HEADER ISOMERASE 13-AUG-08 3E58
TITLE CRYSTAL STRUCTURE OF PUTATIVE BETA-PHOSPHOGLUCOMUTASE FROM
TITLE 2 STREPTOCOCCUS THERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE BETA-PHOSPHOGLUCOMUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS THERMOPHILUS LMG 18311;
SOURCE 3 ORGANISM_TAXID: 264199;
SOURCE 4 GENE: STU0379;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) DERIVATIVE;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STREPTOCOCCUS THERMOPHILUS, BETA-PHOSPHOGLUCOMUTASE, STRUCTURAL
KEYWDS 2 GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, MCSG, UNKNOWN FUNCTION, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,C.TESAR,K.SOUVONG,G.COBB,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 4 20-OCT-21 3E58 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 3E58 1 VERSN
REVDAT 2 24-FEB-09 3E58 1 VERSN
REVDAT 1 26-AUG-08 3E58 0
JRNL AUTH C.CHANG,C.TESAR,K.SOUVONG,G.COBB,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE BETA-PHOSPHOGLUCOMUTASE FROM
JRNL TITL 2 STREPTOCOCCUS THERMOPHILUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 43701
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2327
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3201
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.1920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3317
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 364
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 18.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : -0.48000
REMARK 3 B12 (A**2) : 0.16000
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): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.985
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
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): 3537 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4829 ; 1.191 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 456 ; 5.347 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;34.556 ;25.889
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 614 ;12.166 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ; 9.920 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 539 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2720 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1668 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2461 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 272 ; 0.133 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 53 ; 0.179 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.170 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2224 ; 0.700 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3483 ; 1.065 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1506 ; 2.040 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1324 ; 3.239 ; 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 1 A 15
REMARK 3 ORIGIN FOR THE GROUP (A): 69.9836 21.5132 4.8287
