HEADER HYDROLASE 11-JUL-07 2QKM
TITLE THE CRYSTAL STRUCTURE OF FISSION YEAST MRNA DECAPPING ENZYME DCP1-DCP2
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPBC3B9.21 PROTEIN;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 SYNONYM: DCP1 PROTEIN;
COMPND 5 EC: 3.6.1.30;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SPAC19A8.12 PROTEIN;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 FRAGMENT: RESIDUES 1-266;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 4896;
SOURCE 5 GENE: DCP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 13 ORGANISM_COMMON: FISSION YEAST;
SOURCE 14 ORGANISM_TAXID: 4896;
SOURCE 15 GENE: SPAC19A8.12;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 STAR;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS PROTEIN-PROTEIN COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SHE,H.SONG
REVDAT 4 30-AUG-23 2QKM 1 REMARK
REVDAT 3 13-JUL-11 2QKM 1 VERSN
REVDAT 2 24-FEB-09 2QKM 1 VERSN
REVDAT 1 15-APR-08 2QKM 0
JRNL AUTH M.SHE,C.J.DECKER,D.I.SVERGUN,A.ROUND,N.CHEN,D.MUHLRAD,
JRNL AUTH 2 R.PARKER,H.SONG
JRNL TITL STRUCTURAL BASIS OF DCP2 RECOGNITION AND ACTIVATION BY DCP1.
JRNL REF MOL.CELL V. 29 337 2008
JRNL REFN ISSN 1097-2765
JRNL PMID 18280239
JRNL DOI 10.1016/J.MOLCEL.2008.01.002
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 45695
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2373
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3331
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 154
REMARK 3 BIN FREE R VALUE : 0.3840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11704
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.02000
REMARK 3 B22 (A**2) : 0.84000
REMARK 3 B33 (A**2) : -5.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.82000
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): 0.420
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.302
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.214
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12041 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16283 ; 1.241 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1397 ; 5.590 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 613 ;37.251 ;23.915
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2150 ;18.753 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 85 ;17.630 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1767 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9090 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5473 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8081 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 451 ; 0.158 ; 0.200
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): 57 ; 0.260 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.213 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7261 ; 0.633 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11493 ; 1.131 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5446 ; 1.048 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4790 ; 1.694 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 127 4
REMARK 3 1 E 1 E 127 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1034 ; 0.35 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1034 ; 0.34 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 266 4
REMARK 3 1 F 1 F 266 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 2143 ; 0.49 ; 0.50
REMARK 3 MEDIUM THERMAL 2 B (A**2): 2143 ; 0.42 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 123 4
REMARK 3 1 G 1 G 123 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 C (A): 1026 ; 0.48 ; 0.50
REMARK 3 MEDIUM THERMAL 3 C (A**2): 1026 ; 0.33 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : D H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 1 D 233 6
REMARK 3 1 H 1 H 233 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 4 D (A): 1540 ; 0.74 ; 5.00
REMARK 3 LOOSE THERMAL 4 D (A**2): 1540 ; 2.13 ; 10.00
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 1 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3221 -45.6183 15.7576
REMARK 3 T TENSOR
REMARK 3 T11: -0.0676 T22: -0.0576
REMARK 3 T33: -0.1058 T12: 0.0400
REMARK 3 T13: 0.0129 T23: -0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 2.1041 L22: 3.6956
REMARK 3 L33: 2.1038 L12: 0.0165
REMARK 3 L13: -0.2075 L23: 0.3156
REMARK 3 S TENSOR
REMARK 3 S11: 0.0883 S12: -0.0715 S13: -0.0774
REMARK 3 S21: -0.0469 S22: 0.0245 S23: -0.5338
REMARK 3 S31: 0.1516 S32: 0.2153 S33: -0.1128
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 : B 1 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9105 -34.4805 39.9733
REMARK 3 T TENSOR
REMARK 3 T11: -0.0802 T22: -0.0748
REMARK 3 T33: -0.1012 T12: -0.0193
REMARK 3 T13: 0.0317 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 0.6054 L22: 0.8568
