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HEADER HYDROLASE 01-FEB-08 3C5W
TITLE COMPLEX BETWEEN PP2A-SPECIFIC METHYLESTERASE PME-1 AND PP2A
TITLE 2 CORE ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PP2A A SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PP2A C SUBUNIT;
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PP2A-SPECIFIC METHYLESTERASE PME-1;
COMPND 11 CHAIN: P;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS METHYLESTERASE, PHOSPHATASE, PP2A, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XING,Z.LI,Y.CHEN,J.STOCK,P.D.JEFFREY,Y.SHI
REVDAT 1 15-APR-08 3C5W 0
JRNL AUTH Y.XING,Z.LI,Y.CHEN,J.STOCK,P.D.JEFFREY,Y.SHI
JRNL TITL STRUCTURAL MECHANISM OF DEMETHYLATION AND
JRNL TITL 2 INACTIVATION OF PROTEIN PHOSPHATASE 2A
JRNL REF CELL(CAMBRIDGE,MASS.) V. 133 154 2008
JRNL REFN ASTM CELLB5 US ISSN 0092-8674
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0038
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 19235
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1018
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1356
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 6504
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.32000
REMARK 3 B22 (A**2) : 1.39000
REMARK 3 B33 (A**2) : 0.93000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.39000
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): 0.438
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.325
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.630
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6579 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8922 ; 1.087 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 811 ; 5.123 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 297 ;39.029 ;24.276
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1142 ;18.005 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;16.990 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1005 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4950 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3244 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4503 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 235 ; 0.130 ; 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): 62 ; 0.154 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.155 ; 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): 4175 ; 0.249 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6557 ; 0.445 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2730 ; 0.633 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2365 ; 1.049 ; 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 : 5
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 9 A 46
REMARK 3 ORIGIN FOR THE GROUP (A): -35.9461 2.1780 42.6351
REMARK 3 T TENSOR
REMARK 3 T11: .3270 T22: .4444
REMARK 3 T33: .1794 T12: .0837
REMARK 3 T13: .0498 T23: -.0687
REMARK 3 L TENSOR
REMARK 3 L11: 11.0328 L22: 6.9677
REMARK 3 L33: 6.9044 L12: -2.4129
REMARK 3 L13: -2.1094 L23: .4251
REMARK 3 S TENSOR
REMARK 3 S11: .3782 S12: .0349 S13: -.1889
REMARK 3 S21: .2988 S22: -.2210 S23: .9352
REMARK 3 S31: .9379 S32: -.2054 S33: -.1573
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 402 A 454
REMARK 3 ORIGIN FOR THE GROUP (A): -34.4704 2.9924 28.3509
REMARK 3 T TENSOR
REMARK 3 T11: -.0857 T22: -.0594
REMARK 3 T33: .3068 T12: -.0145
REMARK 3 T13: -.0566 T23: .0778
REMARK 3 L TENSOR
REMARK 3 L11: 10.5488 L22: 1.0825
REMARK 3 L33: 7.2277 L12: -2.0080
REMARK 3 L13: -4.4543 L23: 1.7018
REMARK 3 S TENSOR
REMARK 3 S11: -.5512 S12: -.7235 S13: .7518
REMARK 3 S21: -.2593 S22: .3857 S23: .9387
REMARK 3 S31: -.4504 S32: -.3627 S33: .1655
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 455 A 589
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0487 -8.7261 7.2781
REMARK 3 T TENSOR
REMARK 3 T11: .0515 T22: .3031
REMARK 3 T33: -.1483 T12: -.2975
REMARK 3 T13: -.0379 T23: .0178
REMARK 3 L TENSOR
REMARK 3 L11: 4.4106 L22: 1.6241
REMARK 3 L33: 2.2941 L12: .3187
REMARK 3 L13: -2.6385 L23: -.6808
REMARK 3 S TENSOR
REMARK 3 S11: -.3509 S12: 1.2696 S13: -.3582
REMARK 3 S21: -.5932 S22: .1747 S23: .5516
