HEADER TRANSCRIPTION REGULATOR 13-MAR-08 3CJN
TITLE CRYSTAL STRUCTURE OF TRANSCRIPTIONAL REGULATOR, MARR FAMILY, FROM
TITLE 2 SILICIBACTER POMEROYI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR, MARR FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SILICIBACTER POMEROYI DSS-3;
SOURCE 3 ORGANISM_TAXID: 246200;
SOURCE 4 STRAIN: DSS-3 / DSM 15171;
SOURCE 5 ATCC: 700808;
SOURCE 6 GENE: SPO1458;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS TRANSCRIPTIONAL REGULATOR, MARR FAMILY, SILICIBACTER POMEROYI,
KEYWDS 2 STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST
KEYWDS 3 CENTER FOR STRUCTURAL GENOMICS, MCSG, DNA-BINDING, TRANSCRIPTION
KEYWDS 4 REGULATION, TRANSCRIPTION REGULATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,L.VOLKART,L.FREEMAN,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 3 13-JUL-11 3CJN 1 VERSN
REVDAT 2 24-FEB-09 3CJN 1 VERSN
REVDAT 1 25-MAR-08 3CJN 0
JRNL AUTH C.CHANG,L.VOLKART,L.FREEMAN,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF MARR FAMILY TRANSCRIPTIONAL REGULATOR
JRNL TITL 2 FROM SILICIBACTER POMEROYI.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 12819
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 624
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 864
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE SET COUNT : 36
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1133
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 142
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 28.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.75000
REMARK 3 B22 (A**2) : -0.75000
REMARK 3 B33 (A**2) : 1.50000
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): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.092
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.913
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1172 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1583 ; 1.282 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 148 ; 5.126 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ;22.835 ;21.923
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 209 ;12.965 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;17.392 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 178 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 880 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 535 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 821 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 106 ; 0.132 ; 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): 64 ; 0.266 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.176 ; 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): 764 ; 0.857 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1169 ; 1.329 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 463 ; 2.006 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 414 ; 2.881 ; 4.500
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 : 4
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 12 A 46
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7941 20.8937 22.8327
REMARK 3 T TENSOR
REMARK 3 T11: -0.0855 T22: -0.0766
REMARK 3 T33: -0.0743 T12: -0.0044
REMARK 3 T13: -0.0521 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 5.6368 L22: 1.9477
REMARK 3 L33: 11.1979 L12: -0.0487
REMARK 3 L13: -6.4319 L23: -0.9280
REMARK 3 S TENSOR
REMARK 3 S11: -0.1328 S12: 0.0160 S13: 0.2256
REMARK 3 S21: 0.1154 S22: 0.1242 S23: 0.0041
REMARK 3 S31: -0.1113 S32: -0.2850 S33: 0.0086
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 47 A 112
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2192 30.3322 30.0672
REMARK 3 T TENSOR
REMARK 3 T11: -0.1113 T22: -0.0854
REMARK 3 T33: -0.0329 T12: -0.0056
REMARK 3 T13: -0.0357 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 5.1725 L22: 2.3664
REMARK 3 L33: 3.9984 L12: 1.2373
REMARK 3 L13: -2.3614 L23: 0.2687
REMARK 3 S TENSOR
REMARK 3 S11: -0.0937 S12: 0.0654 S13: 0.0642
REMARK 3 S21: -0.1900 S22: 0.0665 S23: 0.0912
REMARK 3 S31: -0.1485 S32: -0.1511 S33: 0.0272
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 113 A 135
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7760 28.5663 37.7967
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: 0.0206
REMARK 3 T33: 0.0054 T12: 0.0297
REMARK 3 T13: -0.0666 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 17.3069 L22: 0.0608
REMARK 3 L33: 2.8986 L12: 0.9291
REMARK 3 L13: -4.9080 L23: -0.3920
REMARK 3 S TENSOR
REMARK 3 S11: -0.2421 S12: -0.5449 S13: 0.7257
REMARK 3 S21: 0.0799 S22: 0.3126 S23: -0.0707
REMARK 3 S31: 0.2059 S32: 0.1366 S33: -0.0705
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 136 A 159
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4731 37.8468 21.0356
REMARK 3 T TENSOR
REMARK 3 T11: -0.0573 T22: -0.1655
REMARK 3 T33: 0.0164 T12: -0.0096
REMARK 3 T13: -0.0208 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 8.7764 L22: 2.0207
REMARK 3 L33: 4.6672 L12: -0.9485
REMARK 3 L13: 5.0470 L23: 0.1590
REMARK 3 S TENSOR
REMARK 3 S11: 0.0549 S12: 0.2712 S13: 0.3255
REMARK 3 S21: -0.1319 S22: -0.0419 S23: -0.5277
REMARK 3 S31: 0.0336 S32: 0.2562 S33: -0.0130
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 3CJN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-08.
