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HEADER HYDROLASE 04-MAY-12 4F0J
TITLE CRYSTAL STRUCTURE OF A PROBABLE HYDROLYTIC ENZYME (PA3053) FROM
TITLE 2 PSEUDOMONAS AERUGINOSA PAO1 AT 1.50 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE HYDROLYTIC ENZYME;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 22-335;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: PA3053;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS ALPHA/BETA HYDROLASE FOLD, STRUCTURAL GENOMICS, JOINT CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 3 BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 04-JUL-12 4F0J 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PROBABLE HYDROLYTIC ENZYME (PA3053)
JRNL TITL 2 FROM PSEUDOMONAS AERUGINOSA PAO1 AT 1.50 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 49133
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2484
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3123
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 183
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2471
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 61
REMARK 3 SOLVENT ATOMS : 283
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.09000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : 2.49000
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): 0.070
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.848
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2635 ; 0.017 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1814 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3575 ; 1.703 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4384 ; 0.974 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 327 ; 6.097 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;35.857 ;23.386
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 421 ;12.068 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;18.159 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 377 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2937 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 564 ; 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 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 22 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): 50.0760 10.4280 5.4110
REMARK 3 T TENSOR
REMARK 3 T11: 0.1127 T22: 0.0928
REMARK 3 T33: 0.0259 T12: -0.0047
REMARK 3 T13: 0.0037 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 1.0347 L22: 0.4540
REMARK 3 L33: 0.4071 L12: 0.0250
REMARK 3 L13: 0.0536 L23: -0.0672
REMARK 3 S TENSOR
REMARK 3 S11: -0.0607 S12: 0.0801 S13: 0.0984
REMARK 3 S21: -0.0537 S22: 0.0356 S23: -0.0409
REMARK 3 S31: -0.0345 S32: 0.0382 S33: 0.0251
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 128 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3660 4.9140 18.1630
REMARK 3 T TENSOR
REMARK 3 T11: 0.1237 T22: 0.1146
REMARK 3 T33: 0.0142 T12: -0.0003
REMARK 3 T13: -0.0048 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.2913 L22: 1.1374
REMARK 3 L33: 0.3139 L12: -0.5352
REMARK 3 L13: -0.3483 L23: 0.1879
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: -0.1561 S13: -0.0695
REMARK 3 S21: 0.0402 S22: -0.0051 S23: -0.0867
REMARK 3 S31: 0.0293 S32: 0.0024 S33: 0.0160
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 179 A 272
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6520 17.0580 11.2670
REMARK 3 T TENSOR
REMARK 3 T11: 0.1434 T22: 0.0901
REMARK 3 T33: 0.0669 T12: 0.0110
REMARK 3 T13: -0.0001 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.9709 L22: 0.3061
REMARK 3 L33: 0.8500 L12: -0.0120
REMARK 3 L13: 0.4551 L23: -0.1721
REMARK 3 S TENSOR
REMARK 3 S11: -0.0535 S12: -0.0632 S13: 0.2412
REMARK 3 S21: 0.0208 S22: 0.0006 S23: 0.0306
REMARK 3 S31: -0.1416 S32: -0.0081 S33: 0.0528
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 273 A 293
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6910 17.8440 24.4300
REMARK 3 T TENSOR
REMARK 3 T11: 0.2045 T22: 0.2407
REMARK 3 T33: 0.1397 T12: 0.0347
REMARK 3 T13: 0.0370 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 9.1564 L22: 1.6819
REMARK 3 L33: 2.1354 L12: -0.6895
REMARK 3 L13: -1.0658 L23: 1.6759
REMARK 3 S TENSOR
REMARK 3 S11: 0.0755 S12: -0.1719 S13: 0.3822
REMARK 3 S21: -0.0355 S22: -0.1411 S23: 0.2316
REMARK 3 S31: -0.2256 S32: -0.3250 S33: 0.0656
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 : A 294 A 333
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6290 17.2500 26.1380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1703 T22: 0.1691
REMARK 3 T33: 0.0549 T12: 0.0123
REMARK 3 T13: -0.0226 T23: -0.0830
REMARK 3 L TENSOR
REMARK 3 L11: 2.4500 L22: 1.8749
REMARK 3 L33: 1.0444 L12: -0.3100
REMARK 3 L13: -0.5114 L23: -0.5236
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: -0.3266 S13: 0.2928
REMARK 3 S21: 0.0981 S22: 0.0239 S23: -0.0590
REMARK 3 S31: 0.0168 S32: 0.0584 S33: -0.0258
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL
REMARK 3 B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.
