HEADER HYDROLASE 31-MAR-18 6CWX
TITLE CRYSTAL STRUCTURE OF HUMAN RIBONUCLEASE P/MRP PROTEINS RPP20/RPP25
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE P PROTEIN SUBUNIT P20;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNASEP PROTEIN P20,RIBONUCLEASES P/MRP PROTEIN SUBUNIT POP7
COMPND 5 HOMOLOG,HPOP7;
COMPND 6 EC: 3.1.26.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RIBONUCLEASE P PROTEIN SUBUNIT P25;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: RNASE P PROTEIN SUBUNIT P25;
COMPND 12 EC: 3.1.26.5;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POP7, RPP20;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHTT7K;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RPP25;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHTT7K
KEYWDS ENDONUCLEASE, RIBONUCLEASE P, RIBONUCLEASE P COMPLEX, RIBONUCLEASE
KEYWDS 2 MRP, RIBONUCLEASE MRP COMPLEX, TRNA PROCESSING, RRNA PROCESSING,
KEYWDS 3 NUCLEIC ACID BINDING, RNA BINDING, PROTEIN BINDING, PROTEIN
KEYWDS 4 HETERODIMER, HETERODIMER, DIMER, HYDROLASE, NUCLEUS, NUCLEOLUS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.W.CHAN,B.R.KIESEL,A.MONDRAGON
REVDAT 3 01-JAN-20 6CWX 1 REMARK
REVDAT 2 23-MAY-18 6CWX 1 JRNL
REVDAT 1 18-APR-18 6CWX 0
JRNL AUTH C.W.CHAN,B.R.KIESEL,A.MONDRAGON
JRNL TITL CRYSTAL STRUCTURE OF HUMAN RPP20/RPP25 REVEALS QUATERNARY
JRNL TITL 2 LEVEL ADAPTATION OF THE ALBA SCAFFOLD AS STRUCTURAL BASIS
JRNL TITL 3 FOR SINGLE-STRANDED RNA BINDING.
JRNL REF J. MOL. BIOL. V. 430 1403 2018
JRNL REFN ESSN 1089-8638
JRNL PMID 29625199
JRNL DOI 10.1016/J.JMB.2018.03.029
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0218
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23502
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1211
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1720
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1746
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.799
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1785 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1732 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2405 ; 1.384 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4001 ; 0.866 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 221 ; 5.477 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;31.779 ;22.432
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 304 ;13.032 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;13.925 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 277 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1934 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 350 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
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 29 A 140
REMARK 3 ORIGIN FOR THE GROUP (A): 240.4611 164.0226 36.1985
REMARK 3 T TENSOR
REMARK 3 T11: 0.1584 T22: 0.1432
REMARK 3 T33: 0.1093 T12: -0.0308
REMARK 3 T13: 0.0471 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 1.3461 L22: 2.8234
REMARK 3 L33: 0.4970 L12: -0.7537
REMARK 3 L13: -0.3281 L23: 0.5362
REMARK 3 S TENSOR
REMARK 3 S11: 0.0931 S12: 0.0606 S13: 0.2128
REMARK 3 S21: -0.2319 S22: 0.0780 S23: -0.2020
REMARK 3 S31: -0.0665 S32: 0.1548 S33: -0.1711
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 22 B 157
REMARK 3 ORIGIN FOR THE GROUP (A): 220.9172 164.5102 39.6873
REMARK 3 T TENSOR
REMARK 3 T11: 0.1416 T22: 0.0247
REMARK 3 T33: 0.2952 T12: 0.0141