REMARK 3 L33: 2.9942 L12: -0.1781
REMARK 3 L13: -0.0488 L23: -0.4751
REMARK 3 S TENSOR
REMARK 3 S11: -0.0209 S12: -0.0080 S13: 0.0586
REMARK 3 S21: -0.0038 S22: 0.0217 S23: -0.0052
REMARK 3 S31: 0.0533 S32: -0.2053 S33: -0.0009
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 : C 1 C 123
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2315 -41.0874 -8.3299
REMARK 3 T TENSOR
REMARK 3 T11: 0.0718 T22: -0.0895
REMARK 3 T33: -0.2625 T12: 0.0487
REMARK 3 T13: -0.0052 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 4.0392 L22: 1.7242
REMARK 3 L33: 2.8308 L12: -0.5330
REMARK 3 L13: -0.1862 L23: 1.0951
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: 0.1571 S13: 0.0922
REMARK 3 S21: -0.3047 S22: 0.0393 S23: -0.0676
REMARK 3 S31: -0.1886 S32: -0.0748 S33: -0.0471
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 : D 1 D 233
REMARK 3 ORIGIN FOR THE GROUP (A): -29.6247 -34.8332 26.9877
REMARK 3 T TENSOR
REMARK 3 T11: -0.2834 T22: 0.1906
REMARK 3 T33: 0.0271 T12: -0.0036
REMARK 3 T13: -0.0595 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 1.2156 L22: 0.7079
REMARK 3 L33: 5.5416 L12: -0.1181
REMARK 3 L13: -2.0489 L23: 0.0891
REMARK 3 S TENSOR
REMARK 3 S11: 0.0653 S12: 0.2245 S13: -0.0857
REMARK 3 S21: -0.1395 S22: -0.1231 S23: 0.4551
REMARK 3 S31: 0.0565 S32: -0.9584 S33: 0.0578
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 : E 1 E 127
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4874 12.5650 12.1639
REMARK 3 T TENSOR
REMARK 3 T11: -0.0095 T22: -0.0585
REMARK 3 T33: -0.1167 T12: 0.0600
REMARK 3 T13: -0.0295 T23: 0.0764
REMARK 3 L TENSOR
REMARK 3 L11: 1.9114 L22: 4.1071
REMARK 3 L33: 2.3016 L12: 0.3700
REMARK 3 L13: -0.0580 L23: -0.6140
REMARK 3 S TENSOR
REMARK 3 S11: 0.0308 S12: 0.0349 S13: 0.2379
REMARK 3 S21: -0.2692 S22: 0.0677 S23: 0.4294
REMARK 3 S31: -0.0262 S32: -0.2476 S33: -0.0985
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 : F 1 F 266
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8201 1.1391 40.1211
REMARK 3 T TENSOR
REMARK 3 T11: 0.0493 T22: -0.0856
REMARK 3 T33: -0.1331 T12: -0.0025
REMARK 3 T13: 0.0008 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 0.6520 L22: 0.9297
REMARK 3 L33: 2.6079 L12: -0.2225
REMARK 3 L13: -0.4197 L23: 0.3688
REMARK 3 S TENSOR
REMARK 3 S11: -0.0408 S12: -0.0598 S13: -0.0254
REMARK 3 S21: 0.1162 S22: 0.0402 S23: 0.0135
REMARK 3 S31: 0.0178 S32: 0.1257 S33: 0.0006
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 : G 1 G 123
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7470 7.3774 -6.9353
REMARK 3 T TENSOR
REMARK 3 T11: 0.0977 T22: -0.0426
REMARK 3 T33: -0.2488 T12: 0.0867
REMARK 3 T13: 0.0956 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 3.7504 L22: 1.2105
REMARK 3 L33: 3.0457 L12: -0.2661
REMARK 3 L13: 0.3270 L23: -1.2163
REMARK 3 S TENSOR
REMARK 3 S11: -0.0690 S12: 0.0345 S13: -0.2065
REMARK 3 S21: -0.3641 S22: -0.0024 S23: 0.0697
REMARK 3 S31: 0.2676 S32: 0.1845 S33: 0.0714
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 : H 1 H 235
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2854 1.4860 32.6773
REMARK 3 T TENSOR
REMARK 3 T11: -0.2142 T22: 0.1060
REMARK 3 T33: -0.0878 T12: 0.0033
REMARK 3 T13: -0.0185 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 1.5397 L22: 0.8072
REMARK 3 L33: 5.8546 L12: -0.7189
REMARK 3 L13: 0.8494 L23: 0.1288
REMARK 3 S TENSOR
REMARK 3 S11: -0.0446 S12: -0.2399 S13: 0.2673
REMARK 3 S21: -0.0154 S22: 0.0506 S23: -0.3906
REMARK 3 S31: 0.1657 S32: 0.6235 S33: -0.0060
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
REMARK 4
REMARK 4 2QKM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1000043716.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48226
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 90.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.32300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRIES 2A6T, 2QKL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% ETHYLENE GLYCOL, 100 MM HEPES PH
REMARK 280 7.0, 11.6% MPD, 4.4% PEG 4000 AND 10 MM ATP, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 285K
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 80.72150
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 2010 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 2140 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 VAL A 40
REMARK 465 GLY A 41
REMARK 465 SER A 42
REMARK 465 GLN A 43
REMARK 465 SER C 124
REMARK 465 LEU C 125
REMARK 465 LEU C 126
REMARK 465 ARG C 127
REMARK 465 PRO D 73
REMARK 465 LEU D 74
REMARK 465 LEU D 75
REMARK 465 LYS D 115
REMARK 465 GLY D 116
REMARK 465 TRP D 117
REMARK 465 LYS D 118
REMARK 465 ALA D 119
REMARK 465 SER D 120
REMARK 465 SER D 121
REMARK 465 GLY D 122
REMARK 465 THR D 189