REMARK 3 T TENSOR
REMARK 3 T11: -0.0206 T22: 0.0038
REMARK 3 T33: 0.0352 T12: -0.0182
REMARK 3 T13: -0.0026 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 1.3405 L22: 2.2851
REMARK 3 L33: 3.1219 L12: -1.1911
REMARK 3 L13: -0.6032 L23: 2.4060
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: 0.0378 S13: 0.0080
REMARK 3 S21: 0.0749 S22: -0.0072 S23: -0.0571
REMARK 3 S31: 0.0202 S32: 0.0043 S33: -0.0137
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 16 A 81
REMARK 3 ORIGIN FOR THE GROUP (A): 58.0946 41.8884 -3.3663
REMARK 3 T TENSOR
REMARK 3 T11: -0.0124 T22: 0.0021
REMARK 3 T33: -0.0502 T12: 0.0061
REMARK 3 T13: -0.0082 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.7458 L22: 1.9863
REMARK 3 L33: 1.0591 L12: 0.2295
REMARK 3 L13: -0.2026 L23: -0.1369
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: 0.2374 S13: 0.0184
REMARK 3 S21: -0.1502 S22: 0.0257 S23: 0.1600
REMARK 3 S31: -0.1035 S32: -0.0706 S33: -0.0095
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 82 A 211
REMARK 3 ORIGIN FOR THE GROUP (A): 68.8556 22.2456 2.7621
REMARK 3 T TENSOR
REMARK 3 T11: -0.0272 T22: -0.0513
REMARK 3 T33: -0.0320 T12: -0.0098
REMARK 3 T13: 0.0134 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.0625 L22: 1.0411
REMARK 3 L33: 0.7432 L12: 0.2012
REMARK 3 L13: 0.2208 L23: 0.4330
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: 0.0244 S13: -0.0977
REMARK 3 S21: 0.0277 S22: -0.0160 S23: 0.0093
REMARK 3 S31: 0.0606 S32: 0.0134 S33: 0.0051
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 1 B 15
REMARK 3 ORIGIN FOR THE GROUP (A): 65.5055 56.5501 23.7802
REMARK 3 T TENSOR
REMARK 3 T11: -0.0222 T22: -0.0212
REMARK 3 T33: -0.0333 T12: -0.0003
REMARK 3 T13: 0.0190 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 3.3384 L22: 1.3527
REMARK 3 L33: 2.3280 L12: 0.7424
REMARK 3 L13: 1.4917 L23: 0.4138
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: -0.0710 S13: 0.0018
REMARK 3 S21: 0.0544 S22: -0.0217 S23: -0.0011
REMARK 3 S31: 0.0339 S32: -0.0775 S33: 0.0012
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 16 B 81
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4792 43.0111 15.6318
REMARK 3 T TENSOR
REMARK 3 T11: -0.0228 T22: -0.0188
REMARK 3 T33: -0.0177 T12: 0.0011
REMARK 3 T13: 0.0221 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.4458 L22: 0.7831
REMARK 3 L33: 0.4568 L12: 0.4793
REMARK 3 L13: -0.5681 L23: 0.1271
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: 0.0692 S13: -0.0395
REMARK 3 S21: -0.0245 S22: -0.0084 S23: -0.0552
REMARK 3 S31: 0.0168 S32: -0.0052 S33: -0.0147
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 82 B 211
REMARK 3 ORIGIN FOR THE GROUP (A): 64.9435 54.8263 24.8035
REMARK 3 T TENSOR
REMARK 3 T11: -0.0343 T22: -0.0411
REMARK 3 T33: -0.0500 T12: -0.0163
REMARK 3 T13: 0.0144 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.9034 L22: 0.6440
REMARK 3 L33: 1.5540 L12: -0.0147
