HEADER HYDROLASE 23-MAY-14 4QGP
TITLE CRYSTAL STRUCTURE OF A PYROPHOSPHATASE (AF1178) FROM ARCHAEOGLOBUS
TITLE 2 FULGIDUS DSM 4304 AT 1.80 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYROPHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 224325;
SOURCE 4 STRAIN: DSM 4304;
SOURCE 5 GENE: AF_1178;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MH4A
KEYWDS DIMERIC FOUR ALPHA-HELICAL BUNDLE, STRUCTURAL GENOMICS, JOINT CENTER
KEYWDS 2 FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 3 BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 3 24-JAN-18 4QGP 1 JRNL
REVDAT 2 22-NOV-17 4QGP 1 REMARK
REVDAT 1 02-JUL-14 4QGP 0
SPRSDE 02-JUL-14 4QGP 3OBC
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PYROPHOSPHATASE (AF1178) FROM
JRNL TITL 2 ARCHAEOGLOBUS FULGIDUS DSM 4304 AT 1.80 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 24325
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1230
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) : 1.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1089
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.1960
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1785
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -20.86000
REMARK 3 B22 (A**2) : 4.07000
REMARK 3 B33 (A**2) : 16.79000
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): 0.027
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.027
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.006
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1923 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2609 ; 1.406 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 241 ; 4.823 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;31.027 ;23.900
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 351 ;14.058 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;15.081 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 289 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1443 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 886 ; 1.875 ; 2.787
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1111 ; 2.480 ; 5.202
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1034 ; 3.074 ; 3.422
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.706
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, L, K
REMARK 3 TWIN FRACTION : 0.294
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 -7 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3829 7.9754 13.3497
REMARK 3 T TENSOR
REMARK 3 T11: 0.1416 T22: 0.1022
REMARK 3 T33: 0.0130 T12: -0.0081
REMARK 3 T13: 0.0064 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.6001 L22: 0.5253
REMARK 3 L33: 0.5806 L12: 0.0577
REMARK 3 L13: 0.0050 L23: -0.1499
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: 0.0607 S13: 0.0739
REMARK 3 S21: -0.1050 S22: 0.0431 S23: -0.0097
REMARK 3 S31: -0.0672 S32: 0.0247 S33: -0.0269
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 -6 B 100
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7499 10.8011 16.5581
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.0867
REMARK 3 T33: 0.0041 T12: 0.0040
REMARK 3 T13: -0.0054 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.9651 L22: 0.4843
REMARK 3 L33: 0.4417 L12: 0.1402
REMARK 3 L13: -0.1113 L23: -0.2177
REMARK 3 S TENSOR
REMARK 3 S11: 0.0116 S12: 0.0541 S13: 0.0002
REMARK 3 S21: -0.0519 S22: 0.0101 S23: 0.0199
REMARK 3 S31: -0.0402 S32: -0.0235 S33: -0.0217
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. A MET-INHIBITION PROTOCOL WAS USED
REMARK 3 FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION.
REMARK 3 THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 3. MAGNESIUM (MG), CHLORIDE (CL), AND POLYETHYLENE
REMARK 3 GLYCOL 200 FRAGMENTS (PG4 AND PGE) FROM THE CRYSTALLIZATION/CRYO
REMARK 3 CONDITIONS ARE MODELED INTO THE STRUCTURE. 4. THE DIFFRACTION
REMARK 3 DATA ARE PSEUDO-MEROHEDRALLY TWINNED WITH TWIN LAW (-H, L, K).
REMARK 3 THE REFINED TWIN FRACTION WAS 0.30. 6. REFLECTIONS FOR THE FREE-
REMARK 3 R SET WERE SELECTED BY RANDOM EXPANDED BY THE TWIN LAW. 7. NCS
REMARK 3 RESTRAINTS WERE APPLIED USING REFMAC'S LOCAL NCS OPT
REMARK 4
REMARK 4 4QGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000086032.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91837,0.97954
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : DOUBLE CRYSTAL 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 JANUARY 30, 2009
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24327
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 28.202