REMARK 3 T13: 0.0083 T23: 0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 0.5458 L22: 1.8289
REMARK 3 L33: 0.9974 L12: -0.3401
REMARK 3 L13: -0.0318 L23: 0.5301
REMARK 3 S TENSOR
REMARK 3 S11: 0.0522 S12: 0.0916 S13: 0.1079
REMARK 3 S21: -0.1286 S22: 0.0200 S23: 0.5029
REMARK 3 S31: -0.1010 S32: 0.0764 S33: -0.0723
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6CWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1000228844.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0 - 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.2.1
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.29
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24742
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 48.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.80
REMARK 200 R MERGE FOR SHELL (I) : 0.49500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: AUTOSHARP 3.10.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM POTASSIUM FORMATE, PH 7.5, 300
REMARK 280 MM MAGNESIUM SULFATE, 4.5% PEG 300, 4.5% PEG 400, 4.5% PEG 1000,
REMARK 280 4.5% PEG 4000, AND 4.5% PEG 8000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 2
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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 Y,X,-Z
REMARK 290 14555 -Y,-X,-Z
REMARK 290 15555 Y,-X,Z
REMARK 290 16555 -Y,X,Z
REMARK 290 17555 X,Z,-Y
REMARK 290 18555 -X,Z,Y
REMARK 290 19555 -X,-Z,-Y
REMARK 290 20555 X,-Z,Y
REMARK 290 21555 Z,Y,-X
REMARK 290 22555 Z,-Y,X
REMARK 290 23555 -Z,Y,X
REMARK 290 24555 -Z,-Y,-X
REMARK 290 25555 X+1/2,Y+1/2,Z+1/2
REMARK 290 26555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 27555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 28555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 29555 Z+1/2,X+1/2,Y+1/2
REMARK 290 30555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 31555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 32555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 33555 Y+1/2,Z+1/2,X+1/2
REMARK 290 34555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 35555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 36555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290 37555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 38555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290 39555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 40555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 41555 X+1/2,Z+1/2,-Y+1/2
REMARK 290 42555 -X+1/2,Z+1/2,Y+1/2
REMARK 290 43555 -X+1/2,-Z+1/2,-Y+1/2
REMARK 290 44555 X+1/2,-Z+1/2,Y+1/2
REMARK 290 45555 Z+1/2,Y+1/2,-X+1/2
REMARK 290 46555 Z+1/2,-Y+1/2,X+1/2
REMARK 290 47555 -Z+1/2,Y+1/2,X+1/2
REMARK 290 48555 -Z+1/2,-Y+1/2,-X+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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 91.09500
REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 91.09500
REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 91.09500
REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 91.09500
REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 91.09500
REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 91.09500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 48-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 121590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 262750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1370.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 364.38000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 364.38000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 364.38000