REMARK 3 L13: 0.0566 L23: 0.0783
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: -0.0350 S13: 0.0422
REMARK 3 S21: 0.0219 S22: -0.0034 S23: -0.0106
REMARK 3 S31: 0.0135 S32: -0.0310 S33: 0.0067
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
REMARK 4
REMARK 4 3E58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000048890.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97959
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46069
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.10
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.40400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.760
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE, 0.1M TRIS-CL PH
REMARK 280 7.0, 2.0M AMMOUNIUM SULFATE , VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.23067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.61533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.61533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 79.23067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 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 ASN A -1
REMARK 465 ALA A 0
REMARK 465 SER B -2
REMARK 465 GLY B 45
REMARK 465 GLY B 46
REMARK 465 ASN B 47
REMARK 465 THR B 48
REMARK 465 LYS B 49
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 MSE A 1 CG SE CE
REMARK 470 LYS A 49 CG CD CE NZ
REMARK 470 GLN A 50 CG CD OE1 NE2
REMARK 470 GLU A 53 CG CD OE1 OE2
REMARK 470 LYS A 62 CG CD CE NZ
REMARK 470 GLU A 70 CG CD OE1 OE2
REMARK 470 MSE B 1 CG SE CE
REMARK 470 GLN B 50 CG CD OE1 NE2
REMARK 470 LYS B 139 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 MSE A 9 -66.93 -94.33
REMARK 500 VAL A 12 -57.86 -124.60
REMARK 500 ARG A 57 -124.56 50.03
REMARK 500 ASP A 167 -36.74 -136.43
REMARK 500 MSE B 9 -74.97 -100.56
REMARK 500 ARG B 57 -118.34 52.54
REMARK 500 ASP B 167 -50.89 -139.65
REMARK 500 ASP B 179 30.40 70.85
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC61126.1 RELATED DB: TARGETDB
DBREF 3E58 A 1 211 UNP Q5M5S4 Q5M5S4_STRT2 1 211
DBREF 3E58 B 1 211 UNP Q5M5S4 Q5M5S4_STRT2 1 211
SEQADV 3E58 SER A -2 UNP Q5M5S4 EXPRESSION TAG
SEQADV 3E58 ASN A -1 UNP Q5M5S4 EXPRESSION TAG
SEQADV 3E58 ALA A 0 UNP Q5M5S4 EXPRESSION TAG
SEQADV 3E58 GLU A 104 UNP Q5M5S4 ASN 104 ENGINEERED MUTATION
SEQADV 3E58 GLY A 127 UNP Q5M5S4 ALA 127 ENGINEERED MUTATION
SEQADV 3E58 GLU A 189 UNP Q5M5S4 LEU 189 ENGINEERED MUTATION
SEQADV 3E58 SER B -2 UNP Q5M5S4 EXPRESSION TAG
SEQADV 3E58 ASN B -1 UNP Q5M5S4 EXPRESSION TAG
SEQADV 3E58 ALA B 0 UNP Q5M5S4 EXPRESSION TAG
SEQADV 3E58 GLU B 104 UNP Q5M5S4 ASN 104 ENGINEERED MUTATION
SEQADV 3E58 GLY B 127 UNP Q5M5S4 ALA 127 ENGINEERED MUTATION
SEQADV 3E58 GLU B 189 UNP Q5M5S4 LEU 189 ENGINEERED MUTATION
SEQRES 1 A 214 SER ASN ALA MSE VAL GLU ALA ILE ILE PHE ASP MSE ASP
SEQRES 2 A 214 GLY VAL LEU PHE ASP THR GLU LYS TYR TYR TYR ASP ARG
SEQRES 3 A 214 ARG ALA SER PHE LEU GLY GLN LYS GLY ILE SER ILE ASP
