HEADER HYDROLASE 22-APR-09 2WGP
TITLE CRYSTAL STRUCTURE OF HUMAN DUAL SPECIFICITY PHOSPHATASE 14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY PROTEIN PHOSPHATASE 14;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2-191;
COMPND 5 SYNONYM: DUAL SPECIFICITY PHOSPHATASE 14, MITOGEN-ACTIVATED PROTEIN
COMPND 6 KINASE PHOSPHATASE 6, MKP-1-LIKE PROTEIN TYROSINE PHOSPHATASE, MAP
COMPND 7 KINASE PHOSPHATASE 6, MKP-6, MKP-L;
COMPND 8 EC: 3.1.3.48, 3.1.3.16;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJT92
KEYWDS MKP6, DUSP14, HYDROLASE, PROTEIN PHOSPHATASE, DUAL SPECIFICITY
KEYWDS 2 PHOSPHATASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.T.LOUNTOS,J.E.TROPEA,S.CHERRY,D.S.WAUGH
REVDAT 3 13-DEC-23 2WGP 1 REMARK
REVDAT 2 13-JUL-11 2WGP 1 VERSN
REVDAT 1 06-OCT-09 2WGP 0
JRNL AUTH G.T.LOUNTOS,J.E.TROPEA,S.CHERRY,D.S.WAUGH
JRNL TITL OVERPRODUCTION, PURIFICATION AND STRUCTURE DETERMINATION OF
JRNL TITL 2 HUMAN DUAL-SPECIFICITY PHOSPHATASE 14.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 65 1013 2009
JRNL REFN ISSN 0907-4449
JRNL PMID 19770498
JRNL DOI 10.1107/S0907444909023762
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.MARTI,A.KRAUSE,N.H.POST,C.LYDDANE,B.DUPONT,M.SADELAIN,
REMARK 1 AUTH 2 P.D.KING
REMARK 1 TITL NEGATIVE-FEEDBACK REGULATION OF CD28 COSTIMULATION BY A
REMARK 1 TITL 2 NOVEL MITOGEN-ACTIVATED PROTEIN KINASE PHOSPHATASE, MKP6.
REMARK 1 REF J.IMMUNOL. V. 166 197 2001
REMARK 1 REFN ISSN 0022-1767
REMARK 1 PMID 11123293
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0057
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 31259
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1670
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2118
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2651
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 347
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) : 21.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.30000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.133
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.131
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.695
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2741 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1866 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3729 ; 1.411 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4523 ; 1.031 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 337 ; 5.877 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;34.558 ;22.203
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 448 ;13.914 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;21.876 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 415 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3019 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 589 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1675 ; 0.660 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 674 ; 0.192 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2719 ; 1.162 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1066 ; 1.848 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1008 ; 2.943 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 24 A 103
REMARK 3 ORIGIN FOR THE GROUP (A): -38.0710 -21.9600 7.1740
REMARK 3 T TENSOR
REMARK 3 T11: -0.1042 T22: -0.1079
REMARK 3 T33: 0.0730 T12: 0.0098
REMARK 3 T13: -0.0218 T23: -0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 1.7259 L22: 0.9269
REMARK 3 L33: 1.4584 L12: 0.0002
REMARK 3 L13: 0.1550 L23: 0.2298
REMARK 3 S TENSOR
REMARK 3 S11: -0.0785 S12: -0.1698 S13: 0.1850