REMARK 465 ARG D 190
REMARK 465 LYS D 191
REMARK 465 GLU D 192
REMARK 465 ILE D 193
REMARK 465 SER D 194
REMARK 465 LYS D 195
REMARK 465 PHE D 207
REMARK 465 LYS D 208
REMARK 465 LYS D 209
REMARK 465 ASN D 210
REMARK 465 LYS D 211
REMARK 465 PRO D 212
REMARK 465 GLN D 213
REMARK 465 THR D 214
REMARK 465 MET D 215
REMARK 465 LYS D 216
REMARK 465 ASN D 217
REMARK 465 LYS D 218
REMARK 465 PHE D 219
REMARK 465 LYS D 234
REMARK 465 LYS D 235
REMARK 465 ARG D 236
REMARK 465 ASN D 237
REMARK 465 ILE D 238
REMARK 465 ALA D 239
REMARK 465 ASN D 240
REMARK 465 ASN D 241
REMARK 465 THR D 242
REMARK 465 THR D 243
REMARK 465 LYS D 244
REMARK 465 GLU D 245
REMARK 465 LYS D 246
REMARK 465 ASN D 247
REMARK 465 ILE D 248
REMARK 465 SER D 249
REMARK 465 VAL D 250
REMARK 465 ASP D 251
REMARK 465 VAL D 252
REMARK 465 ASP D 253
REMARK 465 ALA D 254
REMARK 465 ASP D 255
REMARK 465 ALA D 256
REMARK 465 SER D 257
REMARK 465 SER D 258
REMARK 465 GLN D 259
REMARK 465 LEU D 260
REMARK 465 LEU D 261
REMARK 465 SER D 262
REMARK 465 LEU D 263
REMARK 465 LEU D 264
REMARK 465 LYS D 265
REMARK 465 SER D 266
REMARK 465 VAL E 40
REMARK 465 GLY E 41
REMARK 465 SER E 42
REMARK 465 GLN E 43
REMARK 465 LYS F 211
REMARK 465 PRO F 212
REMARK 465 GLN F 213
REMARK 465 THR F 214
REMARK 465 PRO H 73
REMARK 465 LEU H 74
REMARK 465 LEU H 75
REMARK 465 TRP H 76
REMARK 465 LYS H 115
REMARK 465 GLY H 116
REMARK 465 TRP H 117
REMARK 465 LYS H 118
REMARK 465 ALA H 119
REMARK 465 SER H 120
REMARK 465 SER H 121
REMARK 465 ILE H 176
REMARK 465 PRO H 177
REMARK 465 GLY H 178
REMARK 465 ILE H 179
REMARK 465 SER H 180
REMARK 465 LEU H 181
REMARK 465 ASP H 182
REMARK 465 THR H 183
REMARK 465 ARG H 184
REMARK 465 PHE H 185
REMARK 465 GLU H 186
REMARK 465 SER H 187
REMARK 465 ARG H 188
REMARK 465 THR H 189
REMARK 465 ARG H 190
REMARK 465 LYS H 191
REMARK 465 GLU H 192
REMARK 465 ILE H 193
REMARK 465 SER H 194
REMARK 465 LYS H 195
REMARK 465 PHE H 207
REMARK 465 LYS H 208
REMARK 465 LYS H 209
REMARK 465 ASN H 210
REMARK 465 LYS H 211
REMARK 465 PRO H 212
REMARK 465 GLN H 213
REMARK 465 THR H 214
REMARK 465 MET H 215
REMARK 465 LYS H 216
REMARK 465 ASN H 217
REMARK 465 LYS H 218
REMARK 465 PHE H 219
REMARK 465 TYR H 220
REMARK 465 ARG H 236
REMARK 465 ASN H 237
REMARK 465 ILE H 238
REMARK 465 ALA H 239
REMARK 465 ASN H 240
REMARK 465 ASN H 241
REMARK 465 THR H 242
REMARK 465 THR H 243
REMARK 465 LYS H 244
REMARK 465 GLU H 245
REMARK 465 LYS H 246
REMARK 465 ASN H 247
REMARK 465 ILE H 248
REMARK 465 SER H 249
REMARK 465 VAL H 250
REMARK 465 ASP H 251
REMARK 465 VAL H 252
REMARK 465 ASP H 253
REMARK 465 ALA H 254
REMARK 465 ASP H 255
REMARK 465 ALA H 256
REMARK 465 SER H 257
REMARK 465 SER H 258
REMARK 465 GLN H 259
REMARK 465 LEU H 260
REMARK 465 LEU H 261
REMARK 465 SER H 262
REMARK 465 LEU H 263
REMARK 465 LEU H 264
REMARK 465 LYS H 265
REMARK 465 SER H 266
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 LYS H 235 C LYS H 235 O 0.373
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 ASN A 100 22.31 -72.49
REMARK 500 LEU A 126 -89.42 -97.73
REMARK 500 ASN B 53 87.33 -153.72
REMARK 500 LYS B 118 -15.09 131.95
REMARK 500 ALA B 119 -24.54 66.61
REMARK 500 TRP B 123 148.83 -35.34
REMARK 500 ASP B 133 -7.77 64.37
REMARK 500 LYS B 209 -59.12 -20.38
REMARK 500 MET B 215 47.66 -85.35
REMARK 500 TYR B 220 -108.87 -83.02
REMARK 500 MET B 221 54.84 -96.01
REMARK 500 THR B 242 -49.05 -151.73
REMARK 500 THR B 243 -105.20 -144.01
REMARK 500 LYS B 244 105.37 -172.15
REMARK 500 GLU B 245 -125.85 12.58
REMARK 500 LYS B 246 -67.20 62.91
REMARK 500 ALA B 254 -127.08 -99.72
REMARK 500 SER C 42 -177.53 60.54
REMARK 500 ARG C 61 1.71 89.68
REMARK 500 GLU C 75 85.93 -64.30
REMARK 500 ASN C 76 -177.71 -69.59
REMARK 500 ASP C 91 73.43 30.08
REMARK 500 ARG C 92 0.56 58.07
REMARK 500 ASN C 100 36.69 -70.82
REMARK 500 SER D 2 -43.39 -151.59
REMARK 500 PHE D 19 -50.72 -134.42
REMARK 500 LEU D 21 -31.62 66.35
REMARK 500 GLU D 27 38.57 -88.36
REMARK 500 SER D 29 32.55 -150.56
REMARK 500 ALA D 70 40.31 -80.77
REMARK 500 HIS D 71 -32.73 -136.46
REMARK 500 MET D 106 -60.86 160.19
REMARK 500 LYS D 127 -164.49 -126.43
REMARK 500 LYS D 132 -72.86 -6.45
REMARK 500 ASP D 133 64.74 -150.26
REMARK 500 GLU D 134 -169.78 -73.25
REMARK 500 ILE D 179 79.24 -104.15
REMARK 500 SER D 180 -46.05 51.76
REMARK 500 LEU D 181 -2.98 79.97
REMARK 500 ASP D 182 43.87 -147.02
REMARK 500 GLU D 186 -109.02 -157.27
REMARK 500 SER D 187 19.45 52.04
REMARK 500 GLU D 197 156.64 63.58
REMARK 500 PRO D 205 -58.41 -20.70
REMARK 500 GLN E 37 -150.35 -128.76
REMARK 500 SER E 85 -5.58 -55.12
REMARK 500 GLN E 101 10.42 50.40
REMARK 500 LEU E 126 -131.02 -108.11
REMARK 500 LEU F 61 -71.25 -10.78
REMARK 500 LYS F 77 2.57 -69.27
REMARK 500
REMARK 500 THIS ENTRY HAS 97 RAMACHANDRAN OUTLIERS.