SEQRES 4 A 214 HIS LEU PRO PRO SER PHE PHE ILE GLY GLY ASN THR LYS
SEQRES 5 A 214 GLN VAL TRP GLU ASN ILE LEU ARG ASP GLU TYR ASP LYS
SEQRES 6 A 214 TRP ASP VAL SER THR LEU GLN GLU GLU TYR ASN THR TYR
SEQRES 7 A 214 LYS GLN ASN ASN PRO LEU PRO TYR LYS GLU LEU ILE PHE
SEQRES 8 A 214 PRO ASP VAL LEU LYS VAL LEU ASN GLU VAL LYS SER GLN
SEQRES 9 A 214 GLY LEU GLU ILE GLY LEU ALA SER SER SER VAL LYS ALA
SEQRES 10 A 214 ASP ILE PHE ARG ALA LEU GLU GLU ASN ARG LEU GLN GLY
SEQRES 11 A 214 PHE PHE ASP ILE VAL LEU SER GLY GLU GLU PHE LYS GLU
SEQRES 12 A 214 SER LYS PRO ASN PRO GLU ILE TYR LEU THR ALA LEU LYS
SEQRES 13 A 214 GLN LEU ASN VAL GLN ALA SER ARG ALA LEU ILE ILE GLU
SEQRES 14 A 214 ASP SER GLU LYS GLY ILE ALA ALA GLY VAL ALA ALA ASP
SEQRES 15 A 214 VAL GLU VAL TRP ALA ILE ARG ASP ASN GLU PHE GLY MSE
SEQRES 16 A 214 ASP GLN SER ALA ALA LYS GLY LEU LEU ASP SER LEU THR
SEQRES 17 A 214 ASP VAL LEU ASP LEU ILE
SEQRES 1 B 214 SER ASN ALA MSE VAL GLU ALA ILE ILE PHE ASP MSE ASP
SEQRES 2 B 214 GLY VAL LEU PHE ASP THR GLU LYS TYR TYR TYR ASP ARG
SEQRES 3 B 214 ARG ALA SER PHE LEU GLY GLN LYS GLY ILE SER ILE ASP
SEQRES 4 B 214 HIS LEU PRO PRO SER PHE PHE ILE GLY GLY ASN THR LYS
SEQRES 5 B 214 GLN VAL TRP GLU ASN ILE LEU ARG ASP GLU TYR ASP LYS
SEQRES 6 B 214 TRP ASP VAL SER THR LEU GLN GLU GLU TYR ASN THR TYR
SEQRES 7 B 214 LYS GLN ASN ASN PRO LEU PRO TYR LYS GLU LEU ILE PHE
SEQRES 8 B 214 PRO ASP VAL LEU LYS VAL LEU ASN GLU VAL LYS SER GLN
SEQRES 9 B 214 GLY LEU GLU ILE GLY LEU ALA SER SER SER VAL LYS ALA
SEQRES 10 B 214 ASP ILE PHE ARG ALA LEU GLU GLU ASN ARG LEU GLN GLY
SEQRES 11 B 214 PHE PHE ASP ILE VAL LEU SER GLY GLU GLU PHE LYS GLU
SEQRES 12 B 214 SER LYS PRO ASN PRO GLU ILE TYR LEU THR ALA LEU LYS
SEQRES 13 B 214 GLN LEU ASN VAL GLN ALA SER ARG ALA LEU ILE ILE GLU
SEQRES 14 B 214 ASP SER GLU LYS GLY ILE ALA ALA GLY VAL ALA ALA ASP
SEQRES 15 B 214 VAL GLU VAL TRP ALA ILE ARG ASP ASN GLU PHE GLY MSE
SEQRES 16 B 214 ASP GLN SER ALA ALA LYS GLY LEU LEU ASP SER LEU THR
SEQRES 17 B 214 ASP VAL LEU ASP LEU ILE
MODRES 3E58 MSE A 1 MET SELENOMETHIONINE
MODRES 3E58 MSE A 9 MET SELENOMETHIONINE
MODRES 3E58 MSE A 192 MET SELENOMETHIONINE
MODRES 3E58 MSE B 1 MET SELENOMETHIONINE
MODRES 3E58 MSE B 9 MET SELENOMETHIONINE
MODRES 3E58 MSE B 192 MET SELENOMETHIONINE
HET MSE A 1 5
HET MSE A 9 8
HET MSE A 192 8
HET MSE B 1 5
HET MSE B 9 8
HET MSE B 192 8
HET SO4 A 301 5
HET SO4 A 302 5
HET GOL A 303 6
HET SO4 B 301 5
HET GOL B 302 6
HET GOL B 303 6
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 9 HOH *364(H2 O)
HELIX 1 1 THR A 16 LYS A 31 1 16
HELIX 2 2 PRO A 39 ILE A 44 1 6
HELIX 3 3 ASN A 47 GLN A 50 5 4
HELIX 4 4 VAL A 51 ARG A 57 1 7
HELIX 5 5 ASP A 58 TRP A 63 5 6
HELIX 6 6 ASP A 64 ASN A 79 1 16
HELIX 7 7 PRO A 82 ILE A 87 1 6
HELIX 8 8 ASP A 90 GLN A 101 1 12
HELIX 9 9 VAL A 112 ASN A 123 1 12
HELIX 10 10 LEU A 125 PHE A 129 5 5
HELIX 11 11 GLU A 136 PHE A 138 5 3