REMARK 3 S31: .2963 S32: -.7657 S33: .1763
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 : C 6 C 293
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5805 -2.8999 20.9402
REMARK 3 T TENSOR
REMARK 3 T11: -.2067 T22: -.2771
REMARK 3 T33: -.2787 T12: -.0494
REMARK 3 T13: .0212 T23: -.0078
REMARK 3 L TENSOR
REMARK 3 L11: 3.1165 L22: 1.8864
REMARK 3 L33: 2.4860 L12: .4031
REMARK 3 L13: -.1517 L23: -.2950
REMARK 3 S TENSOR
REMARK 3 S11: -.0511 S12: .2420 S13: -.1052
REMARK 3 S21: -.0734 S22: .0574 S23: -.0669
REMARK 3 S31: .3041 S32: .0489 S33: -.0063
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 39 P 376
REMARK 3 RESIDUE RANGE : C 304 C 309
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6125 1.2218 52.5886
REMARK 3 T TENSOR
REMARK 3 T11: -.1149 T22: -.0634
REMARK 3 T33: -.0996 T12: -.0943
REMARK 3 T13: -.0792 T23: -.0248
REMARK 3 L TENSOR
REMARK 3 L11: 2.3233 L22: 2.6104
REMARK 3 L33: 3.7488 L12: -.9654
REMARK 3 L13: .7763 L23: -1.8643
REMARK 3 S TENSOR
REMARK 3 S11: -.1714 S12: -.1943 S13: .0232
REMARK 3 S21: .4565 S22: -.1691 S23: -.4014
REMARK 3 S31: -.3589 S32: .4543 S33: .3405
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3C5W COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB046380.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : SI(111)
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 : 20623
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 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) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40000
REMARK 200 FOR SHELL : NULL
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: PP2A A SUBUNIT, PP2A C SUBUNIT, PME-1 MONOMER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V PEG3350, 100 MM AMMONIUM
REMARK 280 CITRATE, AND 5 MM DTT, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 1/2+X,1/2+Y,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 64.64600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.41950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.64600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.41950
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4920 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, P
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 HIS A 7
REMARK 465 MET A 8
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 GLU C 3
REMARK 465 LYS C 4
REMARK 465 VAL C 5
REMARK 465 ARG C 294
REMARK 465 ARG C 295
REMARK 465 GLY C 296
REMARK 465 GLU C 297
REMARK 465 PRO C 298
REMARK 465 HIS C 299
REMARK 465 VAL C 300
REMARK 465 THR C 301
REMARK 465 ARG C 302
REMARK 465 ARG C 303
REMARK 465 GLY P 35
REMARK 465 SER P 36
REMARK 465 HIS P 37
REMARK 465 MET P 38
REMARK 465 GLU P 239
REMARK 465 GLY P 240
REMARK 465 GLY P 377
REMARK 465 GLY P 378
REMARK 465 PHE P 379
REMARK 465 GLN P 380
REMARK 465 CYS P 381
REMARK 465 VAL P 382
REMARK 465 PHE P 383
REMARK 465 PRO P 384
REMARK 465 GLY P 385
REMARK 465 CYS P 386
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 LYS A 34 -14.48 -159.53
REMARK 500 LEU A 42 80.86 -168.34
REMARK 500 LEU A 404 -33.18 -148.07
REMARK 500 GLU A 441 -98.38 -65.77
REMARK 500 SER A 587 7.49 59.11
REMARK 500 ASP C 88 -113.24 -153.79
REMARK 500 TYR C 91 -64.70 -96.20
REMARK 500 ASN C 139 -158.96 -101.87
REMARK 500 GLN C 162 -45.20 -131.29
REMARK 500 ALA C 240 -131.42 -125.03
REMARK 500 HIS C 241 -31.72 78.98
REMARK 500 TYR C 267 18.76 59.43
REMARK 500 ARG C 268 -16.63 -142.78
REMARK 500 ASP C 279 -166.68 -78.63
REMARK 500 ASP C 306 53.33 -98.11
REMARK 500 ASN P 60 -118.74 -139.74
REMARK 500 ARG P 68 112.70 81.62
REMARK 500 HIS P 87 -156.95 -105.94
REMARK 500 SER P 114 -5.57 66.88
REMARK 500 TYR P 143 -72.73 -127.07
REMARK 500 ALA P 156 -115.60 39.27
REMARK 500 ARG P 201 151.88 -48.59
REMARK 500 GLU P 290 79.34 -67.37
REMARK 500 PRO P 313 48.01 -79.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C5V RELATED DB: PDB
REMARK 900 PME-1 MONOMER
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAIN A HAS 47-399 RESIDUES DELETION AND CHAIN P HAS 239-
REMARK 999 283 LOOP REPLACED BY EGK. THE PROTEIN CONSTRUCT (CHAIN P)
REMARK 999 IS A NON-CATALYTIC MUTANT WITH SER156 REPLACED BY ALA.