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 ATP B 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP F 267
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QKL RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH PB
REMARK 900 RELATED ID: 2A6T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S.POMBE MRNA DECAPPING ENZYME DCP2P
DBREF 2QKM A 1 127 UNP Q9P805 Q9P805_SCHPO 1 127
DBREF 2QKM B 1 266 UNP O13828 O13828_SCHPO 1 266
DBREF 2QKM C 1 127 UNP Q9P805 Q9P805_SCHPO 1 127
DBREF 2QKM D 1 266 UNP O13828 O13828_SCHPO 1 266
DBREF 2QKM E 1 127 UNP Q9P805 Q9P805_SCHPO 1 127
DBREF 2QKM F 1 266 UNP O13828 O13828_SCHPO 1 266
DBREF 2QKM G 1 127 UNP Q9P805 Q9P805_SCHPO 1 127
DBREF 2QKM H 1 266 UNP O13828 O13828_SCHPO 1 266
SEQRES 1 A 127 MET GLU ASP GLU ASN ILE LEU ARG ASN ALA VAL ASN LEU
SEQRES 2 A 127 GLN VAL LEU LYS PHE HIS TYR PRO GLU ILE GLU SER ILE
SEQRES 3 A 127 ILE ASP ILE ALA SER HIS VAL ALA VAL TYR GLN PHE ASP
SEQRES 4 A 127 VAL GLY SER GLN LYS TRP LEU LYS THR SER ILE GLU GLY
SEQRES 5 A 127 THR PHE PHE LEU VAL LYS ASP GLN ARG ALA ARG VAL GLY
SEQRES 6 A 127 TYR VAL ILE LEU ASN ARG ASN SER PRO GLU ASN LEU TYR
SEQRES 7 A 127 LEU PHE ILE ASN HIS PRO SER ASN VAL HIS LEU VAL ASP
SEQRES 8 A 127 ARG TYR LEU ILE HIS ARG THR GLU ASN GLN HIS VAL VAL
SEQRES 9 A 127 GLY LEU TRP MET PHE ASP PRO ASN ASP MET SER ARG ILE
SEQRES 10 A 127 PHE ASN ILE VAL LYS GLU SER LEU LEU ARG
SEQRES 1 B 266 MET SER PHE THR ASN ALA THR PHE SER GLN VAL LEU ASP
SEQRES 2 B 266 ASP LEU SER ALA ARG PHE ILE LEU ASN LEU PRO ALA GLU
SEQRES 3 B 266 GLU GLN SER SER VAL GLU ARG LEU CYS PHE GLN ILE GLU
SEQRES 4 B 266 GLN ALA HIS TRP PHE TYR GLU ASP PHE ILE ARG ALA GLN
SEQRES 5 B 266 ASN ASP GLN LEU PRO SER LEU GLY LEU ARG VAL PHE SER
SEQRES 6 B 266 ALA LYS LEU PHE ALA HIS CYS PRO LEU LEU TRP LYS TRP
SEQRES 7 B 266 SER LYS VAL HIS GLU GLU ALA PHE ASP ASP PHE LEU ARG
SEQRES 8 B 266 TYR LYS THR ARG ILE PRO VAL ARG GLY ALA ILE MET LEU
SEQRES 9 B 266 ASP MET SER MET GLN GLN CYS VAL LEU VAL LYS GLY TRP
SEQRES 10 B 266 LYS ALA SER SER GLY TRP GLY PHE PRO LYS GLY LYS ILE
SEQRES 11 B 266 ASP LYS ASP GLU SER ASP VAL ASP CYS ALA ILE ARG GLU
SEQRES 12 B 266 VAL TYR GLU GLU THR GLY PHE ASP CYS SER SER ARG ILE
SEQRES 13 B 266 ASN PRO ASN GLU PHE ILE ASP MET THR ILE ARG GLY GLN
SEQRES 14 B 266 ASN VAL ARG LEU TYR ILE ILE PRO GLY ILE SER LEU ASP
SEQRES 15 B 266 THR ARG PHE GLU SER ARG THR ARG LYS GLU ILE SER LYS
SEQRES 16 B 266 ILE GLU TRP HIS ASN LEU MET ASP LEU PRO THR PHE LYS
SEQRES 17 B 266 LYS ASN LYS PRO GLN THR MET LYS ASN LYS PHE TYR MET
SEQRES 18 B 266 VAL ILE PRO PHE LEU ALA PRO LEU LYS LYS TRP ILE LYS
SEQRES 19 B 266 LYS ARG ASN ILE ALA ASN ASN THR THR LYS GLU LYS ASN
SEQRES 20 B 266 ILE SER VAL ASP VAL ASP ALA ASP ALA SER SER GLN LEU
SEQRES 21 B 266 LEU SER LEU LEU LYS SER
