HYDROLASE, 6-DEOXYERYTHRONOLIDE,
KEYWDS 3 PICROMYCIN, PIKROMYCIN, ERYTHROMYCIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-C.TSAI,H.LU,D.E.CANE,C.KHOSLA,R.M.STROUD
REVDAT 1 04-FEB-03 1MO2 0
JRNL AUTH S.-C.TSAI,H.LU,D.E.CANE,C.KHOSLA,R.M.STROUD
JRNL TITL INSIGHTS INTO CHANNEL ARCHITECTURE AND SUBSTRATE
JRNL TITL 2 SPECIFICITY FROM CRYSTAL STRUCTURES OF TWO
JRNL TITL 3 MACROCYCLE-FORMING THIOESTERASES OF MODULAR
JRNL TITL 4 POLYKETIDE SYNTHASES
JRNL REF BIOCHEMISTRY V. 41 12598 2002
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 22595
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1223
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1531
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 93
REMARK 3 BIN FREE R VALUE : 0.3930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 3832
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.40000
REMARK 3 B22 (A**2) : -1.03000
REMARK 3 B33 (A**2) : -3.37000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.893
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.855
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3880 ; 0.043 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5304 ; 3.562 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 498 ;12.597 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 580 ; 0.240 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3058 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2049 ; 0.336 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 179 ; 0.241 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 326 ; 0.748 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.570 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 2494 ; 1.318 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3984 ; 2.470 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1386 ; 4.183 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1320 ; 6.983 ; 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 : 0
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 26 A 160
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2379 50.7432 63.4611
REMARK 3 T TENSOR
REMARK 3 T11: 0.2426 T22: 0.0783
REMARK 3 T33: 0.1628 T12: -0.0073
REMARK 3 T13: -0.0176 T23: -0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 1.9796 L22: 4.0227
REMARK 3 L33: 8.0957 L12: 0.5264
REMARK 3 L13: -0.3124 L23: -3.7010
REMARK 3 S TENSOR
REMARK 3 S11: 0.1379 S12: -0.2848 S13: 0.1926
REMARK 3 S21: 0.6558 S22: 0.0078 S23: 0.1722
REMARK 3 S31: -0.7097 S32: -0.0596 S33: -0.1457
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 161 A 220
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5046 39.5223 62.0341
REMARK 3 T TENSOR
REMARK 3 T11: 0.2792 T22: 0.3817
REMARK 3 T33: 0.3010 T12: 0.1346
REMARK 3 T13: 0.0090 T23: 0.0312
REMARK 3 L TENSOR
REMARK 3 L11: 2.9896 L22: 5.2681
REMARK 3 L33: 6.5389 L12: -0.3886
REMARK 3 L13: 0.1494 L23: -0.8359
REMARK 3 S TENSOR
REMARK 3 S11: 0.0683 S12: -0.1288 S13: -0.4295
REMARK 3 S21: 0.1066 S22: -0.0219 S23: -0.6599
REMARK 3 S31: 0.9077 S32: 1.3865 S33: -0.0464
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 221 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5248 37.2728 46.4705
REMARK 3 T TENSOR
REMARK 3 T11: 0.4539 T22: 0.3279