DBREF 3C5W A 9 46 UNP P30153 2AAA_HUMAN 9 46
DBREF 3C5W A 400 589 UNP P30153 2AAA_HUMAN 400 589
DBREF 3C5W C 1 309 UNP P67775 PP2AA_HUMAN 1 309
DBREF 3C5W P 39 238 UNP Q9Y570 PPME1_HUMAN 39 238
DBREF 3C5W P 284 386 UNP Q9Y570 PPME1_HUMAN 284 386
SEQADV 3C5W GLY A 5 UNP P30153 EXPRESSION TAG
SEQADV 3C5W SER A 6 UNP P30153 EXPRESSION TAG
SEQADV 3C5W HIS A 7 UNP P30153 EXPRESSION TAG
SEQADV 3C5W MET A 8 UNP P30153 EXPRESSION TAG
SEQADV 3C5W GLY C 0 UNP P67775 EXPRESSION TAG
SEQADV 3C5W GLY P 35 UNP Q9Y570 EXPRESSION TAG
SEQADV 3C5W SER P 36 UNP Q9Y570 EXPRESSION TAG
SEQADV 3C5W HIS P 37 UNP Q9Y570 EXPRESSION TAG
SEQADV 3C5W MET P 38 UNP Q9Y570 EXPRESSION TAG
SEQADV 3C5W ALA P 156 UNP Q9Y570 SER 156 SEE REMARK 999
SEQADV 3C5W GLU P 239 UNP Q9Y570 SEE REMARK 999
SEQADV 3C5W GLY P 240 UNP Q9Y570 SEE REMARK 999
SEQADV 3C5W LYS P 283 UNP Q9Y570 SEE REMARK 999
SEQRES 1 A 232 GLY SER HIS MET SER LEU TYR PRO ILE ALA VAL LEU ILE
SEQRES 2 A 232 ASP GLU LEU ARG ASN GLU ASP VAL GLN LEU ARG LEU ASN
SEQRES 3 A 232 SER ILE LYS LYS LEU SER THR ILE ALA LEU ALA LEU GLY
SEQRES 4 A 232 VAL GLU ARG LEU SER GLN SER LEU LEU PRO ALA ILE VAL
SEQRES 5 A 232 GLU LEU ALA GLU ASP ALA LYS TRP ARG VAL ARG LEU ALA
SEQRES 6 A 232 ILE ILE GLU TYR MET PRO LEU LEU ALA GLY GLN LEU GLY
SEQRES 7 A 232 VAL GLU PHE PHE ASP GLU LYS LEU ASN SER LEU CYS MET
SEQRES 8 A 232 ALA TRP LEU VAL ASP HIS VAL TYR ALA ILE ARG GLU ALA
SEQRES 9 A 232 ALA THR SER ASN LEU LYS LYS LEU VAL GLU LYS PHE GLY
SEQRES 10 A 232 LYS GLU TRP ALA HIS ALA THR ILE ILE PRO LYS VAL LEU
SEQRES 11 A 232 ALA MET SER GLY ASP PRO ASN TYR LEU HIS ARG MET THR
SEQRES 12 A 232 THR LEU PHE CYS ILE ASN VAL LEU SER GLU VAL CYS GLY
SEQRES 13 A 232 GLN ASP ILE THR THR LYS HIS MET LEU PRO THR VAL LEU
SEQRES 14 A 232 ARG MET ALA GLY ASP PRO VAL ALA ASN VAL ARG PHE ASN
SEQRES 15 A 232 VAL ALA LYS SER LEU GLN LYS ILE GLY PRO ILE LEU ASP
SEQRES 16 A 232 ASN SER THR LEU GLN SER GLU VAL LYS PRO ILE LEU GLU
SEQRES 17 A 232 LYS LEU THR GLN ASP GLN ASP VAL ASP VAL LYS TYR PHE
SEQRES 18 A 232 ALA GLN GLU ALA LEU THR VAL LEU SER LEU ALA
SEQRES 1 C 310 GLY MET ASP GLU LYS VAL PHE THR LYS GLU LEU ASP GLN
SEQRES 2 C 310 TRP ILE GLU GLN LEU ASN GLU CYS LYS GLN LEU SER GLU
