HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 08-DEC-09 3KZP
TITLE CRYSTAL STRUCTURE OF PUTATIVE DIGUANYLATE CYCLASE/PHOSPHODIESTERASE
TITLE 2 FROM LISTARIA MONOCYTIGENES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DIGUANYLATE CYCLASE/PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LMO0111 PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 3 ORGANISM_TAXID: 1639;
SOURCE 4 GENE: LMO0111;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS EAL-DOMAIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.M.KLIMECKA,M.CHRUSZCZ,M.D.ZIMMERMAN,M.KUDRITSKA,A.SAVCHENKO,
AUTHOR 2 A.EDWARDS,A.JOACHIMIAK,W.MINOR,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 3 GENOMICS (MCSG)
REVDAT 3 13-APR-22 3KZP 1 AUTHOR JRNL REMARK SEQADV
REVDAT 3 2 1 LINK
REVDAT 2 13-JUL-11 3KZP 1 VERSN
REVDAT 1 22-DEC-09 3KZP 0
JRNL AUTH M.M.KLIMECKA,M.CHRUSZCZ,M.D.ZIMMERMAN,M.KUDRITSKA,
JRNL AUTH 2 A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK,W.MINOR
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE DIGUANYLATE
JRNL TITL 2 CYCLASE/PHOSPHODIESTERASE FROM LISTARIA MONOCYTIGENES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 34327
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1714
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2221
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3771
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 408
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 1.44000
REMARK 3 B33 (A**2) : -1.55000
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): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.057
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3927 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2617 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5343 ; 1.750 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6422 ; 0.999 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 473 ; 6.303 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;41.118 ;24.754
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 683 ;13.975 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.007 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 606 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4317 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 797 ; 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): 2355 ; 0.959 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 932 ; 0.296 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3832 ; 1.617 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1572 ; 2.698 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1511 ; 4.135 ; 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 : 8
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 5 A 36
REMARK 3 ORIGIN FOR THE GROUP (A): 43.5750 48.3170 25.5280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0310 T22: 0.1011
REMARK 3 T33: 0.0765 T12: -0.0071
REMARK 3 T13: -0.0052 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 3.4807 L22: 5.2799
REMARK 3 L33: 3.4164 L12: 1.8724
REMARK 3 L13: -1.4941 L23: -1.6506
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: -0.1112 S13: 0.1369
REMARK 3 S21: -0.2674 S22: 0.1777 S23: 0.4599
REMARK 3 S31: 0.0031 S32: -0.2406 S33: -0.1556
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 37 A 142
REMARK 3 ORIGIN FOR THE GROUP (A): 58.3100 57.6270 23.8340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.0429