REMARK 3 T33: 0.3903 T12: -0.0486
REMARK 3 T13: 0.1565 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 13.4036 L22: 14.0993
REMARK 3 L33: 11.4652 L12: -0.3289
REMARK 3 L13: -2.4054 L23: 0.7738
REMARK 3 S TENSOR
REMARK 3 S11: -0.8356 S12: -0.6464 S13: -2.3100
REMARK 3 S21: -1.9777 S22: 0.6412 S23: -1.2321
REMARK 3 S31: 0.9234 S32: 1.6924 S33: 0.1944
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 251 A 280
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7673 50.9046 43.2633
REMARK 3 T TENSOR
REMARK 3 T11: 0.3398 T22: 0.1333
REMARK 3 T33: 0.1023 T12: 0.0641
REMARK 3 T13: 0.0910 T23: 0.0594
REMARK 3 L TENSOR
REMARK 3 L11: 8.0159 L22: 8.9776
REMARK 3 L33: 7.2555 L12: -1.6598
REMARK 3 L13: -1.0714 L23: -3.1028
REMARK 3 S TENSOR
REMARK 3 S11: 0.3739 S12: -0.3891 S13: 0.5271
REMARK 3 S21: -0.7895 S22: -0.6408 S23: -0.8896
REMARK 3 S31: 0.5868 S32: 0.9843 S33: 0.2668
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 26 B 160
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8513 32.3085 98.4186
REMARK 3 T TENSOR
REMARK 3 T11: 0.0267 T22: 0.1633
REMARK 3 T33: 0.1072 T12: 0.0327
REMARK 3 T13: 0.0509 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 3.3949 L22: 2.4245
REMARK 3 L33: 6.1430 L12: -0.1336
REMARK 3 L13: 2.2441 L23: 0.2726
REMARK 3 S TENSOR
REMARK 3 S11: 0.1171 S12: 0.2069 S13: 0.0802
REMARK 3 S21: -0.4922 S22: 0.0540 S23: -0.1221
REMARK 3 S31: 0.1775 S32: 0.0338 S33: -0.1711
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 161 B 220
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3030 35.2171 99.5533
REMARK 3 T TENSOR
REMARK 3 T11: 0.2971 T22: 0.5326
REMARK 3 T33: 0.3385 T12: 0.1382
REMARK 3 T13: -0.0030 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 7.7237 L22: 3.6171
REMARK 3 L33: 7.7213 L12: 1.2652
REMARK 3 L13: 3.2158 L23: 0.2943
REMARK 3 S TENSOR
REMARK 3 S11: -0.1019 S12: -0.4187 S13: 0.3179
REMARK 3 S21: -0.6052 S22: 0.2133 S23: 1.2628
REMARK 3 S31: -0.4100 S32: -1.9267 S33: -0.1114
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 221 B 250
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0816 33.7765 115.0855
REMARK 3 T TENSOR
REMARK 3 T11: 0.2892 T22: 0.7483
REMARK 3 T33: 0.6294 T12: 0.0210
REMARK 3 T13: 0.1069 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 10.8375 L22: 5.0728
REMARK 3 L33: 13.3263 L12: 7.4091
REMARK 3 L13: -4.5828 L23: 2.6574
REMARK 3 S TENSOR
REMARK 3 S11: 0.4684 S12: -0.6468 S13: 0.9059
REMARK 3 S21: 0.3249 S22: -0.4265 S23: 2.6659
REMARK 3 S31: -0.8170 S32: -2.1137 S33: -0.0419
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 251 B 280
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3683 43.5914 118.4553
REMARK 3 T TENSOR
REMARK 3 T11: 0.0497 T22: 0.3977
REMARK 3 T33: 0.2695 T12: 0.0456
REMARK 3 T13: 0.0695 T23: -0.0876
REMARK 3 L TENSOR
REMARK 3 L11: 6.8040 L22: 7.8034
REMARK 3 L33: 3.0840 L12: 0.0251
REMARK 3 L13: 1.2589 L23: 2.6878
REMARK 3 S TENSOR
REMARK 3 S11: -0.1319 S12: -0.5668 S13: 0.9318
REMARK 3 S21: -0.0126 S22: -0.4000 S23: 0.0956
REMARK 3 S31: -0.4596 S32: -0.9797 S33: 0.5319
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 : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MO2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PRAGUE ON 19-SEP-2002.