SEQRES 1 C 127 MET GLU ASP GLU ASN ILE LEU ARG ASN ALA VAL ASN LEU
SEQRES 2 C 127 GLN VAL LEU LYS PHE HIS TYR PRO GLU ILE GLU SER ILE
SEQRES 3 C 127 ILE ASP ILE ALA SER HIS VAL ALA VAL TYR GLN PHE ASP
SEQRES 4 C 127 VAL GLY SER GLN LYS TRP LEU LYS THR SER ILE GLU GLY
SEQRES 5 C 127 THR PHE PHE LEU VAL LYS ASP GLN ARG ALA ARG VAL GLY
SEQRES 6 C 127 TYR VAL ILE LEU ASN ARG ASN SER PRO GLU ASN LEU TYR
SEQRES 7 C 127 LEU PHE ILE ASN HIS PRO SER ASN VAL HIS LEU VAL ASP
SEQRES 8 C 127 ARG TYR LEU ILE HIS ARG THR GLU ASN GLN HIS VAL VAL
SEQRES 9 C 127 GLY LEU TRP MET PHE ASP PRO ASN ASP MET SER ARG ILE
SEQRES 10 C 127 PHE ASN ILE VAL LYS GLU SER LEU LEU ARG
SEQRES 1 D 266 MET SER PHE THR ASN ALA THR PHE SER GLN VAL LEU ASP
SEQRES 2 D 266 ASP LEU SER ALA ARG PHE ILE LEU ASN LEU PRO ALA GLU
SEQRES 3 D 266 GLU GLN SER SER VAL GLU ARG LEU CYS PHE GLN ILE GLU
SEQRES 4 D 266 GLN ALA HIS TRP PHE TYR GLU ASP PHE ILE ARG ALA GLN
SEQRES 5 D 266 ASN ASP GLN LEU PRO SER LEU GLY LEU ARG VAL PHE SER
SEQRES 6 D 266 ALA LYS LEU PHE ALA HIS CYS PRO LEU LEU TRP LYS TRP
SEQRES 7 D 266 SER LYS VAL HIS GLU GLU ALA PHE ASP ASP PHE LEU ARG
SEQRES 8 D 266 TYR LYS THR ARG ILE PRO VAL ARG GLY ALA ILE MET LEU
SEQRES 9 D 266 ASP MET SER MET GLN GLN CYS VAL LEU VAL LYS GLY TRP
SEQRES 10 D 266 LYS ALA SER SER GLY TRP GLY PHE PRO LYS GLY LYS ILE
SEQRES 11 D 266 ASP LYS ASP GLU SER ASP VAL ASP CYS ALA ILE ARG GLU
SEQRES 12 D 266 VAL TYR GLU GLU THR GLY PHE ASP CYS SER SER ARG ILE
SEQRES 13 D 266 ASN PRO ASN GLU PHE ILE ASP MET THR ILE ARG GLY GLN
SEQRES 14 D 266 ASN VAL ARG LEU TYR ILE ILE PRO GLY ILE SER LEU ASP
SEQRES 15 D 266 THR ARG PHE GLU SER ARG THR ARG LYS GLU ILE SER LYS
SEQRES 16 D 266 ILE GLU TRP HIS ASN LEU MET ASP LEU PRO THR PHE LYS
SEQRES 17 D 266 LYS ASN LYS PRO GLN THR MET LYS ASN LYS PHE TYR MET
SEQRES 18 D 266 VAL ILE PRO PHE LEU ALA PRO LEU LYS LYS TRP ILE LYS
SEQRES 19 D 266 LYS ARG ASN ILE ALA ASN ASN THR THR LYS GLU LYS ASN
SEQRES 20 D 266 ILE SER VAL ASP VAL ASP ALA ASP ALA SER SER GLN LEU
SEQRES 21 D 266 LEU SER LEU LEU LYS SER
SEQRES 1 E 127 MET GLU ASP GLU ASN ILE LEU ARG ASN ALA VAL ASN LEU
SEQRES 2 E 127 GLN VAL LEU LYS PHE HIS TYR PRO GLU ILE GLU SER ILE
SEQRES 3 E 127 ILE ASP ILE ALA SER HIS VAL ALA VAL TYR GLN PHE ASP
SEQRES 4 E 127 VAL GLY SER GLN LYS TRP LEU LYS THR SER ILE GLU GLY
SEQRES 5 E 127 THR PHE PHE LEU VAL LYS ASP GLN ARG ALA ARG VAL GLY
SEQRES 6 E 127 TYR VAL ILE LEU ASN ARG ASN SER PRO GLU ASN LEU TYR
SEQRES 7 E 127 LEU PHE ILE ASN HIS PRO SER ASN VAL HIS LEU VAL ASP
SEQRES 8 E 127 ARG TYR LEU ILE HIS ARG THR GLU ASN GLN HIS VAL VAL
SEQRES 9 E 127 GLY LEU TRP MET PHE ASP PRO ASN ASP MET SER ARG ILE
SEQRES 10 E 127 PHE ASN ILE VAL LYS GLU SER LEU LEU ARG
SEQRES 1 F 266 MET SER PHE THR ASN ALA THR PHE SER GLN VAL LEU ASP
SEQRES 2 F 266 ASP LEU SER ALA ARG PHE ILE LEU ASN LEU PRO ALA GLU