REMARK 3 5. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
REMARK 3 INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE
REMARK 3 ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED
REMARK 3 SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 6.
REMARK 3 NONAETHYLENE GLYCOL (2PE), SULFATE ION (SO4), CHLORIDE ION (CL)
REMARK 3 AND 1,2-ETHANEDIOL (EDO) MOLECULES FROM THE CRYSTALLIZATION/
REMARK 3 CRYOPROTECTION SOLUTION ARE MODELED. 7. THE TLS GROUPS WERE
REMARK 3 ASSIGNED WITH THE AID OF TLSMD SERVER.
REMARK 4
REMARK 4 4F0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072301.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : VERTICAL FOCUSING MIRROR; DOUBLE
REMARK 200 CRYSTAL SI(111) MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49169
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 27.811
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.67300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD,SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.00M AMMONIUM SULFATE, 2.00%
REMARK 280 POLYETHYLENE GLYCOL 400, 0.1M SODIUM HEPES PH 7.5, NANODROP,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 31.61700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.44300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.61700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.44300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A
REMARK 300 MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 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 -1.000000 0.000000 0.000000 63.23400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 779 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 GLN A 334
REMARK 465 PRO A 335
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 ARG A 298 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 321 CG CD OE1 OE2
REMARK 470 THR A 333 OG1 CG2
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 OH TYR A 206 O2 SO4 A 402 2.16
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 OE2 GLU A 129 O HOH A 590 3645 2.15
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 CYS A 105 -125.70 62.41
REMARK 500 SER A 142 -118.46 60.48
REMARK 500 ASN A 166 53.33 38.71
REMARK 500 GLN A 302 66.74 -118.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 2PE A 400
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 414
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-419247 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 22-335 OF THE TARGET
REMARK 999 SEQUENCE.
DBREF 4F0J A 22 335 UNP Q9HZF5 Q9HZF5_PSEAE 22 335
SEQADV 4F0J GLY A 0 UNP Q9HZF5 LEADER SEQUENCE
SEQRES 1 A 315 GLY SER GLN ALA PRO VAL TYR GLY GLU ARG LEU GLU GLY
SEQRES 2 A 315 PHE ASP TYR ALA TYR PRO VAL HIS TYR LEU ASP PHE THR
SEQRES 3 A 315 SER GLN GLY GLN PRO LEU SER MSE ALA TYR LEU ASP VAL