REMARK 3 T33: 0.0561 T12: -0.0197
REMARK 3 T13: 0.0001 T23: -0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 0.9596 L22: 0.9522
REMARK 3 L33: 1.6852 L12: 0.0296
REMARK 3 L13: -0.3545 L23: -0.4655
REMARK 3 S TENSOR
REMARK 3 S11: 0.0404 S12: -0.1799 S13: 0.0889
REMARK 3 S21: 0.0370 S22: -0.0255 S23: 0.0105
REMARK 3 S31: -0.2090 S32: 0.1389 S33: -0.0149
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 143 A 205
REMARK 3 ORIGIN FOR THE GROUP (A): 58.4450 38.7010 14.9630
REMARK 3 T TENSOR
REMARK 3 T11: 0.0703 T22: 0.0209
REMARK 3 T33: 0.0751 T12: 0.0014
REMARK 3 T13: 0.0149 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 0.8734 L22: 0.7050
REMARK 3 L33: 2.2904 L12: -0.3368
REMARK 3 L13: -0.3475 L23: 0.2617
REMARK 3 S TENSOR
REMARK 3 S11: -0.0397 S12: -0.0090 S13: -0.1705
REMARK 3 S21: 0.0419 S22: 0.0328 S23: 0.0612
REMARK 3 S31: 0.2427 S32: 0.0663 S33: 0.0069
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 206 A 235
REMARK 3 ORIGIN FOR THE GROUP (A): 46.0540 34.4280 21.1060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0896 T22: 0.1273
REMARK 3 T33: 0.1375 T12: -0.0561
REMARK 3 T13: 0.0181 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 6.2121 L22: 12.2807
REMARK 3 L33: 2.4216 L12: -8.0570
REMARK 3 L13: -2.4438 L23: 3.5547
REMARK 3 S TENSOR
REMARK 3 S11: 0.1261 S12: 0.0928 S13: -0.6814
REMARK 3 S21: -0.1575 S22: -0.4059 S23: 0.8315
REMARK 3 S31: 0.2241 S32: -0.4244 S33: 0.2798
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 5 B 36
REMARK 3 ORIGIN FOR THE GROUP (A): 75.8700 47.8170 -10.6270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0333 T22: 0.1241
REMARK 3 T33: 0.1014 T12: -0.0108
REMARK 3 T13: -0.0074 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 3.9627 L22: 5.6215
REMARK 3 L33: 3.8179 L12: -1.7002
REMARK 3 L13: -1.6481 L23: 1.9992
REMARK 3 S TENSOR
REMARK 3 S11: 0.0507 S12: 0.1131 S13: 0.1526
REMARK 3 S21: 0.2099 S22: 0.1409 S23: -0.5574
REMARK 3 S31: 0.0127 S32: 0.3139 S33: -0.1916
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 37 B 142
REMARK 3 ORIGIN FOR THE GROUP (A): 61.2300 57.3250 -9.2640
REMARK 3 T TENSOR
REMARK 3 T11: 0.1097 T22: 0.0657
REMARK 3 T33: 0.0771 T12: 0.0200
REMARK 3 T13: 0.0105 T23: 0.0502
REMARK 3 L TENSOR
REMARK 3 L11: 1.3079 L22: 0.7994
REMARK 3 L33: 2.0936 L12: -0.2206
REMARK 3 L13: -0.5981 L23: 0.9790
REMARK 3 S TENSOR
REMARK 3 S11: 0.1144 S12: 0.2876 S13: 0.1842
REMARK 3 S21: -0.1120 S22: -0.0514 S23: -0.0353
REMARK 3 S31: -0.3209 S32: -0.1373 S33: -0.0631
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 143 B 205
REMARK 3 ORIGIN FOR THE GROUP (A): 61.2950 38.4670 0.0750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0876 T22: 0.0146
REMARK 3 T33: 0.0630 T12: 0.0098
REMARK 3 T13: 0.0187 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 1.5908 L22: 1.3567
REMARK 3 L33: 3.1257 L12: -0.2216
REMARK 3 L13: 0.3996 L23: -0.5222
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.0393 S13: -0.2172
REMARK 3 S21: -0.0380 S22: 0.0389 S23: -0.0295
REMARK 3 S31: 0.3653 S32: 0.1370 S33: -0.0273
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 206 B 235
REMARK 3 ORIGIN FOR THE GROUP (A): 73.9550 34.4190 -5.8960
REMARK 3 T TENSOR
REMARK 3 T11: 0.1594 T22: 0.1211
REMARK 3 T33: 0.1861 T12: 0.0724
REMARK 3 T13: 0.0624 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 6.7964 L22: 9.8720
REMARK 3 L33: 7.0364 L12: 2.3299
REMARK 3 L13: -2.2493 L23: -3.5453