SEQRES 3 F 266 GLU GLN SER SER VAL GLU ARG LEU CYS PHE GLN ILE GLU
SEQRES 4 F 266 GLN ALA HIS TRP PHE TYR GLU ASP PHE ILE ARG ALA GLN
SEQRES 5 F 266 ASN ASP GLN LEU PRO SER LEU GLY LEU ARG VAL PHE SER
SEQRES 6 F 266 ALA LYS LEU PHE ALA HIS CYS PRO LEU LEU TRP LYS TRP
SEQRES 7 F 266 SER LYS VAL HIS GLU GLU ALA PHE ASP ASP PHE LEU ARG
SEQRES 8 F 266 TYR LYS THR ARG ILE PRO VAL ARG GLY ALA ILE MET LEU
SEQRES 9 F 266 ASP MET SER MET GLN GLN CYS VAL LEU VAL LYS GLY TRP
SEQRES 10 F 266 LYS ALA SER SER GLY TRP GLY PHE PRO LYS GLY LYS ILE
SEQRES 11 F 266 ASP LYS ASP GLU SER ASP VAL ASP CYS ALA ILE ARG GLU
SEQRES 12 F 266 VAL TYR GLU GLU THR GLY PHE ASP CYS SER SER ARG ILE
SEQRES 13 F 266 ASN PRO ASN GLU PHE ILE ASP MET THR ILE ARG GLY GLN
SEQRES 14 F 266 ASN VAL ARG LEU TYR ILE ILE PRO GLY ILE SER LEU ASP
SEQRES 15 F 266 THR ARG PHE GLU SER ARG THR ARG LYS GLU ILE SER LYS
SEQRES 16 F 266 ILE GLU TRP HIS ASN LEU MET ASP LEU PRO THR PHE LYS
SEQRES 17 F 266 LYS ASN LYS PRO GLN THR MET LYS ASN LYS PHE TYR MET
SEQRES 18 F 266 VAL ILE PRO PHE LEU ALA PRO LEU LYS LYS TRP ILE LYS
SEQRES 19 F 266 LYS ARG ASN ILE ALA ASN ASN THR THR LYS GLU LYS ASN
SEQRES 20 F 266 ILE SER VAL ASP VAL ASP ALA ASP ALA SER SER GLN LEU
SEQRES 21 F 266 LEU SER LEU LEU LYS SER
SEQRES 1 G 127 MET GLU ASP GLU ASN ILE LEU ARG ASN ALA VAL ASN LEU
SEQRES 2 G 127 GLN VAL LEU LYS PHE HIS TYR PRO GLU ILE GLU SER ILE
SEQRES 3 G 127 ILE ASP ILE ALA SER HIS VAL ALA VAL TYR GLN PHE ASP
SEQRES 4 G 127 VAL GLY SER GLN LYS TRP LEU LYS THR SER ILE GLU GLY
SEQRES 5 G 127 THR PHE PHE LEU VAL LYS ASP GLN ARG ALA ARG VAL GLY
SEQRES 6 G 127 TYR VAL ILE LEU ASN ARG ASN SER PRO GLU ASN LEU TYR
SEQRES 7 G 127 LEU PHE ILE ASN HIS PRO SER ASN VAL HIS LEU VAL ASP
SEQRES 8 G 127 ARG TYR LEU ILE HIS ARG THR GLU ASN GLN HIS VAL VAL
SEQRES 9 G 127 GLY LEU TRP MET PHE ASP PRO ASN ASP MET SER ARG ILE
SEQRES 10 G 127 PHE ASN ILE VAL LYS GLU SER LEU LEU ARG
SEQRES 1 H 266 MET SER PHE THR ASN ALA THR PHE SER GLN VAL LEU ASP
SEQRES 2 H 266 ASP LEU SER ALA ARG PHE ILE LEU ASN LEU PRO ALA GLU
SEQRES 3 H 266 GLU GLN SER SER VAL GLU ARG LEU CYS PHE GLN ILE GLU
SEQRES 4 H 266 GLN ALA HIS TRP PHE TYR GLU ASP PHE ILE ARG ALA GLN
SEQRES 5 H 266 ASN ASP GLN LEU PRO SER LEU GLY LEU ARG VAL PHE SER
SEQRES 6 H 266 ALA LYS LEU PHE ALA HIS CYS PRO LEU LEU TRP LYS TRP
SEQRES 7 H 266 SER LYS VAL HIS GLU GLU ALA PHE ASP ASP PHE LEU ARG
SEQRES 8 H 266 TYR LYS THR ARG ILE PRO VAL ARG GLY ALA ILE MET LEU
SEQRES 9 H 266 ASP MET SER MET GLN GLN CYS VAL LEU VAL LYS GLY TRP
SEQRES 10 H 266 LYS ALA SER SER GLY TRP GLY PHE PRO LYS GLY LYS ILE
SEQRES 11 H 266 ASP LYS ASP GLU SER ASP VAL ASP CYS ALA ILE ARG GLU
SEQRES 12 H 266 VAL TYR GLU GLU THR GLY PHE ASP CYS SER SER ARG ILE
SEQRES 13 H 266 ASN PRO ASN GLU PHE ILE ASP MET THR ILE ARG GLY GLN