REMARK 3 S21: 0.0609 S22: -0.0062 S23: 0.0187
REMARK 3 S31: -0.0513 S32: -0.0348 S33: 0.0847
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 104 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): -28.9530 -25.3880 -6.3000
REMARK 3 T TENSOR
REMARK 3 T11: -0.0883 T22: -0.0817
REMARK 3 T33: 0.0745 T12: -0.0152
REMARK 3 T13: -0.0084 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.7543 L22: 1.0405
REMARK 3 L33: 0.8019 L12: -0.0948
REMARK 3 L13: 0.0684 L23: 0.0655
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: 0.0540 S13: 0.1099
REMARK 3 S21: -0.0717 S22: -0.0451 S23: -0.1084
REMARK 3 S31: -0.0555 S32: 0.0856 S33: 0.0704
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 186 A 191
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0450 -35.8510 -10.8260
REMARK 3 T TENSOR
REMARK 3 T11: -0.1329 T22: -0.0822
REMARK 3 T33: 0.0667 T12: 0.0056
REMARK 3 T13: 0.0866 T23: 0.0686
REMARK 3 L TENSOR
REMARK 3 L11: 40.5697 L22: 55.5619
REMARK 3 L33: 8.1592 L12: -2.8051
REMARK 3 L13: -1.8190 L23: 0.9586
REMARK 3 S TENSOR
REMARK 3 S11: 0.6258 S12: 0.5613 S13: 1.2397
REMARK 3 S21: -1.7467 S22: -0.5903 S23: -1.6275
REMARK 3 S31: -0.1791 S32: 1.0562 S33: -0.0355
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 : B 26 B 80
REMARK 3 ORIGIN FOR THE GROUP (A): -34.2660 -24.4050 -52.2330
REMARK 3 T TENSOR
REMARK 3 T11: -0.0799 T22: -0.0529
REMARK 3 T33: 0.0260 T12: -0.0209
REMARK 3 T13: -0.0109 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.8143 L22: 0.8823
REMARK 3 L33: 1.1771 L12: 0.4170
REMARK 3 L13: -0.8668 L23: 0.3894
REMARK 3 S TENSOR
REMARK 3 S11: -0.0730 S12: 0.2960 S13: -0.0644
REMARK 3 S21: -0.1136 S22: 0.0619 S23: -0.0329
REMARK 3 S31: -0.0405 S32: 0.0254 S33: 0.0110
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 81 B 162
REMARK 3 ORIGIN FOR THE GROUP (A): -38.2130 -20.3610 -38.1700
REMARK 3 T TENSOR
REMARK 3 T11: -0.0698 T22: -0.0877
REMARK 3 T33: 0.0425 T12: -0.0074
REMARK 3 T13: 0.0097 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.7313 L22: 0.7021
REMARK 3 L33: 1.3021 L12: 0.0701
REMARK 3 L13: -0.0400 L23: -0.0724
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: -0.0212 S13: 0.0478
REMARK 3 S21: -0.0234 S22: -0.0136 S23: 0.0340
REMARK 3 S31: -0.0754 S32: 0.0239 S33: 0.0061
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 163 B 190
REMARK 3 ORIGIN FOR THE GROUP (A): -49.5830 -22.4440 -26.7600
REMARK 3 T TENSOR
REMARK 3 T11: -0.0423 T22: -0.0609
REMARK 3 T33: 0.0504 T12: 0.0056
REMARK 3 T13: 0.0285 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 3.9553 L22: 1.3901
REMARK 3 L33: 1.5063 L12: 2.1290
REMARK 3 L13: 1.1137 L23: 1.1391
REMARK 3 S TENSOR
REMARK 3 S11: 0.1041 S12: -0.3771 S13: 0.1551
REMARK 3 S21: 0.1389 S22: -0.1715 S23: 0.0827
REMARK 3 S31: -0.0963 S32: -0.1120 S33: 0.0674
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. NO ELECTRON DENSITY WAS PRESENT FOR RESIDUES 2-23 AND
REMARK 3 THUS ARE NOT INCLUDED IN THE FINAL MODEL
REMARK 4
REMARK 4 2WGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1290038883.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MSC OSMIC MIRROR SYSTEM
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32950
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2ESB
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE PH 5.4, 1.1 M
REMARK 280 AMMONIUM PHOSPHATE MONOBASIC,0.1 M NDSB-256 CRYOPROTECTED WITH
REMARK 280 20% GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 42.50550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.50550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 57.55600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.50550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.50550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.55600