REMARK 350 BIOMT2 3 0.000000 1.000000 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 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 364.38000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 0.000000 0.000000 1.000000 182.19000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 -182.19000
REMARK 350 BIOMT1 6 0.000000 0.000000 1.000000 182.19000
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 364.38000
REMARK 350 BIOMT3 6 0.000000 -1.000000 0.000000 182.19000
REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 182.19000
REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 364.38000
REMARK 350 BIOMT3 7 0.000000 1.000000 0.000000 -182.19000
REMARK 350 BIOMT1 8 0.000000 0.000000 -1.000000 182.19000
REMARK 350 BIOMT2 8 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 -1.000000 0.000000 182.19000
REMARK 350 BIOMT1 9 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 9 0.000000 0.000000 1.000000 182.19000
REMARK 350 BIOMT3 9 1.000000 0.000000 0.000000 -182.19000
REMARK 350 BIOMT1 10 0.000000 -1.000000 0.000000 364.38000
REMARK 350 BIOMT2 10 0.000000 0.000000 1.000000 182.19000
REMARK 350 BIOMT3 10 -1.000000 0.000000 0.000000 182.19000
REMARK 350 BIOMT1 11 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 11 0.000000 0.000000 -1.000000 182.19000
REMARK 350 BIOMT3 11 -1.000000 0.000000 0.000000 182.19000
REMARK 350 BIOMT1 12 0.000000 -1.000000 0.000000 364.38000
REMARK 350 BIOMT2 12 0.000000 0.000000 -1.000000 182.19000
REMARK 350 BIOMT3 12 1.000000 0.000000 0.000000 -182.19000
REMARK 350 BIOMT1 13 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 13 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 14 0.000000 -1.000000 0.000000 364.38000
REMARK 350 BIOMT2 14 -1.000000 0.000000 0.000000 364.38000
REMARK 350 BIOMT3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 15 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 15 -1.000000 0.000000 0.000000 364.38000
REMARK 350 BIOMT3 15 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 16 0.000000 -1.000000 0.000000 364.38000
REMARK 350 BIOMT2 16 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 16 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 17 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 17 0.000000 0.000000 1.000000 182.19000
REMARK 350 BIOMT3 17 0.000000 -1.000000 0.000000 182.19000
REMARK 350 BIOMT1 18 -1.000000 0.000000 0.000000 364.38000
REMARK 350 BIOMT2 18 0.000000 0.000000 1.000000 182.19000
REMARK 350 BIOMT3 18 0.000000 1.000000 0.000000 -182.19000
REMARK 350 BIOMT1 19 -1.000000 0.000000 0.000000 364.38000
REMARK 350 BIOMT2 19 0.000000 0.000000 -1.000000 182.19000
REMARK 350 BIOMT3 19 0.000000 -1.000000 0.000000 182.19000
REMARK 350 BIOMT1 20 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 20 0.000000 0.000000 -1.000000 182.19000
REMARK 350 BIOMT3 20 0.000000 1.000000 0.000000 -182.19000
REMARK 350 BIOMT1 21 0.000000 0.000000 1.000000 182.19000
REMARK 350 BIOMT2 21 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 21 -1.000000 0.000000 0.000000 182.19000
REMARK 350 BIOMT1 22 0.000000 0.000000 1.000000 182.19000
REMARK 350 BIOMT2 22 0.000000 -1.000000 0.000000 364.38000
REMARK 350 BIOMT3 22 1.000000 0.000000 0.000000 -182.19000