REMARK 100 THE RCSB ID CODE IS RCSB017046.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-1999
REMARK 200 TEMPERATURE (KELVIN) : 190.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26440
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.200
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1KEZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, BICINE, MAGNESIUM
REMARK 280 CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP AT 277K
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-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 SMTRY1 2 -1.000000 0.000000 0.000000 40.25000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.25000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.25000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.25000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.25000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 LEU A 5
REMARK 465 ASP A 6
REMARK 465 SER A 7
REMARK 465 GLY A 8
REMARK 465 THR A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 GLU A 13
REMARK 465 ALA A 14
REMARK 465 SER A 15
REMARK 465 SER A 16
REMARK 465 ALA A 17
REMARK 465 LEU A 18
REMARK 465 ARG A 19
REMARK 465 ASP A 20
REMARK 465 GLY A 21
REMARK 465 TYR A 22
REMARK 465 ARG A 23
REMARK 465 GLN A 24
REMARK 465 ALA A 25
REMARK 465 ASP A 192
REMARK 465 ARG A 193
REMARK 465 GLU A 194
REMARK 465 THR A 195
REMARK 465 GLY A 281
REMARK 465 ASN A 282
REMARK 465 SER A 283
REMARK 465 SER A 284
REMARK 465 SER A 285
REMARK 465 VAL A 286
REMARK 465 ASP A 287
REMARK 465 LYS A 288
REMARK 465 LEU A 289
REMARK 465 ALA A 290
REMARK 465 ALA A 291
REMARK 465 ALA A 292
REMARK 465 LEU A 293
REMARK 465 GLU A 294
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 LEU B 5
REMARK 465 ASP B 6
REMARK 465 SER B 7
REMARK 465 GLY B 8
REMARK 465 THR B 9
REMARK 465 PRO B 10
REMARK 465 ALA B 11
REMARK 465 ARG B 12
REMARK 465 GLU B 13
REMARK 465 ALA B 14
REMARK 465 SER B 15
REMARK 465 SER B 16
REMARK 465 ALA B 17
REMARK 465 LEU B 18
REMARK 465 ARG B 19
REMARK 465 ASP B 20
REMARK 465 GLY B 21
REMARK 465 TYR B 22
REMARK 465 ARG B 23
REMARK 465 GLN B 24
REMARK 465 ALA B 25
REMARK 465 ASP B 192
REMARK 465 ARG B 193
REMARK 465 GLU B 194
REMARK 465 THR B 195
REMARK 465 GLY B 281
REMARK 465 ASN B 282
REMARK 465 SER B 283
REMARK 465 SER B 284
REMARK 465 SER B 285
REMARK 465 VAL B 286
REMARK 465 ASP B 287
REMARK 465 LYS B 288
REMARK 465 LEU B 289
REMARK 465 ALA B 290
REMARK 465 ALA B 291
REMARK 465 ALA B 292
REMARK 465 LEU B 293
REMARK 465 GLU B 294
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 N THR A 261 N HIS B 259 2564 2.19
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 233 CG PRO A 233 CB 0.106
REMARK 500 PHE A 260 C PHE A 260 CA 0.084
REMARK 500 ILE B 128 CB ILE B 128 CA 0.059
REMARK 500 PRO B 233 CG PRO B 233 CB 0.058
REMARK 500 MET B 234 CE MET B 234 SD 0.064
REMARK 500 HIS B 259 CA HIS B 259 N -0.057
REMARK 500 THR B 261 CB THR B 261 CA 0.081
REMARK 500 MET B 262 CE MET B 262 SD -0.074
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 29 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 GLY A 64 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLN A 176 N - CA - C ANGL. DEV. =-12.8 DEGREES
REMARK 500 LEU A 190 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 PRO A 247 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 HIS A 259 N - CA - C ANGL. DEV. = 14.0 DEGREES
REMARK 500 PHE A 260 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 VAL B 138 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 HIS B 259 N - CA - C ANGL. DEV. = 10.2 DEGREES
REMARK 500 HIS B 266 N - CA - C ANGL. DEV. =-13.9 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 142 -51.49 134.64
REMARK 500 TYR A 171 160.06 63.64