SEQRES 3 C 310 SER GLN VAL LYS SER LEU CYS GLU LYS ALA LYS GLU ILE
SEQRES 4 C 310 LEU THR LYS GLU SER ASN VAL GLN GLU VAL ARG CYS PRO
SEQRES 5 C 310 VAL THR VAL CYS GLY ASP VAL HIS GLY GLN PHE HIS ASP
SEQRES 6 C 310 LEU MET GLU LEU PHE ARG ILE GLY GLY LYS SER PRO ASP
SEQRES 7 C 310 THR ASN TYR LEU PHE MET GLY ASP TYR VAL ASP ARG GLY
SEQRES 8 C 310 TYR TYR SER VAL GLU THR VAL THR LEU LEU VAL ALA LEU
SEQRES 9 C 310 LYS VAL ARG TYR ARG GLU ARG ILE THR ILE LEU ARG GLY
SEQRES 10 C 310 ASN HIS GLU SER ARG GLN ILE THR GLN VAL TYR GLY PHE
SEQRES 11 C 310 TYR ASP GLU CYS LEU ARG LYS TYR GLY ASN ALA ASN VAL
SEQRES 12 C 310 TRP LYS TYR PHE THR ASP LEU PHE ASP TYR LEU PRO LEU
SEQRES 13 C 310 THR ALA LEU VAL ASP GLY GLN ILE PHE CYS LEU HIS GLY
SEQRES 14 C 310 GLY LEU SER PRO SER ILE ASP THR LEU ASP HIS ILE ARG
SEQRES 15 C 310 ALA LEU ASP ARG LEU GLN GLU VAL PRO HIS GLU GLY PRO
SEQRES 16 C 310 MET CYS ASP LEU LEU TRP SER ASP PRO ASP ASP ARG GLY
SEQRES 17 C 310 GLY TRP GLY ILE SER PRO ARG GLY ALA GLY TYR THR PHE
SEQRES 18 C 310 GLY GLN ASP ILE SER GLU THR PHE ASN HIS ALA ASN GLY
SEQRES 19 C 310 LEU THR LEU VAL SER ARG ALA HIS GLN LEU VAL MET GLU
SEQRES 20 C 310 GLY TYR ASN TRP CYS HIS ASP ARG ASN VAL VAL THR ILE
SEQRES 21 C 310 PHE SER ALA PRO ASN TYR CYS TYR ARG CYS GLY ASN GLN
SEQRES 22 C 310 ALA ALA ILE MET GLU LEU ASP ASP THR LEU LYS TYR SER
SEQRES 23 C 310 PHE LEU GLN PHE ASP PRO ALA PRO ARG ARG GLY GLU PRO
SEQRES 24 C 310 HIS VAL THR ARG ARG THR PRO ASP TYR PHE LEU
SEQRES 1 P 310 GLY SER HIS MET ARG ASP PHE SER PRO VAL PRO TRP SER
SEQRES 2 P 310 GLN TYR PHE GLU SER MET GLU ASP VAL GLU VAL GLU ASN
SEQRES 3 P 310 GLU THR GLY LYS ASP THR PHE ARG VAL TYR LYS SER GLY
SEQRES 4 P 310 SER GLU GLY PRO VAL LEU LEU LEU LEU HIS GLY GLY GLY
SEQRES 5 P 310 HIS SER ALA LEU SER TRP ALA VAL PHE THR ALA ALA ILE
SEQRES 6 P 310 ILE SER ARG VAL GLN CYS ARG ILE VAL ALA LEU ASP LEU
SEQRES 7 P 310 ARG SER HIS GLY GLU THR LYS VAL LYS ASN PRO GLU ASP
SEQRES 8 P 310 LEU SER ALA GLU THR MET ALA LYS ASP VAL GLY ASN VAL
SEQRES 9 P 310 VAL GLU ALA MET TYR GLY ASP LEU PRO PRO PRO ILE MET
SEQRES 10 P 310 LEU ILE GLY HIS ALA MET GLY GLY ALA ILE ALA VAL HIS
SEQRES 11 P 310 THR ALA SER SER ASN LEU VAL PRO SER LEU LEU GLY LEU
SEQRES 12 P 310 CYS MET ILE ASP VAL VAL GLU GLY THR ALA MET ASP ALA