REMARK 350 BIOMT1 23 0.000000 0.000000 -1.000000 182.19000
REMARK 350 BIOMT2 23 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 23 1.000000 0.000000 0.000000 -182.19000
REMARK 350 BIOMT1 24 0.000000 0.000000 -1.000000 182.19000
REMARK 350 BIOMT2 24 0.000000 -1.000000 0.000000 364.38000
REMARK 350 BIOMT3 24 -1.000000 0.000000 0.000000 182.19000
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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 ASN A 4
REMARK 465 ARG A 5
REMARK 465 GLU A 6
REMARK 465 PRO A 7
REMARK 465 ARG A 8
REMARK 465 GLY A 9
REMARK 465 ALA A 10
REMARK 465 VAL A 11
REMARK 465 GLU A 12
REMARK 465 ALA A 13
REMARK 465 GLU A 14
REMARK 465 LEU A 15
REMARK 465 ASP A 16
REMARK 465 PRO A 17
REMARK 465 VAL A 18
REMARK 465 GLU A 19
REMARK 465 TYR A 20
REMARK 465 THR A 21
REMARK 465 LEU A 22
REMARK 465 ARG A 23
REMARK 465 LYS A 24
REMARK 465 ARG A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 SER A 28
REMARK 465 ALA A 60
REMARK 465 ARG A 61
REMARK 465 GLY A 62
REMARK 465 THR A 115
REMARK 465 ASP A 116
REMARK 465 THR A 117
REMARK 465 ARG A 118
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASN B 3
REMARK 465 PHE B 4
REMARK 465 ARG B 5
REMARK 465 LYS B 6
REMARK 465 VAL B 7
REMARK 465 ARG B 8
REMARK 465 SER B 9
REMARK 465 GLU B 10
REMARK 465 GLU B 11
REMARK 465 ALA B 12
REMARK 465 PRO B 13
REMARK 465 ALA B 14
REMARK 465 GLY B 15
REMARK 465 CYS B 16
REMARK 465 GLY B 17
REMARK 465 ALA B 18
REMARK 465 GLU B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 PRO B 110
REMARK 465 PRO B 111
REMARK 465 GLY B 112
REMARK 465 PRO B 113
REMARK 465 THR B 114
REMARK 465 GLN B 115
REMARK 465 GLY B 116
REMARK 465 GLN B 117
REMARK 465 THR B 118
REMARK 465 PRO B 119
REMARK 465 GLY B 120
REMARK 465 GLU B 121
REMARK 465 PRO B 122
REMARK 465 ALA B 123
REMARK 465 ALA B 124
REMARK 465 PRO B 158
REMARK 465 GLY B 159
REMARK 465 PRO B 160
REMARK 465 SER B 161
REMARK 465 SER B 162
REMARK 465 PRO B 163
REMARK 465 PRO B 164
REMARK 465 ALA B 165
REMARK 465 ALA B 166
REMARK 465 PRO B 167
REMARK 465 ALA B 168
REMARK 465 SER B 169
REMARK 465 LYS B 170
REMARK 465 ARG B 171
REMARK 465 SER B 172
REMARK 465 LEU B 173
REMARK 465 GLY B 174
REMARK 465 GLU B 175
REMARK 465 PRO B 176
REMARK 465 ALA B 177
REMARK 465 ALA B 178
REMARK 465 GLY B 179
REMARK 465 GLU B 180
REMARK 465 GLY B 181
REMARK 465 SER B 182
REMARK 465 ALA B 183
REMARK 465 LYS B 184
REMARK 465 ARG B 185
REMARK 465 SER B 186
REMARK 465 GLN B 187
REMARK 465 PRO B 188
REMARK 465 GLU B 189
REMARK 465 PRO B 190
REMARK 465 GLY B 191
REMARK 465 VAL B 192
REMARK 465 ALA B 193
REMARK 465 ASP B 194
REMARK 465 GLU B 195
REMARK 465 ASP B 196
REMARK 465 GLN B 197
REMARK 465 THR B 198
REMARK 465 ALA B 199
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 B 32 73.61 -152.75
REMARK 500 LEU B 126 104.09 -166.56
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 FMT A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 203
DBREF 6CWX A 1 140 UNP O75817 POP7_HUMAN 1 140
DBREF 6CWX B 1 199 UNP Q9BUL9 RPP25_HUMAN 1 199
SEQADV 6CWX GLY A -1 UNP O75817 EXPRESSION TAG
SEQADV 6CWX HIS A 0 UNP O75817 EXPRESSION TAG
SEQADV 6CWX GLY B -1 UNP Q9BUL9 EXPRESSION TAG
SEQADV 6CWX HIS B 0 UNP Q9BUL9 EXPRESSION TAG
SEQRES 1 A 142 GLY HIS MET ALA GLU ASN ARG GLU PRO ARG GLY ALA VAL
SEQRES 2 A 142 GLU ALA GLU LEU ASP PRO VAL GLU TYR THR LEU ARG LYS
SEQRES 3 A 142 ARG LEU PRO SER ARG LEU PRO ARG ARG PRO ASN ASP ILE