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 42.50550
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 42.50550
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 57.55600
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 42.50550
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 42.50550
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 57.55600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -154.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 -85.01100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 -85.01100
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 -85.01100
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 -85.01100
REMARK 350 BIOMT2 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 -85.01100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -85.01100
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -85.01100
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 -85.01100
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 -85.01100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -85.01100
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -85.01100
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 -85.01100
REMARK 350 BIOMT3 4 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 SER A 2
REMARK 465 SER A 3
REMARK 465 ARG A 4
REMARK 465 GLY A 5
REMARK 465 HIS A 6
REMARK 465 SER A 7
REMARK 465 THR A 8
REMARK 465 LEU A 9
REMARK 465 PRO A 10
REMARK 465 ARG A 11
REMARK 465 THR A 12
REMARK 465 LEU A 13
REMARK 465 MET A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 MET A 18
REMARK 465 ILE A 19
REMARK 465 SER A 20
REMARK 465 GLU A 21
REMARK 465 GLY A 22
REMARK 465 ASP A 23
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 ARG B 4
REMARK 465 GLY B 5
REMARK 465 HIS B 6
REMARK 465 SER B 7
REMARK 465 THR B 8
REMARK 465 LEU B 9
REMARK 465 PRO B 10
REMARK 465 ARG B 11
REMARK 465 THR B 12
REMARK 465 LEU B 13
REMARK 465 MET B 14
REMARK 465 ALA B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
REMARK 465 MET B 18
REMARK 465 ILE B 19
REMARK 465 SER B 20
REMARK 465 GLU B 21
REMARK 465 GLY B 22
REMARK 465 ASP B 23
REMARK 465 ILE B 24
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 24 CG1 CG2 CD1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 2147 O HOH B 2148 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2068 O HOH B 2157 4545 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 38 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 59 49.55 -85.43
REMARK 500 CYS A 111 -139.00 -128.86
REMARK 500 SER A 116 -67.09 -121.66
REMARK 500 ARG A 149 73.47 -165.67
REMARK 500 CYS B 111 -140.31 -123.19
REMARK 500 SER B 116 -67.35 -121.75
REMARK 500 ARG B 149 74.85 -161.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2018 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A2043 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B2011 DISTANCE = 6.59 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 200
DBREF 2WGP A 2 191 UNP O95147 DUS14_HUMAN 2 191
DBREF 2WGP B 2 191 UNP O95147 DUS14_HUMAN 2 191
SEQRES 1 A 190 SER SER ARG GLY HIS SER THR LEU PRO ARG THR LEU MET
SEQRES 2 A 190 ALA PRO ARG MET ILE SER GLU GLY ASP ILE GLY GLY ILE
SEQRES 3 A 190 ALA GLN ILE THR SER SER LEU PHE LEU GLY ARG GLY SER
SEQRES 4 A 190 VAL ALA SER ASN ARG HIS LEU LEU GLN ALA ARG GLY ILE
SEQRES 5 A 190 THR CYS ILE VAL ASN ALA THR ILE GLU ILE PRO ASN PHE