REMARK 100 THE RCSB ID CODE IS RCSB046856.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-07
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-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97935
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12941
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 : 21.000
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 77.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.80
REMARK 200 R MERGE FOR SHELL (I) : 0.47200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 14.500
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 (%): 45.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 SUCCINIC ACID PH 7.0, 12 % PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 21.59850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.98800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.98800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.39775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.98800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.98800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 10.79925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.98800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.98800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 32.39775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.98800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.98800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 10.79925
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 21.59850
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 43.19700
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 286 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 342 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 ASP A 6
REMARK 465 GLN A 7
REMARK 465 THR A 8
REMARK 465 GLU A 9
REMARK 465 GLN A 10
REMARK 465 LEU A 11
REMARK 465 SER A 99
REMARK 465 ASP A 100
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 12 CG CD NE CZ NH1 NH2
REMARK 470 THR A 43 OG1 CG2
REMARK 470 ASP A 101 CG OD1 OD2
REMARK 470 GLN A 102 CG CD OE1 NE2
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 342 DISTANCE = 5.86 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC88806 RELATED DB: TARGETDB
DBREF 3CJN A 1 159 UNP Q5LTF6 Q5LTF6_SILPO 1 159
SEQADV 3CJN SER A -2 UNP Q5LTF6 EXPRESSION TAG
SEQADV 3CJN ASN A -1 UNP Q5LTF6 EXPRESSION TAG
SEQADV 3CJN ALA A 0 UNP Q5LTF6 EXPRESSION TAG
SEQRES 1 A 162 SER ASN ALA MSE ALA GLU SER THR ASP GLN THR GLU GLN
SEQRES 2 A 162 LEU ARG GLU LEU ALA GLU ILE GLY LEU GLU GLY TYR ALA
SEQRES 3 A 162 PRO TYR LEU MSE ASN ARG ILE MSE GLY ARG TYR ASN ALA
SEQRES 4 A 162 ASN LEU ARG LYS GLU MSE THR ALA LEU GLY LEU SER THR
SEQRES 5 A 162 ALA LYS MSE ARG ALA LEU ALA ILE LEU SER ALA LYS ASP
SEQRES 6 A 162 GLY LEU PRO ILE GLY THR LEU GLY ILE PHE ALA VAL VAL
SEQRES 7 A 162 GLU GLN SER THR LEU SER ARG ALA LEU ASP GLY LEU GLN
SEQRES 8 A 162 ALA ASP GLY LEU VAL ARG ARG GLU VAL ASP SER ASP ASP
SEQRES 9 A 162 GLN ARG SER SER ARG VAL TYR LEU THR PRO ALA GLY ARG
SEQRES 10 A 162 ALA VAL TYR ASP ARG LEU TRP PRO HIS MSE ARG ALA SER
SEQRES 11 A 162 HIS ASP ARG MSE PHE GLN GLY ILE THR PRO GLN GLU ARG
SEQRES 12 A 162 GLN ALA PHE LEU ALA THR LEU ASN LYS MSE LEU ALA ASN
SEQRES 13 A 162 ILE ARG VAL HIS GLU ILE
MODRES 3CJN MSE A 27 MET SELENOMETHIONINE
MODRES 3CJN MSE A 31 MET SELENOMETHIONINE
MODRES 3CJN MSE A 42 MET SELENOMETHIONINE
MODRES 3CJN MSE A 52 MET SELENOMETHIONINE
MODRES 3CJN MSE A 124 MET SELENOMETHIONINE
MODRES 3CJN MSE A 131 MET SELENOMETHIONINE
MODRES 3CJN MSE A 150 MET SELENOMETHIONINE
HET MSE A 27 8
HET MSE A 31 8
HET MSE A 42 8
HET MSE A 52 8
HET MSE A 124 8
HET MSE A 131 8
HET MSE A 150 8
HET PO4 A 201 5
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 PO4 O4 P 3-
FORMUL 3 HOH *142(H2 O)
HELIX 1 1 GLU A 13 GLY A 18 1 6
HELIX 2 2 LEU A 19 GLY A 21 5 3
HELIX 3 3 TYR A 22 LYS A 40 1 19
HELIX 4 4 GLU A 41 GLY A 46 1 6
HELIX 5 5 SER A 48 LYS A 61 1 14
HELIX 6 6 ILE A 66 VAL A 74 1 9
HELIX 7 7 GLU A 76 ASP A 90 1 15
HELIX 8 8 THR A 110 PHE A 132 1 23
HELIX 9 9 THR A 136 ARG A 155 1 20
SHEET 1 A 3 LEU A 64 PRO A 65 0
SHEET 2 A 3 SER A 105 LEU A 109 -1 O VAL A 107 N LEU A 64
SHEET 3 A 3 VAL A 93 VAL A 97 -1 N GLU A 96 O ARG A 106
LINK C LEU A 26 N MSE A 27 1555 1555 1.33
LINK C MSE A 27 N ASN A 28 1555 1555 1.34
LINK C ILE A 30 N MSE A 31 1555 1555 1.34
LINK C MSE A 31 N GLY A 32 1555 1555 1.33
LINK C GLU A 41 N MSE A 42 1555 1555 1.34
LINK C MSE A 42 N THR A 43 1555 1555 1.33
LINK C LYS A 51 N MSE A 52 1555 1555 1.33
LINK C MSE A 52 N ARG A 53 1555 1555 1.33
LINK C HIS A 123 N MSE A 124 1555 1555 1.33
LINK C MSE A 124 N ARG A 125 1555 1555 1.34
LINK C ARG A 130 N MSE A 131 1555 1555 1.34
LINK C MSE A 131 N PHE A 132 1555 1555 1.34
LINK C LYS A 149 N MSE A 150 1555 1555 1.32
LINK C MSE A 150 N LEU A 151 1555 1555 1.33
SITE 1 AC1 6 ARG A 29 ARG A 33 ARG A 155 HIS A 157
SITE 2 AC1 6 HOH A 211 HOH A 285
CRYST1 87.976 87.976 43.197 90.00 90.00 90.00 P 43 21 2 8
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 0.011367 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011367 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023150 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