SEQRES 14 H 266 ASN VAL ARG LEU TYR ILE ILE PRO GLY ILE SER LEU ASP
SEQRES 15 H 266 THR ARG PHE GLU SER ARG THR ARG LYS GLU ILE SER LYS
SEQRES 16 H 266 ILE GLU TRP HIS ASN LEU MET ASP LEU PRO THR PHE LYS
SEQRES 17 H 266 LYS ASN LYS PRO GLN THR MET LYS ASN LYS PHE TYR MET
SEQRES 18 H 266 VAL ILE PRO PHE LEU ALA PRO LEU LYS LYS TRP ILE LYS
SEQRES 19 H 266 LYS ARG ASN ILE ALA ASN ASN THR THR LYS GLU LYS ASN
SEQRES 20 H 266 ILE SER VAL ASP VAL ASP ALA ASP ALA SER SER GLN LEU
SEQRES 21 H 266 LEU SER LEU LEU LYS SER
HET ATP B 267 31
HET ATP F 267 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 9 ATP 2(C10 H16 N5 O13 P3)
FORMUL 11 HOH *108(H2 O)
HELIX 1 1 GLU A 2 TYR A 20 1 19
HELIX 2 2 HIS A 83 SER A 85 5 3
HELIX 3 3 ASP A 110 LEU A 125 1 16
HELIX 4 4 MET B 1 ASN B 5 5 5
HELIX 5 5 THR B 7 ILE B 20 1 14
HELIX 6 6 PRO B 24 SER B 29 1 6
HELIX 7 7 SER B 30 PHE B 48 1 19
HELIX 8 8 ILE B 49 ASN B 53 5 5
HELIX 9 9 GLY B 60 ALA B 70 1 11
HELIX 10 10 HIS B 71 TRP B 76 5 6
HELIX 11 11 SER B 79 LYS B 93 1 15
HELIX 12 12 SER B 135 GLY B 149 1 15
HELIX 13 13 MET B 202 LEU B 204 5 3
HELIX 14 14 VAL B 222 PRO B 224 5 3
HELIX 15 15 PHE B 225 ASN B 241 1 17
HELIX 16 16 ALA B 254 SER B 266 1 13
HELIX 17 17 MET C 1 TYR C 20 1 20
HELIX 18 18 HIS C 83 SER C 85 5 3
HELIX 19 19 ASP C 110 LYS C 122 1 13
HELIX 20 20 THR D 7 PHE D 19 1 13
HELIX 21 21 SER D 30 PHE D 48 1 19
HELIX 22 22 ILE D 49 ASN D 53 5 5
HELIX 23 23 GLY D 60 ALA D 70 1 11
HELIX 24 24 LYS D 77 VAL D 81 5 5
HELIX 25 25 GLU D 83 PHE D 89 1 7
HELIX 26 26 ASP D 136 THR D 148 1 13
HELIX 27 27 VAL D 222 ILE D 233 1 12
HELIX 28 28 GLU E 2 TYR E 20 1 19
HELIX 29 29 HIS E 83 SER E 85 5 3
HELIX 30 30 ASP E 110 LEU E 125 1 16
HELIX 31 31 THR F 7 ILE F 20 1 14
HELIX 32 32 PRO F 24 SER F 29 1 6
HELIX 33 33 SER F 30 PHE F 48 1 19
HELIX 34 34 PHE F 48 ASN F 53 1 6
HELIX 35 35 GLY F 60 ALA F 70 1 11
HELIX 36 36 HIS F 71 TRP F 76 5 6
HELIX 37 37 SER F 79 LYS F 93 1 15
HELIX 38 38 SER F 135 GLY F 149 1 15
HELIX 39 39 MET F 202 LEU F 204 5 3
HELIX 40 40 VAL F 222 THR F 242 1 21
HELIX 41 41 ALA F 254 SER F 266 1 13
HELIX 42 42 MET G 1 TYR G 20 1 20
HELIX 43 43 HIS G 83 SER G 85 5 3
HELIX 44 44 ASP G 110 VAL G 121 1 12
HELIX 45 45 PHE H 8 PHE H 19 1 12
HELIX 46 46 SER H 30 PHE H 48 1 19
HELIX 47 47 GLY H 60 PHE H 69 1 10
HELIX 48 48 GLU H 83 TYR H 92 1 10
HELIX 49 49 SER H 135 GLY H 149 1 15
HELIX 50 50 VAL H 222 PHE H 225 5 4
HELIX 51 51 LEU H 226 ILE H 233 1 8
SHEET 1 A 7 LEU A 77 PHE A 80 0
SHEET 2 A 7 VAL A 64 ASN A 70 -1 N ILE A 68 O LEU A 77
SHEET 3 A 7 LEU A 46 ASP A 59 -1 N PHE A 55 O VAL A 67
SHEET 4 A 7 ILE A 23 GLN A 37 -1 N ILE A 27 O LEU A 56
SHEET 5 A 7 VAL A 103 MET A 108 -1 O GLY A 105 N TYR A 36
SHEET 6 A 7 TYR A 93 ARG A 97 -1 N HIS A 96 O VAL A 104
SHEET 7 A 7 VAL A 87 VAL A 90 -1 N VAL A 90 O TYR A 93