REMARK 500 ASP A 177 -33.99 73.02
REMARK 500 ARG A 197 153.36 74.03
REMARK 500 PHE A 248 129.93 80.81
REMARK 500 HIS A 259 -127.50 172.73
REMARK 500 SER B 80 147.02 50.21
REMARK 500 SER B 142 -60.55 63.76
REMARK 500 TYR B 171 153.08 65.95
REMARK 500 ASP B 177 -67.93 76.45
REMARK 500 ARG B 197 127.95 64.01
REMARK 500 SER B 241 -101.66 -164.38
REMARK 500 PHE B 248 155.17 54.18
REMARK 500 THR B 261 -116.10 175.98
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KEZ RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM 6-DEOXYERYTHRONOLIDE SYNTHASE
REMARK 900 (DEBS TE), PH 7.2
REMARK 900 RELATED ID: 1MN6 RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE
REMARK 900 (PICS TE), PH 7.6
REMARK 900 RELATED ID: 1MNA RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE
REMARK 900 (PICS TE), PH 8.0
REMARK 900 RELATED ID: 1MNQ RELATED DB: PDB
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE
REMARK 900 (PICS TE), PH 8.4
DBREF 1MO2 A 4 283 SWS Q03133 ERY3_SACER 2893 3172
DBREF 1MO2 B 4 283 SWS Q03133 ERY3_SACER 2893 3172
SEQADV 1MO2 MET A 1 Q03133 INSERTION
SEQADV 1MO2 ALA A 2 Q03133 INSERTION
SEQADV 1MO2 SER A 3 Q03133 INSERTION
SEQADV 1MO2 SER A 284 Q03133 INSERTION
SEQADV 1MO2 SER A 285 Q03133 INSERTION
SEQADV 1MO2 VAL A 286 Q03133 INSERTION
SEQADV 1MO2 ASP A 287 Q03133 INSERTION
SEQADV 1MO2 LYS A 288 Q03133 INSERTION
SEQADV 1MO2 LEU A 289 Q03133 INSERTION
SEQADV 1MO2 ALA A 290 Q03133 INSERTION
SEQADV 1MO2 ALA A 291 Q03133 INSERTION
SEQADV 1MO2 ALA A 292 Q03133 INSERTION
SEQADV 1MO2 LEU A 293 Q03133 INSERTION
SEQADV 1MO2 GLU A 294 Q03133 INSERTION
SEQADV 1MO2 MET B 1 Q03133 INSERTION
SEQADV 1MO2 ALA B 2 Q03133 INSERTION
SEQADV 1MO2 SER B 3 Q03133 INSERTION
SEQADV 1MO2 SER B 284 Q03133 INSERTION
SEQADV 1MO2 SER B 285 Q03133 INSERTION
SEQADV 1MO2 VAL B 286 Q03133 INSERTION
SEQADV 1MO2 ASP B 287 Q03133 INSERTION
SEQADV 1MO2 LYS B 288 Q03133 INSERTION
SEQADV 1MO2 LEU B 289 Q03133 INSERTION
SEQADV 1MO2 ALA B 290 Q03133 INSERTION
SEQADV 1MO2 ALA B 291 Q03133 INSERTION
SEQADV 1MO2 ALA B 292 Q03133 INSERTION
SEQADV 1MO2 LEU B 293 Q03133 INSERTION
SEQADV 1MO2 GLU B 294 Q03133 INSERTION
SEQRES 1 A 294 MET ALA SER GLN LEU ASP SER GLY THR PRO ALA ARG GLU
SEQRES 2 A 294 ALA SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY
SEQRES 3 A 294 VAL SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA
SEQRES 4 A 294 GLY LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP
SEQRES 5 A 294 GLY PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO
SEQRES 6 A 294 GLY GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA
SEQRES 7 A 294 ILE SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA
SEQRES 8 A 294 LEU ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO
SEQRES 9 A 294 GLY TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA
SEQRES 10 A 294 ALA VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR
SEQRES 11 A 294 GLN GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA
SEQRES 12 A 294 GLY ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU
SEQRES 13 A 294 ASP ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP
SEQRES 14 A 294 VAL TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP
SEQRES 15 A 294 LEU GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR
SEQRES 16 A 294 VAL ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA
SEQRES 17 A 294 TYR ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR
SEQRES 18 A 294 GLY LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET
SEQRES 19 A 294 GLY PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO
SEQRES 20 A 294 PHE GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE
SEQRES 21 A 294 THR MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS
SEQRES 22 A 294 ILE ASP ALA TRP LEU GLY GLY GLY ASN SER SER SER VAL
SEQRES 23 A 294 ASP LYS LEU ALA ALA ALA LEU GLU
SEQRES 1 B 294 MET ALA SER GLN LEU ASP SER GLY THR PRO ALA ARG GLU
SEQRES 2 B 294 ALA SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY
SEQRES 3 B 294 VAL SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA
SEQRES 4 B 294 GLY LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP
SEQRES 5 B 294 GLY PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO
SEQRES 6 B 294 GLY GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA
SEQRES 7 B 294 ILE SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA
SEQRES 8 B 294 LEU ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO
SEQRES 9 B 294 GLY TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA
SEQRES 10 B 294 ALA VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR
SEQRES 11 B 294 GLN GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA
SEQRES 12 B 294 GLY ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU
SEQRES 13 B 294 ASP ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP
SEQRES 14 B 294 VAL TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP
SEQRES 15 B 294 LEU GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR
SEQRES 16 B 294 VAL ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA
SEQRES 17 B 294 TYR ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR
SEQRES 18 B 294 GLY LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET
SEQRES 19 B 294 GLY PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO
SEQRES 20 B 294 PHE GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE
SEQRES 21 B 294 THR MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS
SEQRES 22 B 294 ILE ASP ALA TRP LEU GLY GLY GLY ASN SER SER SER VAL
SEQRES 23 B 294 ASP LYS LEU ALA ALA ALA LEU GLU
FORMUL 3 HOH *56(H2 O1)
HELIX 1 1 GLY A 29 ASP A 43 1 15
HELIX 2 2 GLY A 81 GLU A 84 5 4
HELIX 3 3 PHE A 85 ARG A 93 1 9
HELIX 4 4 SER A 115 THR A 130 1 16
HELIX 5 5 GLY A 144 GLY A 159 1 16
HELIX 6 6 GLY A 174 ALA A 188 1 15
HELIX 7 7 ASP A 199 TRP A 216 1 18
HELIX 8 8 HIS A 266 GLY A 279 1 14
HELIX 9 9 GLY B 29 ASP B 43 1 15
HELIX 10 10 GLY B 81 GLU B 84 5 4
HELIX 11 11 PHE B 85 ARG B 93 1 9
HELIX 12 12 SER B 115 THR B 130 1 16
HELIX 13 13 GLY B 144 ARG B 158 1 15
HELIX 14 14 GLY B 174 THR B 187 1 14
HELIX 15 15 ALA B 188 LEU B 190 5 3
HELIX 16 16 ASP B 199 GLN B 215 1 17
HELIX 17 17 HIS B 266 GLY B 280 1 15
SHEET 1 A 2 HIS A 47 PHE A 48 0
SHEET 2 A 2 LEU A 112 PRO A 113 1 O LEU A 112 N PHE A 48
SHEET 1 B 7 VAL A 59 ALA A 62 0
SHEET 2 B 7 VAL A 98 VAL A 101 -1 O VAL A 98 N ALA A 62
SHEET 3 B 7 THR A 69 CYS A 73 1 N CYS A 72 O VAL A 101
SHEET 4 B 7 PHE A 136 GLY A 140 1 O ALA A 139 N CYS A 73
SHEET 5 B 7 GLY A 164 ASP A 169 1 O ILE A 168 N GLY A 140
SHEET 6 B 7 THR A 225 SER A 229 1 O VAL A 228 N LEU A 167
SHEET 7 B 7 ASP A 251 ALA A 254 1 O VAL A 253 N SER A 229
SHEET 1 C 2 HIS B 47 PHE B 48 0
SHEET 2 C 2 LEU B 112 PRO B 113 1 O LEU B 112 N PHE B 48
SHEET 1 D 7 VAL B 59 ALA B 62 0
SHEET 2 D 7 VAL B 98 VAL B 101 -1 O VAL B 98 N ALA B 62
SHEET 3 D 7 THR B 69 CYS B 73 1 N CYS B 72 O VAL B 101
SHEET 4 D 7 PHE B 136 GLY B 140 1 O VAL B 137 N ILE B 71
SHEET 5 D 7 GLY B 164 LEU B 167 1 O VAL B 166 N GLY B 140
SHEET 6 D 7 THR B 225 SER B 229 1 O VAL B 228 N LEU B 167
SHEET 7 D 7 ASP B 251 ALA B 254 1 O ASP B 251 N LEU B 227
CRYST1 80.500 102.500 156.500 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 0.012422 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009756 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006390 0.00000
TER 1888 GLY A 280
TER 3776 GLY B 280
MASTER 556 0 0 17 18 0 0 6 3830 2 0 46
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