SEQRES 6 A 190 ASN TRP PRO GLN PHE GLU TYR VAL LYS VAL PRO LEU ALA
SEQRES 7 A 190 ASP MET PRO HIS ALA PRO ILE GLY LEU TYR PHE ASP THR
SEQRES 8 A 190 VAL ALA ASP LYS ILE HIS SER VAL SER ARG LYS HIS GLY
SEQRES 9 A 190 ALA THR LEU VAL HIS CYS ALA ALA GLY VAL SER ARG SER
SEQRES 10 A 190 ALA THR LEU CYS ILE ALA TYR LEU MET LYS PHE HIS ASN
SEQRES 11 A 190 VAL CYS LEU LEU GLU ALA TYR ASN TRP VAL LYS ALA ARG
SEQRES 12 A 190 ARG PRO VAL ILE ARG PRO ASN VAL GLY PHE TRP ARG GLN
SEQRES 13 A 190 LEU ILE ASP TYR GLU ARG GLN LEU PHE GLY LYS SER THR
SEQRES 14 A 190 VAL LYS MET VAL GLN THR PRO TYR GLY ILE VAL PRO ASP
SEQRES 15 A 190 VAL TYR GLU LYS GLU SER ARG HIS
SEQRES 1 B 190 SER SER ARG GLY HIS SER THR LEU PRO ARG THR LEU MET
SEQRES 2 B 190 ALA PRO ARG MET ILE SER GLU GLY ASP ILE GLY GLY ILE
SEQRES 3 B 190 ALA GLN ILE THR SER SER LEU PHE LEU GLY ARG GLY SER
SEQRES 4 B 190 VAL ALA SER ASN ARG HIS LEU LEU GLN ALA ARG GLY ILE
SEQRES 5 B 190 THR CYS ILE VAL ASN ALA THR ILE GLU ILE PRO ASN PHE
SEQRES 6 B 190 ASN TRP PRO GLN PHE GLU TYR VAL LYS VAL PRO LEU ALA
SEQRES 7 B 190 ASP MET PRO HIS ALA PRO ILE GLY LEU TYR PHE ASP THR
SEQRES 8 B 190 VAL ALA ASP LYS ILE HIS SER VAL SER ARG LYS HIS GLY
SEQRES 9 B 190 ALA THR LEU VAL HIS CYS ALA ALA GLY VAL SER ARG SER
SEQRES 10 B 190 ALA THR LEU CYS ILE ALA TYR LEU MET LYS PHE HIS ASN
SEQRES 11 B 190 VAL CYS LEU LEU GLU ALA TYR ASN TRP VAL LYS ALA ARG
SEQRES 12 B 190 ARG PRO VAL ILE ARG PRO ASN VAL GLY PHE TRP ARG GLN
SEQRES 13 B 190 LEU ILE ASP TYR GLU ARG GLN LEU PHE GLY LYS SER THR
SEQRES 14 B 190 VAL LYS MET VAL GLN THR PRO TYR GLY ILE VAL PRO ASP
SEQRES 15 B 190 VAL TYR GLU LYS GLU SER ARG HIS
HET PO4 A 200 5
HET PO4 B 200 5
HETNAM PO4 PHOSPHATE ION
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 5 HOH *347(H2 O)
HELIX 1 1 ARG A 38 SER A 43 1 6
HELIX 2 2 ASN A 44 ARG A 51 1 8
HELIX 3 3 PRO A 85 LEU A 88 5 4
HELIX 4 4 TYR A 89 LYS A 103 1 15
HELIX 5 5 SER A 116 ASN A 131 1 16
HELIX 6 6 CYS A 133 ARG A 145 1 13
HELIX 7 7 ASN A 151 GLY A 167 1 17
HELIX 8 8 ASP A 183 ARG A 190 1 8
HELIX 9 9 ARG B 38 SER B 43 1 6
HELIX 10 10 ASN B 44 ALA B 50 1 7
HELIX 11 11 PRO B 85 LEU B 88 5 4
HELIX 12 12 TYR B 89 LYS B 103 1 15
HELIX 13 13 SER B 116 ASN B 131 1 16
HELIX 14 14 CYS B 133 ARG B 145 1 13
HELIX 15 15 ASN B 151 GLY B 167 1 17
HELIX 16 16 ASP B 183 ARG B 190 1 8
SHEET 1 AA 5 ILE A 27 THR A 31 0
SHEET 2 AA 5 LEU A 34 GLY A 37 -1 O LEU A 34 N ILE A 30
SHEET 3 AA 5 THR A 107 HIS A 110 1 O THR A 107 N PHE A 35
SHEET 4 AA 5 CYS A 55 ASN A 58 1 O CYS A 55 N LEU A 108
SHEET 5 AA 5 GLU A 72 LYS A 75 1 O GLU A 72 N ILE A 56
SHEET 1 AB 2 MET A 173 THR A 176 0
SHEET 2 AB 2 GLY A 179 PRO A 182 -1 O GLY A 179 N THR A 176
SHEET 1 BA 5 ILE B 27 THR B 31 0
SHEET 2 BA 5 LEU B 34 GLY B 37 -1 O LEU B 34 N ILE B 30
SHEET 3 BA 5 THR B 107 HIS B 110 1 O THR B 107 N PHE B 35
SHEET 4 BA 5 CYS B 55 ASN B 58 1 O CYS B 55 N LEU B 108
SHEET 5 BA 5 GLU B 72 LYS B 75 1 O GLU B 72 N ILE B 56
SHEET 1 BB 2 MET B 173 THR B 176 0
SHEET 2 BB 2 GLY B 179 PRO B 182 -1 O GLY B 179 N THR B 176
SITE 1 AC1 10 ILE A 61 ASP A 80 CYS A 111 ALA A 112
SITE 2 AC1 10 ALA A 113 GLY A 114 VAL A 115 SER A 116
SITE 3 AC1 10 ARG A 117 HOH A2179
SITE 1 AC2 9 ILE B 61 ASP B 80 CYS B 111 ALA B 112
SITE 2 AC2 9 ALA B 113 GLY B 114 VAL B 115 SER B 116
SITE 3 AC2 9 ARG B 117
CRYST1 85.011 85.011 115.112 90.00 90.00 90.00 I 4 16
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 0.011763 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011763 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008687 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