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.60500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 63.0% POLYETHYLENE GLYCOL 200, 0.2M
REMARK 280 MAGNESIUM CHLORIDE, 0.1M SODIUM CACODYLATE PH 6.0, NANODROP,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-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 24.58400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.64250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.06800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.64250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.58400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.06800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 24.58400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.06800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 51.64250
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.06800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.58400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 51.64250
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -208.0 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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 51.64250
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 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 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 336 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 338 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 349 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 MSE A -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 ASN A 101
REMARK 465 ARG A 102
REMARK 465 VAL A 103
REMARK 465 HIS A 104
REMARK 465 GLU A 105
REMARK 465 PHE A 106
REMARK 465 MSE B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ASN B 101
REMARK 465 ARG B 102
REMARK 465 VAL B 103
REMARK 465 HIS B 104
REMARK 465 GLU B 105
REMARK 465 PHE B 106
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 LYS A -7 CG CD CE NZ
REMARK 470 GLU A 55 CG CD OE1 OE2
REMARK 470 GLU A 62 CD OE1 OE2
REMARK 470 ARG A 89 NE CZ NH1 NH2
REMARK 470 LYS A 97 CG CD CE NZ
REMARK 470 TYR A 98 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B -6 CG1 CG2 CD1
REMARK 470 GLU B 55 CG CD OE1 OE2
REMARK 470 ARG B 56 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 88 CE NZ
REMARK 470 LYS B 97 CG CD CE NZ
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 TYR A 98 76.13 -117.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 36 OE1
REMARK 620 2 ASP B 67 OD2 175.2
REMARK 620 3 GLU B 33 OE1 87.7 92.0
REMARK 620 4 GLU B 64 OE1 86.9 88.3 91.3
REMARK 620 5 HOH B 304 O 92.1 92.7 89.2 178.9
REMARK 620 6 HOH B 302 O 90.7 89.8 177.5 90.5 89.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 36 OE1
REMARK 620 2 GLU A 33 OE1 87.9
REMARK 620 3 ASP A 67 OD2 177.4 93.6
REMARK 620 4 GLU A 64 OE1 90.6 93.1 91.5
REMARK 620 5 HOH A 302 O 89.5 170.7 88.7 95.9
REMARK 620 6 HOH A 305 O 86.6 91.0 91.2 175.0 79.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 205 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PG4 B 202 O5
REMARK 620 2 PG4 B 202 O4 53.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 204 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PGE B 203 O2
REMARK 620 2 PGE B 203 O1 53.0
REMARK 620 3 HOH B 335 O 147.9 113.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 205
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-356701 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT (RESIDUES 1-106) WAS EXPRESSED WITH A PURIFICATION
REMARK 999 TAG MGSDKIHHHHHH.
DBREF 4QGP A 1 106 UNP O29089 O29089_ARCFU 1 106
DBREF 4QGP B 1 106 UNP O29089 O29089_ARCFU 1 106
SEQADV 4QGP MSE A -11 UNP O29089 EXPRESSION TAG
SEQADV 4QGP GLY A -10 UNP O29089 EXPRESSION TAG
SEQADV 4QGP SER A -9 UNP O29089 EXPRESSION TAG
SEQADV 4QGP ASP A -8 UNP O29089 EXPRESSION TAG
SEQADV 4QGP LYS A -7 UNP O29089 EXPRESSION TAG
SEQADV 4QGP ILE A -6 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS A -5 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS A -4 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS A -3 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS A -2 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS A -1 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS A 0 UNP O29089 EXPRESSION TAG
SEQADV 4QGP MSE B -11 UNP O29089 EXPRESSION TAG
SEQADV 4QGP GLY B -10 UNP O29089 EXPRESSION TAG
SEQADV 4QGP SER B -9 UNP O29089 EXPRESSION TAG
SEQADV 4QGP ASP B -8 UNP O29089 EXPRESSION TAG
SEQADV 4QGP LYS B -7 UNP O29089 EXPRESSION TAG