REMARK 3 S TENSOR
REMARK 3 S11: -0.2758 S12: -0.0059 S13: -1.0108
REMARK 3 S21: 0.2070 S22: 0.0182 S23: -0.0650
REMARK 3 S31: 0.7697 S32: 0.1955 S33: 0.2575
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
REMARK 4
REMARK 4 3KZP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056649.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.9
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) : 0.9786
REMARK 200 MONOCHROMATOR : SI-111 CHANNEL
REMARK 200 OPTICS : MIRROR
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-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34443
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 93.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : 0.09100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.8850
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.51300
REMARK 200 R SYM FOR SHELL (I) : 0.51300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, SHELXD, DM, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CA ACETATE, 0.1 M NA CACODILATE,
REMARK 280 9% PEG 8K, PH 6.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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 29.88300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.10500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.02000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.10500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.88300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.02000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 4640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 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 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 1
REMARK 465 GLY A 2
REMARK 465 LEU A 3
REMARK 465 MSE A 4
REMARK 465 MSE B 1
REMARK 465 GLY B 2
REMARK 465 LEU B 3
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 210 CG CD CE NZ
REMARK 470 GLU A 211 CG CD OE1 OE2
REMARK 470 GLU A 217 CG CD OE1 OE2
REMARK 470 MSE B 4 CG SE CE
REMARK 470 LYS B 5 CG CD CE NZ
REMARK 470 GLU B 88 CG CD OE1 OE2
REMARK 470 LYS B 210 CG CD CE NZ
REMARK 470 GLU B 211 CG CD OE1 OE2
REMARK 470 GLU B 217 CG CD OE1 OE2
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 70 79.48 -118.00
REMARK 500 PHE B 224 168.58 176.21
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 CA A 240 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 25 OE2
REMARK 620 2 ASN A 78 OD1 86.9
REMARK 620 3 GLU A 106 OE1 95.4 94.9
REMARK 620 4 ASP A 147 OD2 159.8 105.2 99.5
REMARK 620 5 HOH A 303 O 68.3 88.2 163.2 95.5
REMARK 620 6 HOH A 472 O 80.8 163.9 96.6 83.9 77.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 237 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 25 OE2
REMARK 620 2 ASN B 78 OD1 89.6
REMARK 620 3 GLU B 106 OE1 96.7 95.3
REMARK 620 4 ASP B 147 OD2 159.4 102.7 98.5
REMARK 620 5 HOH B 300 O 68.8 92.1 163.8 93.9
REMARK 620 6 HOH B 338 O 79.7 164.5 97.0 84.7 73.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 236
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 239
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 236
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 238
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 239
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC7867 RELATED DB: TARGETDB
DBREF 3KZP A 2 235 UNP Q8YAK7 Q8YAK7_LISMO 2 235
DBREF 3KZP B 2 235 UNP Q8YAK7 Q8YAK7_LISMO 2 235
SEQADV 3KZP MSE A 1 UNP Q8YAK7 INITIATING METHIONINE