SEQRES 13 P 310 LEU ASN SER MET GLN ASN PHE LEU ARG GLY ARG PRO LYS
SEQRES 14 P 310 THR PHE LYS SER LEU GLU ASN ALA ILE GLU TRP SER VAL
SEQRES 15 P 310 LYS SER GLY GLN ILE ARG ASN LEU GLU SER ALA ARG VAL
SEQRES 16 P 310 SER MET VAL GLY GLN VAL LYS GLN CYS GLU GLY LYS PRO
SEQRES 17 P 310 TYR THR TRP ARG ILE GLU LEU ALA LYS THR GLU LYS TYR
SEQRES 18 P 310 TRP ASP GLY TRP PHE ARG GLY LEU SER ASN LEU PHE LEU
SEQRES 19 P 310 SER CYS PRO ILE PRO LYS LEU LEU LEU LEU ALA GLY VAL
SEQRES 20 P 310 ASP ARG LEU ASP LYS ASP LEU THR ILE GLY GLN MET GLN
SEQRES 21 P 310 GLY LYS PHE GLN MET GLN VAL LEU PRO GLN CYS GLY HIS
SEQRES 22 P 310 ALA VAL HIS GLU ASP ALA PRO ASP LYS VAL ALA GLU ALA
SEQRES 23 P 310 VAL ALA THR PHE LEU ILE ARG HIS ARG PHE ALA GLU PRO
SEQRES 24 P 310 ILE GLY GLY PHE GLN CYS VAL PHE PRO GLY CYS
FORMUL 4 HOH *62(H2 O)
HELIX 1 1 TYR A 11 ARG A 21 1 11
HELIX 2 2 ASP A 24 LYS A 33 1 10
HELIX 3 3 LYS A 34 GLY A 43 1 10
HELIX 4 4 GLU A 45 SER A 403 1 6
HELIX 5 5 LEU A 404 ALA A 412 1 9
HELIX 6 6 LYS A 416 GLU A 425 1 10
HELIX 7 7 TYR A 426 GLY A 435 1 10
HELIX 8 8 VAL A 436 PHE A 439 5 4
HELIX 9 9 LYS A 442 LEU A 451 1 10
HELIX 10 10 VAL A 455 GLY A 474 1 20
HELIX 11 11 GLY A 474 THR A 481 1 8
HELIX 12 12 THR A 481 MET A 489 1 9
HELIX 13 13 SER A 490 ASP A 492 5 3
HELIX 14 14 ASN A 494 MET A 521 1 28
HELIX 15 15 MET A 521 MET A 528 1 8
HELIX 16 16 ALA A 529 ASP A 531 5 3
HELIX 17 17 VAL A 533 GLY A 548 1 16
HELIX 18 18 PRO A 549 LEU A 551 5 3
HELIX 19 19 ASP A 552 GLU A 559 1 8
HELIX 20 20 VAL A 560 GLN A 569 1 10
HELIX 21 21 ASP A 572 LEU A 586 1 15
HELIX 22 22 PHE C 6 ASN C 18 1 13
HELIX 23 23 SER C 24 LYS C 41 1 18
HELIX 24 24 GLN C 61 GLY C 73 1 13
HELIX 25 25 TYR C 92 TYR C 107 1 16
HELIX 26 26 SER C 120 GLY C 128 1 9
HELIX 27 27 GLY C 128 GLY C 138 1 11
HELIX 28 28 ALA C 140 ASP C 151 1 12
HELIX 29 29 THR C 176 LEU C 183 1 8
HELIX 30 30 GLY C 193 SER C 201 1 9
HELIX 31 31 GLY C 221 ASN C 232 1 12
HELIX 32 32 ASN C 264 ARG C 268 5 5
HELIX 33 33 PRO P 45 TYR P 49 5 5
HELIX 34 34 SER P 88 SER P 91 5 4
HELIX 35 35 TRP P 92 SER P 101 1 10
HELIX 36 36 SER P 127 TYR P 143 1 17
HELIX 37 37 ALA P 156 SER P 168 1 13
HELIX 38 38 VAL P 183 ARG P 199 1 17
HELIX 39 39 SER P 207 SER P 218 1 12