SEQRES 4 A 142 TYR VAL ASN MET LYS THR ASP PHE LYS ALA GLN LEU ALA
SEQRES 5 A 142 ARG CME GLN LYS LEU LEU ASP GLY GLY ALA ARG GLY GLN
SEQRES 6 A 142 ASN ALA CME SER GLU ILE TYR ILE HIS GLY LEU GLY LEU
SEQRES 7 A 142 ALA ILE ASN ARG ALA ILE ASN ILE ALA LEU GLN LEU GLN
SEQRES 8 A 142 ALA GLY SER PHE GLY SER LEU GLN VAL ALA ALA ASN THR
SEQRES 9 A 142 SER THR VAL GLU LEU VAL ASP GLU LEU GLU PRO GLU THR
SEQRES 10 A 142 ASP THR ARG GLU PRO LEU THR ARG ILE ARG ASN ASN SER
SEQRES 11 A 142 ALA ILE HIS ILE ARG VAL PHE ARG VAL THR PRO LYS
SEQRES 1 B 201 GLY HIS MET GLU ASN PHE ARG LYS VAL ARG SER GLU GLU
SEQRES 2 B 201 ALA PRO ALA GLY CYS GLY ALA GLU GLY GLY GLY PRO GLY
SEQRES 3 B 201 SER GLY PRO PHE ALA ASP LEU ALA PRO GLY ALA VAL HIS
SEQRES 4 B 201 MET ARG VAL LYS GLU GLY SER LYS ILE ARG ASN LEU MET
SEQRES 5 B 201 ALA PHE ALA THR ALA SER MET ALA GLN PRO ALA THR ARG
SEQRES 6 B 201 ALA ILE VAL PHE SER GLY CME GLY ARG ALA THR THR LYS
SEQRES 7 B 201 THR VAL THR CYS ALA GLU ILE LEU LYS ARG ARG LEU ALA
SEQRES 8 B 201 GLY LEU HIS GLN VAL THR ARG LEU ARG TYR ARG SER VAL
SEQRES 9 B 201 ARG GLU VAL TRP GLN SER LEU PRO PRO GLY PRO THR GLN
SEQRES 10 B 201 GLY GLN THR PRO GLY GLU PRO ALA ALA SER LEU SER VAL
SEQRES 11 B 201 LEU LYS ASN VAL PRO GLY LEU ALA ILE LEU LEU SER LYS
SEQRES 12 B 201 ASP ALA LEU ASP PRO ARG GLN PRO GLY TYR GLN PRO PRO
SEQRES 13 B 201 ASN PRO HIS PRO GLY PRO SER SER PRO PRO ALA ALA PRO
SEQRES 14 B 201 ALA SER LYS ARG SER LEU GLY GLU PRO ALA ALA GLY GLU
SEQRES 15 B 201 GLY SER ALA LYS ARG SER GLN PRO GLU PRO GLY VAL ALA
SEQRES 16 B 201 ASP GLU ASP GLN THR ALA
MODRES 6CWX CME A 52 CYS MODIFIED RESIDUE
MODRES 6CWX CME A 66 CYS MODIFIED RESIDUE
MODRES 6CWX CME B 70 CYS MODIFIED RESIDUE
HET CME A 52 10
HET CME A 66 10
HET CME B 70 10
HET FMT A 201 3
HET FMT B 201 3
HET SO4 B 202 5
HET SO4 B 203 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM FMT FORMIC ACID
HETNAM SO4 SULFATE ION
FORMUL 1 CME 3(C5 H11 N O3 S2)
FORMUL 3 FMT 2(C H2 O2)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *100(H2 O)
HELIX 1 AA1 ASP A 44 GLY A 58 1 15
HELIX 2 AA2 ALA A 77 GLY A 91 1 15
HELIX 3 AA3 LYS B 45 GLN B 59 1 15
HELIX 4 AA4 ALA B 73 LEU B 88 1 16
SHEET 1 AA1 4 ASP A 36 TYR A 38 0
SHEET 2 AA1 4 GLU A 68 LEU A 74 1 O HIS A 72 N ILE A 37
SHEET 3 AA1 4 LEU A 121 ARG A 136 -1 O VAL A 134 N ILE A 69
SHEET 4 AA1 4 LEU A 96 GLU A 112 -1 N LEU A 107 O ARG A 125
SHEET 1 AA2 5 VAL B 36 ARG B 39 0
SHEET 2 AA2 5 ALA B 64 CME B 70 1 O VAL B 66 N MET B 38
SHEET 3 AA2 5 SER B 127 SER B 140 -1 O ILE B 137 N PHE B 67
SHEET 4 AA2 5 HIS B 92 VAL B 105 -1 N GLU B 104 O VAL B 128
SHEET 5 AA2 5 TYR B 151 GLN B 152 -1 O GLN B 152 N GLN B 93
LINK C ARG A 51 N CME A 52 1555 1555 1.33
LINK C CME A 52 N GLN A 53 1555 1555 1.31
LINK C ALA A 65 N CME A 66 1555 1555 1.33
LINK C CME A 66 N SER A 67 1555 1555 1.32
LINK C GLY B 69 N CME B 70 1555 1555 1.33
LINK C CME B 70 N GLY B 71 1555 1555 1.33
SITE 1 AC1 2 ARG A 80 ASN A 83
SITE 1 AC2 2 LYS B 45 ILE B 46
SITE 1 AC3 5 PRO B 27 HIS B 37 ARG B 39 ARG B 98
SITE 2 AC3 5 ARG B 100
SITE 1 AC4 5 PRO B 27 PHE B 28 ARG B 96 HOH B 329
SITE 2 AC4 5 HOH B 331
CRYST1 182.190 182.190 182.190 90.00 90.00 90.00 I 4 3 2 48
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 0.005489 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005489 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005489 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