SHEET 1 B 5 LYS B 127 LYS B 129 0
SHEET 2 B 5 ILE B 96 ASP B 105 -1 N ARG B 99 O GLY B 128
SHEET 3 B 5 GLN B 169 ILE B 179 1 O TYR B 174 N GLY B 100
SHEET 4 B 5 PHE B 161 ILE B 166 -1 N MET B 164 O VAL B 171
SHEET 5 B 5 VAL B 250 ASP B 251 1 O VAL B 250 N ASP B 163
SHEET 1 C 2 GLN B 110 GLY B 116 0
SHEET 2 C 2 ILE B 193 ASN B 200 -1 O LYS B 195 N LYS B 115
SHEET 1 D 7 LEU C 77 PHE C 80 0
SHEET 2 D 7 VAL C 64 ASN C 70 -1 N ILE C 68 O LEU C 77
SHEET 3 D 7 LYS C 44 ASP C 59 -1 N PHE C 55 O VAL C 67
SHEET 4 D 7 ILE C 23 ASP C 39 -1 N ASP C 28 O LEU C 56
SHEET 5 D 7 HIS C 102 MET C 108 -1 O GLY C 105 N TYR C 36
SHEET 6 D 7 TYR C 93 THR C 98 -1 N HIS C 96 O VAL C 104
SHEET 7 D 7 VAL C 87 VAL C 90 -1 N HIS C 88 O ILE C 95
SHEET 1 E 3 VAL D 98 MET D 103 0
SHEET 2 E 3 GLN D 169 ILE D 176 1 O ILE D 176 N ILE D 102
SHEET 3 E 3 MET D 164 ILE D 166 -1 N MET D 164 O VAL D 171
SHEET 1 F 2 GLN D 110 VAL D 112 0
SHEET 2 F 2 TRP D 198 ASN D 200 -1 O HIS D 199 N CYS D 111
SHEET 1 G 7 LEU E 77 PHE E 80 0
SHEET 2 G 7 VAL E 64 ASN E 70 -1 N ILE E 68 O LEU E 77
SHEET 3 G 7 LEU E 46 ASP E 59 -1 N VAL E 57 O GLY E 65
SHEET 4 G 7 ILE E 23 GLN E 37 -1 N ASP E 28 O LEU E 56
SHEET 5 G 7 VAL E 103 MET E 108 -1 O GLY E 105 N TYR E 36
SHEET 6 G 7 TYR E 93 ARG E 97 -1 N HIS E 96 O VAL E 104
SHEET 7 G 7 VAL E 87 VAL E 90 -1 N VAL E 90 O TYR E 93
SHEET 1 H 5 LYS F 127 LYS F 129 0
SHEET 2 H 5 ILE F 96 MET F 103 -1 N ARG F 99 O GLY F 128
SHEET 3 H 5 GLN F 169 ILE F 176 1 O TYR F 174 N GLY F 100
SHEET 4 H 5 PHE F 161 ILE F 166 -1 N ILE F 162 O LEU F 173
SHEET 5 H 5 VAL F 250 ASP F 251 1 O VAL F 250 N ASP F 163
SHEET 1 I 2 GLN F 110 LYS F 115 0
SHEET 2 I 2 LYS F 195 ASN F 200 -1 O HIS F 199 N CYS F 111
SHEET 1 J 7 LEU G 77 PHE G 80 0
SHEET 2 J 7 VAL G 64 ASN G 70 -1 N ILE G 68 O LEU G 77
SHEET 3 J 7 LYS G 44 LYS G 58 -1 N PHE G 55 O VAL G 67
SHEET 4 J 7 SER G 25 ASP G 39 -1 N GLN G 37 O LEU G 46
SHEET 5 J 7 VAL G 103 MET G 108 -1 O GLY G 105 N TYR G 36
SHEET 6 J 7 TYR G 93 ARG G 97 -1 N HIS G 96 O VAL G 104
SHEET 7 J 7 VAL G 87 VAL G 90 -1 N HIS G 88 O ILE G 95
SHEET 1 K 4 LYS H 127 LYS H 129 0
SHEET 2 K 4 VAL H 98 ALA H 101 -1 N ARG H 99 O GLY H 128
SHEET 3 K 4 GLN H 169 TYR H 174 1 O TYR H 174 N GLY H 100
SHEET 4 K 4 PHE H 161 ILE H 166 -1 N ILE H 166 O GLN H 169
SHEET 1 L 2 GLN H 110 VAL H 112 0
SHEET 2 L 2 TRP H 198 ASN H 200 -1 O HIS H 199 N CYS H 111
SITE 1 AC1 5 SER B 120 SER B 121 GLY B 122 ARG B 167
SITE 2 AC1 5 TYR B 220
SITE 1 AC2 7 SER F 120 SER F 121 GLY F 122 LYS F 129
SITE 2 AC2 7 ARG F 167 GLN F 169 TYR F 220
CRYST1 68.289 161.443 91.386 90.00 97.49 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014644 0.000000 0.001925 0.00000
SCALE2 0.000000 0.006194 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011037 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