HELIX 12 12 PRO A 145 ASN A 156 1 12
HELIX 13 13 GLN A 158 SER A 160 5 3
HELIX 14 14 SER A 168 ALA A 178 1 11
HELIX 15 15 SER A 203 ILE A 211 5 9
HELIX 16 16 THR B 16 GLY B 32 1 17
HELIX 17 17 PRO B 39 ILE B 44 5 6
HELIX 18 18 VAL B 51 ARG B 57 1 7
HELIX 19 19 ASP B 58 TRP B 63 5 6
HELIX 20 20 ASP B 64 ASN B 79 1 16
HELIX 21 21 PRO B 82 ILE B 87 1 6
HELIX 22 22 ASP B 90 GLN B 101 1 12
HELIX 23 23 VAL B 112 ASN B 123 1 12
HELIX 24 24 LEU B 125 PHE B 129 5 5
HELIX 25 25 GLU B 136 PHE B 138 5 3
HELIX 26 26 PRO B 145 ASN B 156 1 12
HELIX 27 27 GLN B 158 SER B 160 5 3
HELIX 28 28 SER B 168 ALA B 178 1 11
HELIX 29 29 SER B 203 ILE B 211 5 9
SHEET 1 A 6 ILE A 131 SER A 134 0
SHEET 2 A 6 GLU A 104 SER A 109 1 N LEU A 107 O LEU A 133
SHEET 3 A 6 ALA A 4 ASP A 8 1 N PHE A 7 O GLY A 106
SHEET 4 A 6 ALA A 162 GLU A 166 1 O LEU A 163 N ILE A 6
SHEET 5 A 6 GLU A 181 ILE A 185 1 O TRP A 183 N GLU A 166
SHEET 6 A 6 GLY A 199 LEU A 201 1 O LEU A 201 N ALA A 184
SHEET 1 B 6 ILE B 131 SER B 134 0
SHEET 2 B 6 GLU B 104 SER B 109 1 N LEU B 107 O LEU B 133
SHEET 3 B 6 ALA B 4 ASP B 8 1 N PHE B 7 O GLY B 106
SHEET 4 B 6 ALA B 162 GLU B 166 1 O LEU B 163 N ILE B 6
SHEET 5 B 6 GLU B 181 ILE B 185 1 O ILE B 185 N GLU B 166
SHEET 6 B 6 GLY B 199 LEU B 201 1 O LEU B 201 N ALA B 184
LINK C MSE A 1 N VAL A 2 1555 1555 1.32
LINK C ASP A 8 N MSE A 9 1555 1555 1.33
LINK C MSE A 9 N ASP A 10 1555 1555 1.33
LINK C GLY A 191 N MSE A 192 1555 1555 1.33
LINK C MSE A 192 N ASP A 193 1555 1555 1.33
LINK C ALA B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N VAL B 2 1555 1555 1.34
LINK C ASP B 8 N MSE B 9 1555 1555 1.33
LINK C MSE B 9 N ASP B 10 1555 1555 1.34
LINK C GLY B 191 N MSE B 192 1555 1555 1.34
LINK C MSE B 192 N ASP B 193 1555 1555 1.33
CISPEP 1 LYS A 142 PRO A 143 0 11.70
CISPEP 2 LYS B 142 PRO B 143 0 10.51
SITE 1 AC1 10 TYR A 20 ARG A 24 GLY A 46 ASN A 47
SITE 2 AC1 10 THR A 48 TYR A 72 LYS A 76 HOH A 334
SITE 3 AC1 10 HOH A 344 HOH A 468
SITE 1 AC2 7 GLN A 158 SER A 160 ARG A 161 HOH A 438
SITE 2 AC2 7 GLU B 85 HOH B 530 HOH B 631
SITE 1 AC3 8 GLY A 11 GLU A 17 ASP A 167 ILE A 185
SITE 2 AC3 8 ASP A 187 HOH A 330 HOH A 423 HOH A 440
SITE 1 AC4 4 ARG B 24 TYR B 72 LYS B 76 HOH B 574
SITE 1 AC5 6 GLY B 11 ASP B 167 ASP B 187 GLU B 189
SITE 2 AC5 6 HOH B 485 HOH B 563
SITE 1 AC6 4 GLN B 50 TRP B 52 GLU B 53 TYR B 60
CRYST1 88.784 88.784 118.846 90.00 90.00 120.00 P 32 2 1 12
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 0.011263 0.006503 0.000000 0.00000
SCALE2 0.000000 0.013006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008414 0.00000
HETATM 1 N MSE A 1 70.284 3.035 2.521 1.00 20.53 N
HETATM 2 CA MSE A 1 71.276 3.859 3.273 1.00 19.90 C
HETATM 3 C MSE A 1 71.392 5.235 2.630 1.00 19.41 C
HETATM 4 O MSE A 1 71.595 5.353 1.417 1.00 19.94 O
HETATM 5 CB MSE A 1 72.641 3.174 3.305 1.00 20.48 C
(ATOM LINES ARE NOT SHOWN.)
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