HEADER HYDROLASE 22-OCT-09 2WWD
TITLE 3D-STRUCTURE OF THE MODULAR AUTOLYSIN LYTC FROM STREPTOCOCCUS
TITLE 2 PNEUMONIAE IN COMPLEX WITH PNEUMMOCOCCAL PEPTIDOGLYCAN FRAGMENT
CAVEAT 2WWD GLN A 618 HAS WRONG CHIRALITY AT ATOM CA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,4-BETA-N-ACETYLMURAMIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LYTC AUTOLYSIN;
COMPND 5 EC: 3.2.1.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 171101;
SOURCE 4 STRAIN: R6;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLCC14
KEYWDS HYDROLASE, GLYCOSIDASE, CHOLINE-BINDING PROTEINS
EXPDTA X-RAY DIFFRACTION
AUTHOR I.PEREZ-DORADO,R.SANLES,J.A.HERMOSO,A.GONZALEZ,A.GARCIA,P.GARCIA,
AUTHOR 2 J.L.GARCIA
REVDAT 7 20-DEC-23 2WWD 1 HETSYN SHEET LINK
REVDAT 6 29-JUL-20 2WWD 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 01-JUL-20 2WWD 1 CAVEAT COMPND REMARK HET
REVDAT 5 2 1 HETNAM FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 03-APR-13 2WWD 1 JRNL REMARK HETSYN
REVDAT 3 13-JUL-11 2WWD 1 VERSN
REVDAT 2 28-APR-10 2WWD 1 KEYWDS JRNL
REVDAT 1 21-APR-10 2WWD 0
JRNL AUTH I.PEREZ-DORADO,A.GONZALEZ,M.MORALES,R.SANLES,W.STRIKER,
JRNL AUTH 2 W.VOLLMER,S.MOBASHERY,J.L.GARCIA,M.MARTINEZ-RIPOLL,P.GARCIA,
JRNL AUTH 3 J.A.HERMOSO
JRNL TITL INSIGHTS INTO PNEUMOCOCCAL FRATRICIDE FROM THE CRYSTAL
JRNL TITL 2 STRUCTURES OF THE MODULAR KILLING FACTOR LYTC.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 576 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20400948
JRNL DOI 10.1038/NSMB.1817
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.MONTERROSO,J.L.SAIZ,P.GARCIA,J.L.GARCIA,M.MENENDEZ
REMARK 1 TITL INSIGHTS INTO THE STRUCTURE-FUNCTION RELATIONSHIPS OF
REMARK 1 TITL 2 PNEUMOCOCCAL CELL WALL LYSOZYMES, LYTC AND CPL- 1.
REMARK 1 REF J.BIOL.CHEM. V. 283 28618 2008
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 18667432
REMARK 1 DOI 10.1074/JBC.M802808200
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.MONTERROSO,C.LOPEZ-ZUMEL,J.L.GARCIA,J.L.SAIZ,P.GARCIA,
REMARK 1 AUTH 2 N.E.CAMPILLO,M.MENENDEZ
REMARK 1 TITL UNRAVELLING THE STRUCTURE OF THE PNEUMOCOCCAL AUTOLYTIC
REMARK 1 TITL 2 LYSOZYME.
REMARK 1 REF BIOCHEM.J. V. 391 41 2005
REMARK 1 REFN ISSN 0264-6021
REMARK 1 PMID 15943581
REMARK 1 DOI 10.1042/BJ20050612
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.GARCIA,M.PAZ GONZALEZ,E.GARCIA,J.L.GARCIA,R.LOPEZ
REMARK 1 TITL THE MOLECULAR CHARACTERIZATION OF THE FIRST AUTOLYTIC
REMARK 1 TITL 2 LYSOZYME OF STREPTOCOCCUS PNEUMONIAE REVEALS EVOLUTIONARY
REMARK 1 TITL 3 MOBILE DOMAINS.