SEQADV 4QGP ILE B -6 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS B -5 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS B -4 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS B -3 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS B -2 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS B -1 UNP O29089 EXPRESSION TAG
SEQADV 4QGP HIS B 0 UNP O29089 EXPRESSION TAG
SEQRES 1 A 118 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 A 118 GLU GLU LEU LEU ASP ILE LEU ARG GLU PHE ARG ASP SER
SEQRES 3 A 118 ARG GLY TRP LEU LYS TYR HIS THR PRO LYS ASN LEU ALA
SEQRES 4 A 118 VAL SER ILE SER ILE GLU VAL ALA GLU LEU LEU GLU ILE
SEQRES 5 A 118 PHE GLN TRP THR ARG SER SER ASP GLU GLU PHE GLU VAL
SEQRES 6 A 118 LEU GLU ARG ARG LYS GLY GLU VAL GLU GLU GLU ILE ALA
SEQRES 7 A 118 ASP VAL LEU ILE TYR LEU LEU PHE LEU CYS ASP VAL ALA
SEQRES 8 A 118 GLU ILE ASN PRO ILE GLU ALA VAL LYS ARG LYS MSE GLU
SEQRES 9 A 118 LYS ASN GLU ARG LYS TYR PRO LYS ASN ARG VAL HIS GLU
SEQRES 10 A 118 PHE
SEQRES 1 B 118 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 B 118 GLU GLU LEU LEU ASP ILE LEU ARG GLU PHE ARG ASP SER
SEQRES 3 B 118 ARG GLY TRP LEU LYS TYR HIS THR PRO LYS ASN LEU ALA
SEQRES 4 B 118 VAL SER ILE SER ILE GLU VAL ALA GLU LEU LEU GLU ILE
SEQRES 5 B 118 PHE GLN TRP THR ARG SER SER ASP GLU GLU PHE GLU VAL
SEQRES 6 B 118 LEU GLU ARG ARG LYS GLY GLU VAL GLU GLU GLU ILE ALA
SEQRES 7 B 118 ASP VAL LEU ILE TYR LEU LEU PHE LEU CYS ASP VAL ALA
SEQRES 8 B 118 GLU ILE ASN PRO ILE GLU ALA VAL LYS ARG LYS MSE GLU
SEQRES 9 B 118 LYS ASN GLU ARG LYS TYR PRO LYS ASN ARG VAL HIS GLU
SEQRES 10 B 118 PHE
MODRES 4QGP MSE A 1 MET SELENOMETHIONINE
MODRES 4QGP MSE A 91 MET SELENOMETHIONINE
MODRES 4QGP MSE B 1 MET SELENOMETHIONINE
MODRES 4QGP MSE B 91 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 91 8
HET MSE B 1 8
HET MSE B 91 8
HET MG A 201 1
HET CL A 202 1
HET MG B 201 1
HET PG4 B 202 13
HET PGE B 203 10
HET NA B 204 1
HET NA B 205 1
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM NA SODIUM ION
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 3 MG 2(MG 2+)
FORMUL 4 CL CL 1-
FORMUL 6 PG4 C8 H18 O5
FORMUL 7 PGE C6 H14 O4
FORMUL 8 NA 2(NA 1+)
FORMUL 10 HOH *103(H2 O)
HELIX 1 1 HIS A 0 ARG A 15 1 16
HELIX 2 2 TRP A 17 HIS A 21 5 5
HELIX 3 3 THR A 22 PHE A 41 1 20
HELIX 4 4 SER A 46 ARG A 57 1 12
HELIX 5 5 ARG A 57 GLU A 80 1 24
HELIX 6 6 ASN A 82 TYR A 98 1 17
HELIX 7 7 HIS B -1 ARG B 15 1 17
HELIX 8 8 TRP B 17 HIS B 21 5 5
HELIX 9 9 THR B 22 PHE B 41 1 20
HELIX 10 10 SER B 46 ARG B 57 1 12
HELIX 11 11 ARG B 57 GLU B 80 1 24
HELIX 12 12 ASN B 82 TYR B 98 1 17
SHEET 1 A 2 HIS A -4 HIS A -1 0
SHEET 2 A 2 HIS B -5 HIS B -2 1 O HIS B -4 N HIS A -2
LINK C HIS A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N GLU A 2 1555 1555 1.33
LINK C LYS A 90 N MSE A 91 1555 1555 1.34
LINK C MSE A 91 N GLU A 92 1555 1555 1.33
LINK C HIS B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N GLU B 2 1555 1555 1.33
LINK C LYS B 90 N MSE B 91 1555 1555 1.34
LINK C MSE B 91 N GLU B 92 1555 1555 1.34
LINK OE1 GLU B 36 MG MG B 201 1555 1555 2.02
LINK OE1 GLU A 36 MG MG A 201 1555 1555 2.02
LINK OE1 GLU A 33 MG MG A 201 1555 1555 2.04
LINK OD2 ASP A 67 MG MG A 201 1555 1555 2.04
LINK OD2 ASP B 67 MG MG B 201 1555 1555 2.04
LINK OE1 GLU B 33 MG MG B 201 1555 1555 2.04
LINK OE1 GLU A 64 MG MG A 201 1555 1555 2.08
LINK OE1 GLU B 64 MG MG B 201 1555 1555 2.19
LINK O5 PG4 B 202 NA NA B 205 1555 1555 2.88
LINK O4 PG4 B 202 NA NA B 205 1555 1555 3.10
LINK O2 PGE B 203 NA NA B 204 1555 1555 3.13
LINK O1 PGE B 203 NA NA B 204 1555 1555 3.15
LINK MG MG B 201 O HOH B 304 1555 1555 1.95
LINK MG MG B 201 O HOH B 302 1555 1555 2.15
LINK MG MG A 201 O HOH A 302 1555 1555 2.16
LINK MG MG A 201 O HOH A 305 1555 1555 2.39
LINK NA NA B 204 O HOH B 335 1555 1555 2.75
SITE 1 AC1 6 GLU A 33 GLU A 36 GLU A 64 ASP A 67
SITE 2 AC1 6 HOH A 302 HOH A 305
SITE 1 AC2 5 HIS A -1 MSE A 1 GLU A 2 HIS B 0
SITE 2 AC2 5 HOH B 328
SITE 1 AC3 6 GLU B 33 GLU B 36 GLU B 64 ASP B 67
SITE 2 AC3 6 HOH B 302 HOH B 304
SITE 1 AC4 6 LEU A 18 LYS A 19 HIS A 21 SER B 47
SITE 2 AC4 6 PHE B 51 NA B 205
SITE 1 AC5 5 PHE A 51 LEU B 18 LYS B 19 HIS B 21
SITE 2 AC5 5 NA B 204
SITE 1 AC6 2 PGE B 203 HOH B 335
SITE 1 AC7 1 PG4 B 202
CRYST1 49.168 102.136 103.285 90.00 90.00 90.00 I 21 21 21 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 0.020338 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009791 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009682 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