SEQADV 3KZP MSE B 1 UNP Q8YAK7 INITIATING METHIONINE
SEQRES 1 A 235 MSE GLY LEU MSE LYS PHE GLN LEU PHE ILE GLN PRO LYS
SEQRES 2 A 235 LEU ASP VAL LEU GLN GLY ASN ILE VAL GLU TYR GLU ILE
SEQRES 3 A 235 LEU LEU ARG ASP ASP SER ALA VAL PRO ARG PHE PRO LEU
SEQRES 4 A 235 SER GLU LEU GLU ALA VAL LEU ALA ASP GLU GLU LEU TYR
SEQRES 5 A 235 LEU ALA PHE SER GLU TRP PHE SER GLU ALA PHE LEU ASP
SEQRES 6 A 235 VAL LEU LYS LYS TYR PRO ASN ASP ARG PHE ALA ILE ASN
SEQRES 7 A 235 ILE ALA PRO GLN GLN LEU PHE TYR ILE GLU THR LEU HIS
SEQRES 8 A 235 TRP LEU ASP LYS LEU LYS SER GLU SER HIS ARG ILE THR
SEQRES 9 A 235 VAL GLU MSE THR GLU ASP ILE PHE ASP VAL PRO GLY HIS
SEQRES 10 A 235 LYS ARG HIS LEU ASN ALA ASN ASP LYS ASN ALA PHE ILE
SEQRES 11 A 235 LEU ASN LYS ILE LYS VAL ILE HIS GLY LEU GLY TYR HIS
SEQRES 12 A 235 ILE ALA ILE ASP ASP VAL SER CYS GLY LEU ASN SER LEU
SEQRES 13 A 235 GLU ARG VAL MSE SER TYR LEU PRO TYR ILE ILE GLU ILE
SEQRES 14 A 235 LYS PHE SER LEU ILE HIS PHE LYS ASN ILE PRO LEU GLU
SEQRES 15 A 235 ASP LEU LEU LEU PHE ILE LYS ALA TRP ALA ASN PHE ALA
SEQRES 16 A 235 GLN LYS ASN LYS LEU ASP PHE VAL VAL GLU GLY ILE GLU
SEQRES 17 A 235 THR LYS GLU THR MSE THR LEU LEU GLU SER HIS GLY VAL
SEQRES 18 A 235 SER ILE PHE GLN GLY TYR LEU VAL ASN LYS PRO PHE PRO
SEQRES 19 A 235 VAL
SEQRES 1 B 235 MSE GLY LEU MSE LYS PHE GLN LEU PHE ILE GLN PRO LYS
SEQRES 2 B 235 LEU ASP VAL LEU GLN GLY ASN ILE VAL GLU TYR GLU ILE
SEQRES 3 B 235 LEU LEU ARG ASP ASP SER ALA VAL PRO ARG PHE PRO LEU
SEQRES 4 B 235 SER GLU LEU GLU ALA VAL LEU ALA ASP GLU GLU LEU TYR
SEQRES 5 B 235 LEU ALA PHE SER GLU TRP PHE SER GLU ALA PHE LEU ASP
SEQRES 6 B 235 VAL LEU LYS LYS TYR PRO ASN ASP ARG PHE ALA ILE ASN
SEQRES 7 B 235 ILE ALA PRO GLN GLN LEU PHE TYR ILE GLU THR LEU HIS
SEQRES 8 B 235 TRP LEU ASP LYS LEU LYS SER GLU SER HIS ARG ILE THR
SEQRES 9 B 235 VAL GLU MSE THR GLU ASP ILE PHE ASP VAL PRO GLY HIS
SEQRES 10 B 235 LYS ARG HIS LEU ASN ALA ASN ASP LYS ASN ALA PHE ILE
SEQRES 11 B 235 LEU ASN LYS ILE LYS VAL ILE HIS GLY LEU GLY TYR HIS
SEQRES 12 B 235 ILE ALA ILE ASP ASP VAL SER CYS GLY LEU ASN SER LEU
SEQRES 13 B 235 GLU ARG VAL MSE SER TYR LEU PRO TYR ILE ILE GLU ILE
SEQRES 14 B 235 LYS PHE SER LEU ILE HIS PHE LYS ASN ILE PRO LEU GLU
SEQRES 15 B 235 ASP LEU LEU LEU PHE ILE LYS ALA TRP ALA ASN PHE ALA
SEQRES 16 B 235 GLN LYS ASN LYS LEU ASP PHE VAL VAL GLU GLY ILE GLU
SEQRES 17 B 235 THR LYS GLU THR MSE THR LEU LEU GLU SER HIS GLY VAL
SEQRES 18 B 235 SER ILE PHE GLN GLY TYR LEU VAL ASN LYS PRO PHE PRO
SEQRES 19 B 235 VAL
MODRES 3KZP MSE A 107 MET SELENOMETHIONINE
MODRES 3KZP MSE A 160 MET SELENOMETHIONINE
MODRES 3KZP MSE A 213 MET SELENOMETHIONINE
MODRES 3KZP MSE B 4 MET SELENOMETHIONINE
MODRES 3KZP MSE B 107 MET SELENOMETHIONINE
MODRES 3KZP MSE B 160 MET SELENOMETHIONINE
MODRES 3KZP MSE B 213 MET SELENOMETHIONINE
HET MSE A 107 8
HET MSE A 160 8
HET MSE A 213 8
HET MSE B 4 5
HET MSE B 107 8
HET MSE B 160 8
HET MSE B 213 8
HET CL A 236 1
HET CL A 237 1
HET CL A 238 1
HET CL A 239 1
HET CA A 240 1
HET CAC A 241 5
HET CL B 236 1
HET CA B 237 1
HET CL B 238 1
HET CAC B 239 5
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
HETNAM CAC CACODYLATE ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 3 CL 6(CL 1-)
FORMUL 7 CA 2(CA 2+)
FORMUL 8 CAC 2(C2 H6 AS O2 1-)
FORMUL 13 HOH *408(H2 O)
HELIX 1 1 PRO A 38 ALA A 47 1 10
HELIX 2 2 ASP A 48 TYR A 70 1 23
HELIX 3 3 ALA A 80 PHE A 85 5 6