HELIX 40 40 ASN P 223 MET P 231 1 9
HELIX 41 41 GLU P 290 LYS P 296 5 7
HELIX 42 42 TYR P 297 ARG P 303 1 7
HELIX 43 43 GLY P 304 CYS P 312 1 9
HELIX 44 44 GLY P 322 LEU P 326 5 5
HELIX 45 45 ASP P 327 GLN P 336 1 10
HELIX 46 46 ALA P 350 ALA P 355 1 6
HELIX 47 47 ALA P 355 HIS P 370 1 16
SHEET 1 A 6 VAL C 45 VAL C 48 0
SHEET 2 A 6 THR C 156 VAL C 159 1 O LEU C 158 N VAL C 48
SHEET 3 A 6 ILE C 163 LEU C 166 -1 O CYS C 165 N ALA C 157
SHEET 4 A 6 LEU C 236 ARG C 239 1 O SER C 238 N PHE C 164
SHEET 5 A 6 VAL C 256 ILE C 259 1 O ILE C 259 N ARG C 239
SHEET 6 A 6 TYR C 248 CYS C 251 -1 N ASN C 249 O THR C 258
SHEET 1 B 5 ILE C 111 ILE C 113 0
SHEET 2 B 5 TYR C 80 PHE C 82 1 N PHE C 82 O THR C 112
SHEET 3 B 5 VAL C 52 CYS C 55 1 N CYS C 55 O LEU C 81
SHEET 4 B 5 ALA C 273 LEU C 278 -1 O MET C 276 N VAL C 54
SHEET 5 B 5 TYR C 284 PHE C 289 -1 O PHE C 289 N ALA C 273
SHEET 1 C 3 ASP C 202 PRO C 203 0
SHEET 2 C 3 TYR C 218 PHE C 220 1 O PHE C 220 N ASP C 202
SHEET 3 C 3 TRP C 209 ILE C 211 -1 N GLY C 210 O THR C 219
SHEET 1 D 8 SER P 52 GLU P 54 0
SHEET 2 D 8 VAL P 69 SER P 72 -1 O VAL P 69 N GLU P 54
SHEET 3 D 8 ARG P 106 LEU P 110 -1 O ALA P 109 N TYR P 70
SHEET 4 D 8 VAL P 78 LEU P 82 1 N LEU P 79 O ARG P 106
SHEET 5 D 8 ILE P 150 HIS P 155 1 O HIS P 155 N LEU P 82
SHEET 6 D 8 LEU P 174 ILE P 180 1 O ILE P 180 N GLY P 154
SHEET 7 D 8 LYS P 316 LEU P 320 1 O LEU P 317 N LEU P 177
SHEET 8 D 8 GLN P 340 VAL P 343 1 O GLN P 342 N LEU P 320
SHEET 1 E 2 GLU P 57 GLU P 59 0
SHEET 2 E 2 LYS P 64 THR P 66 -1 O ASP P 65 N VAL P 58
SHEET 1 F 2 VAL P 103 GLN P 104 0
SHEET 2 F 2 GLU P 374 PRO P 375 -1 O GLU P 374 N GLN P 104
SHEET 1 G 3 THR P 204 PHE P 205 0
SHEET 2 G 3 TYR P 285 TRP P 287 -1 O TYR P 285 N PHE P 205
SHEET 3 G 3 VAL P 235 GLN P 237 -1 N LYS P 236 O THR P 286
CISPEP 1 CYS C 50 PRO C 51 0 1.59
CISPEP 2 SER C 75 PRO C 76 0 6.39
CRYST1 129.292 54.839 125.146 90.00 110.87 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007734 0.000000 0.002949 0.00000
SCALE2 0.000000 0.018235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008552 0.00000
TER 1789 ALA A 589
TER 4166 LEU C 309
TER 6444 ILE P 376
MASTER 413 0 0 47 29 0 0 6 6503 3 0 66
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