SEQRES 4 A 315 ALA PRO LYS LYS ALA ASN GLY ARG THR ILE LEU LEU MSE
SEQRES 5 A 315 HIS GLY LYS ASN PHE CYS ALA GLY THR TRP GLU ARG THR
SEQRES 6 A 315 ILE ASP VAL LEU ALA ASP ALA GLY TYR ARG VAL ILE ALA
SEQRES 7 A 315 VAL ASP GLN VAL GLY PHE CYS LYS SER SER LYS PRO ALA
SEQRES 8 A 315 HIS TYR GLN TYR SER PHE GLN GLN LEU ALA ALA ASN THR
SEQRES 9 A 315 HIS ALA LEU LEU GLU ARG LEU GLY VAL ALA ARG ALA SER
SEQRES 10 A 315 VAL ILE GLY HIS SER MSE GLY GLY MSE LEU ALA THR ARG
SEQRES 11 A 315 TYR ALA LEU LEU TYR PRO ARG GLN VAL GLU ARG LEU VAL
SEQRES 12 A 315 LEU VAL ASN PRO ILE GLY LEU GLU ASP TRP LYS ALA LEU
SEQRES 13 A 315 GLY VAL PRO TRP ARG SER VAL ASP ASP TRP TYR ARG ARG
SEQRES 14 A 315 ASP LEU GLN THR SER ALA GLU GLY ILE ARG GLN TYR GLN
SEQRES 15 A 315 GLN ALA THR TYR TYR ALA GLY GLU TRP ARG PRO GLU PHE
SEQRES 16 A 315 ASP ARG TRP VAL GLN MSE GLN ALA GLY MSE TYR ARG GLY
SEQRES 17 A 315 LYS GLY ARG GLU SER VAL ALA TRP ASN SER ALA LEU THR
SEQRES 18 A 315 TYR ASP MSE ILE PHE THR GLN PRO VAL VAL TYR GLU LEU
SEQRES 19 A 315 ASP ARG LEU GLN MSE PRO THR LEU LEU LEU ILE GLY GLU
SEQRES 20 A 315 LYS ASP ASN THR ALA ILE GLY LYS ASP ALA ALA PRO ALA
SEQRES 21 A 315 GLU LEU LYS ALA ARG LEU GLY ASN TYR ALA GLN LEU GLY
SEQRES 22 A 315 LYS ASP ALA ALA ARG ARG ILE PRO GLN ALA THR LEU VAL
SEQRES 23 A 315 GLU PHE PRO ASP LEU GLY HIS THR PRO GLN ILE GLN ALA
SEQRES 24 A 315 PRO GLU ARG PHE HIS GLN ALA LEU LEU GLU GLY LEU GLN
SEQRES 25 A 315 THR GLN PRO
MODRES 4F0J MSE A 54 MET SELENOMETHIONINE
MODRES 4F0J MSE A 72 MET SELENOMETHIONINE
MODRES 4F0J MSE A 143 MET SELENOMETHIONINE
MODRES 4F0J MSE A 146 MET SELENOMETHIONINE
MODRES 4F0J MSE A 221 MET SELENOMETHIONINE
MODRES 4F0J MSE A 225 MET SELENOMETHIONINE
MODRES 4F0J MSE A 244 MET SELENOMETHIONINE
MODRES 4F0J MSE A 259 MET SELENOMETHIONINE
HET MSE A 54 8
HET MSE A 72 13
HET MSE A 143 8
HET MSE A 146 8
HET MSE A 221 8
HET MSE A 225 8
HET MSE A 244 8
HET MSE A 259 8
HET 2PE A 400 7
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET EDO A 411 4
HET EDO A 412 4
HET CL A 413 1
HET CL A 414 1
HETNAM MSE SELENOMETHIONINE
HETNAM 2PE NONAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 2PE C18 H38 O10
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 EDO 8(C2 H6 O2)
FORMUL 15 CL 2(CL 1-)
FORMUL 17 HOH *283(H2 O)
HELIX 1 1 CYS A 78 THR A 81 5 4
HELIX 2 2 TRP A 82 ALA A 92 1 11
HELIX 3 3 SER A 116 LEU A 131 1 16
HELIX 4 4 SER A 142 TYR A 155 1 14
HELIX 5 5 ASP A 172 GLY A 177 5 6
HELIX 6 6 SER A 182 LEU A 191 1 10
HELIX 7 7 SER A 194 TYR A 206 1 13
HELIX 8 8 ARG A 212 GLU A 214 5 3
HELIX 9 9 PHE A 215 TYR A 226 1 12
HELIX 10 10 GLY A 230 GLN A 248 1 19
HELIX 11 11 VAL A 250 LEU A 257 5 8
HELIX 12 12 GLY A 274 ALA A 278 5 5
HELIX 13 13 PRO A 279 ALA A 284 1 6
HELIX 14 14 ASN A 288 ILE A 300 1 13