HELIX 4 4 TYR A 86 LEU A 96 1 11
HELIX 5 5 LYS A 97 HIS A 101 5 5
HELIX 6 6 PRO A 115 ARG A 119 5 5
HELIX 7 7 ASN A 122 LEU A 140 1 19
HELIX 8 8 SER A 155 LEU A 163 1 9
HELIX 9 9 PRO A 164 ILE A 166 5 3
HELIX 10 10 ILE A 174 LYS A 177 5 4
HELIX 11 11 PRO A 180 ASN A 198 1 19
HELIX 12 12 LYS A 210 HIS A 219 1 10
HELIX 13 13 PRO B 38 ALA B 47 1 10
HELIX 14 14 ASP B 48 TYR B 70 1 23
HELIX 15 15 ALA B 80 PHE B 85 5 6
HELIX 16 16 TYR B 86 LEU B 96 1 11
HELIX 17 17 LYS B 97 HIS B 101 5 5
HELIX 18 18 PRO B 115 ARG B 119 5 5
HELIX 19 19 ASN B 122 LEU B 140 1 19
HELIX 20 20 SER B 155 LEU B 163 1 9
HELIX 21 21 PRO B 164 ILE B 166 5 3
HELIX 22 22 ILE B 174 LYS B 177 5 4
HELIX 23 23 PRO B 180 ASN B 198 1 19
HELIX 24 24 THR B 209 HIS B 219 1 11
SHEET 1 A 9 GLN A 225 LEU A 228 0
SHEET 2 A 9 ASP A 201 ILE A 207 1 N PHE A 202 O GLN A 225
SHEET 3 A 9 GLU A 168 SER A 172 1 N PHE A 171 O VAL A 203
SHEET 4 A 9 HIS A 143 ILE A 146 1 N ILE A 146 O LYS A 170
SHEET 5 A 9 ILE A 103 MSE A 107 1 N MSE A 107 O ALA A 145
SHEET 6 A 9 PHE A 75 ILE A 79 1 N ILE A 77 O GLU A 106
SHEET 7 A 9 ILE A 21 ARG A 29 1 N ILE A 26 O ALA A 76
SHEET 8 A 9 GLN A 7 LEU A 14 -1 N LYS A 13 O VAL A 22
SHEET 9 A 9 PHE A 233 PRO A 234 -1 O PHE A 233 N ILE A 10
SHEET 1 B 9 GLN B 225 LEU B 228 0
SHEET 2 B 9 ASP B 201 ILE B 207 1 N VAL B 204 O TYR B 227
SHEET 3 B 9 GLU B 168 SER B 172 1 N ILE B 169 O VAL B 203
SHEET 4 B 9 HIS B 143 ILE B 146 1 N ILE B 146 O LYS B 170
SHEET 5 B 9 ILE B 103 MSE B 107 1 N VAL B 105 O HIS B 143
SHEET 6 B 9 PHE B 75 ILE B 79 1 N ILE B 77 O GLU B 106
SHEET 7 B 9 ILE B 21 ARG B 29 1 N ILE B 26 O ALA B 76
SHEET 8 B 9 GLN B 7 LEU B 14 -1 N LYS B 13 O VAL B 22
SHEET 9 B 9 PHE B 233 PRO B 234 -1 O PHE B 233 N ILE B 10
LINK C MSE A 107 N THR A 108 1555 1555 1.32
LINK C MSE A 160 N SER A 161 1555 1555 1.32
LINK C MSE A 213 N THR A 214 1555 1555 1.33
LINK C MSE B 4 N LYS B 5 1555 1555 1.31
LINK C MSE B 107 N THR B 108 1555 1555 1.34
LINK C MSE B 160 N SER B 161 1555 1555 1.34
LINK C MSE B 213 N THR B 214 1555 1555 1.33
LINK OE2 GLU A 25 CA CA A 240 1555 1555 2.36
LINK OD1 ASN A 78 CA CA A 240 1555 1555 2.38
LINK OE1 GLU A 106 CA CA A 240 1555 1555 2.32
LINK OD2 ASP A 147 CA CA A 240 1555 1555 2.35
LINK CA CA A 240 O HOH A 303 1555 1555 2.63
LINK CA CA A 240 O HOH A 472 1555 1555 2.55
LINK OE2 GLU B 25 CA CA B 237 1555 1555 2.35
LINK OD1 ASN B 78 CA CA B 237 1555 1555 2.42
LINK OE1 GLU B 106 CA CA B 237 1555 1555 2.29
LINK OD2 ASP B 147 CA CA B 237 1555 1555 2.34
LINK CA CA B 237 O HOH B 300 1555 1555 2.58
LINK CA CA B 237 O HOH B 338 1555 1555 2.47
SITE 1 AC1 4 SER A 222 ILE A 223 HOH A 294 HOH A 343
SITE 1 AC2 4 LEU A 28 ASN A 78 HOH A 280 HOH A 382
SITE 1 AC3 2 SER A 150 SER B 150
SITE 1 AC4 5 PHE A 176 ASN A 178 ILE A 179 HOH A 371
SITE 2 AC4 5 MSE B 160
SITE 1 AC5 6 GLU A 25 ASN A 78 GLU A 106 ASP A 147
SITE 2 AC5 6 HOH A 303 HOH A 472
SITE 1 AC6 4 ARG A 74 HOH A 320 HOH A 470 HOH A 507
SITE 1 AC7 3 LEU B 28 ASN B 78 HOH B 271
SITE 1 AC8 6 GLU B 25 ASN B 78 GLU B 106 ASP B 147
SITE 2 AC8 6 HOH B 300 HOH B 338
SITE 1 AC9 4 PHE B 85 TYR B 86 ILE B 87 HIS B 117
SITE 1 BC1 2 ARG B 74 HOH B 267
CRYST1 59.766 92.040 96.210 90.00 90.00 90.00 P 21 21 21 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 0.016730 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010870 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010390 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