HELIX 15 15 THR A 314 ALA A 319 1 6
HELIX 16 16 ALA A 319 GLN A 332 1 14
SHEET 1 A 8 HIS A 41 SER A 47 0
SHEET 2 A 8 GLN A 50 VAL A 59 -1 O TYR A 56 N HIS A 41
SHEET 3 A 8 ARG A 95 VAL A 99 -1 O VAL A 96 N VAL A 59
SHEET 4 A 8 THR A 68 MSE A 72 1 N ILE A 69 O ILE A 97
SHEET 5 A 8 ALA A 136 HIS A 141 1 O ILE A 139 N LEU A 70
SHEET 6 A 8 VAL A 159 VAL A 165 1 O VAL A 163 N VAL A 138
SHEET 7 A 8 THR A 261 GLY A 266 1 O LEU A 262 N LEU A 164
SHEET 8 A 8 ALA A 303 PHE A 308 1 O VAL A 306 N LEU A 263
SSBOND 1 CYS A 78 CYS A 105 1555 1555 2.05
LINK C SER A 53 N MSE A 54 1555 1555 1.34
LINK C MSE A 54 N ALA A 55 1555 1555 1.33
LINK C LEU A 71 N MSE A 72 1555 1555 1.33
LINK C MSE A 72 N HIS A 73 1555 1555 1.35
LINK C SER A 142 N MSE A 143 1555 1555 1.35
LINK C MSE A 143 N GLY A 144 1555 1555 1.32
LINK C GLY A 145 N MSE A 146 1555 1555 1.32
LINK C MSE A 146 N LEU A 147 1555 1555 1.33
LINK C GLN A 220 N MSE A 221 1555 1555 1.34
LINK C MSE A 221 N GLN A 222 1555 1555 1.32
LINK C GLY A 224 N MSE A 225 1555 1555 1.33
LINK C MSE A 225 N TYR A 226 1555 1555 1.34
LINK C ASP A 243 N MSE A 244 1555 1555 1.34
LINK C MSE A 244 N ILE A 245 1555 1555 1.34
LINK C GLN A 258 N MSE A 259 1555 1555 1.33
LINK C MSE A 259 N PRO A 260 1555 1555 1.36
SITE 1 AC1 2 TRP A 236 HOH A 763
SITE 1 AC2 7 ALA A 195 GLU A 196 ARG A 227 HOH A 593
SITE 2 AC2 7 HOH A 618 HOH A 737 HOH A 769
SITE 1 AC3 9 GLY A 74 LYS A 75 ASN A 76 PHE A 77
SITE 2 AC3 9 HIS A 141 SER A 142 TYR A 206 HIS A 313
SITE 3 AC3 9 EDO A 407
SITE 1 AC4 5 ALA A 319 PRO A 320 GLU A 321 ARG A 322
SITE 2 AC4 5 HOH A 776
SITE 1 AC5 7 ARG A 181 ARG A 189 GLY A 274 LYS A 275
SITE 2 AC5 7 ASP A 276 ALA A 277 EDO A 406
SITE 1 AC6 7 VAL A 178 PRO A 179 ARG A 181 TRP A 186
SITE 2 AC6 7 GLY A 274 ALA A 277 HOH A 529
SITE 1 AC7 6 TRP A 186 ALA A 272 GLY A 274 LYS A 275
SITE 2 AC7 6 SO4 A 404 HOH A 609
SITE 1 AC8 6 SER A 142 TYR A 201 TYR A 206 HIS A 313
SITE 2 AC8 6 SO4 A 402 HOH A 581
SITE 1 AC9 8 HIS A 73 GLY A 74 PHE A 77 THR A 81
SITE 2 AC9 8 TRP A 82 HIS A 141 GLN A 316 HOH A 674
SITE 1 BC1 5 ARG A 95 GLU A 129 ARG A 130 LEU A 131
SITE 2 BC1 5 HOH A 775
SITE 1 BC2 8 GLY A 103 PHE A 104 CYS A 105 LYS A 109
SITE 2 BC2 8 MSE A 225 VAL A 234 HOH A 565 HOH A 781
SITE 1 BC3 4 TRP A 180 ARG A 181 SER A 182 ASP A 185
SITE 1 BC4 5 GLY A 33 ASP A 35 ASP A 185 ARG A 217
SITE 2 BC4 5 HOH A 562
SITE 1 BC5 1 ARG A 256
SITE 1 BC6 3 GLN A 118 HOH A 592 HOH A 734
CRYST1 63.234 82.886 58.464 90.00 90.00 90.00 P 21 21 2 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 0.015814 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012065 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017105 0.00000
TER 2517 THR A 333
MASTER 500 0 23 16 8 0 27 6 2815 1 146 25
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