REMARK 1 REF MOL.MICROBIOL. V. 33 128 1999
REMARK 1 REFN ISSN 0950-382X
REMARK 1 PMID 10411730
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 25982
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1925
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1897
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 152
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3653
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 138
REMARK 3 SOLVENT ATOMS : 136
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) : 38.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : 0.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.73000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.291
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.208
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.134
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3899 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5273 ; 1.097 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 431 ; 5.465 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 212 ;37.205 ;24.434
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 614 ;14.444 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;23.612 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 494 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3025 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1690 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2589 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 192 ; 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): 72 ; 0.211 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.148 ; 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): 2181 ; 0.542 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3395 ; 0.981 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2098 ; 1.158 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1878 ; 1.802 ; 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 37 A 76
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3182 -53.4008 3.5460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0382 T22: -0.0326
REMARK 3 T33: -0.0848 T12: -0.0273
REMARK 3 T13: -0.0006 T23: -0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 1.4282 L22: 4.0716
REMARK 3 L33: 3.7297 L12: -1.2355
REMARK 3 L13: -0.7335 L23: 0.1858
REMARK 3 S TENSOR
REMARK 3 S11: -0.0663 S12: 0.1623 S13: -0.0304
REMARK 3 S21: 0.3172 S22: 0.1602 S23: -0.0195
REMARK 3 S31: 0.2591 S32: 0.1184 S33: -0.0938
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 77 A 217
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5136 -16.2703 18.3963
REMARK 3 T TENSOR
REMARK 3 T11: 0.0209 T22: -0.0374
REMARK 3 T33: -0.0175 T12: -0.0344
REMARK 3 T13: -0.0320 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.2619 L22: 2.3662
REMARK 3 L33: 0.4722 L12: 0.6412
REMARK 3 L13: 0.1485 L23: 0.9195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0588 S12: -0.0331 S13: 0.0435
REMARK 3 S21: -0.1201 S22: 0.0700 S23: 0.0609
REMARK 3 S31: 0.0182 S32: 0.0197 S33: -0.0112
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 218 A 242
REMARK 3 ORIGIN FOR THE GROUP (A): 33.7124 21.7035 28.5084
REMARK 3 T TENSOR
REMARK 3 T11: -0.1437 T22: -0.0625
REMARK 3 T33: 0.2304 T12: -0.0589
REMARK 3 T13: -0.0350 T23: -0.1624
REMARK 3 L TENSOR
REMARK 3 L11: 5.9565 L22: 11.4282
REMARK 3 L33: 10.3428 L12: -5.6482
REMARK 3 L13: -5.2786 L23: 8.5951
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: -0.0059 S13: 0.3414
REMARK 3 S21: -0.1347 S22: -0.6668 S23: 0.9701
REMARK 3 S31: -0.1516 S32: -0.0861 S33: 0.6903
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 243 A 267
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8410 31.1129 33.0489
REMARK 3 T TENSOR
REMARK 3 T11: -0.0329 T22: -0.1221
REMARK 3 T33: 0.1414 T12: -0.0632
REMARK 3 T13: 0.1402 T23: -0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 7.4975 L22: 2.7944
REMARK 3 L33: 3.1545 L12: 0.4970
REMARK 3 L13: -1.4500 L23: -0.0155
REMARK 3 S TENSOR
REMARK 3 S11: 0.5791 S12: -0.3526 S13: 0.8101
REMARK 3 S21: 0.2118 S22: -0.2556 S23: -0.0134
REMARK 3 S31: -0.4455 S32: 0.2864 S33: -0.3234
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 268 A 365
REMARK 3 RESIDUE RANGE : A 381 A 468
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9399 14.5061 22.6326
REMARK 3 T TENSOR
REMARK 3 T11: -0.0341 T22: -0.0207
REMARK 3 T33: -0.0245 T12: 0.0059
REMARK 3 T13: 0.0262 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 1.8615 L22: 0.4488
REMARK 3 L33: 0.8365 L12: 0.3784
REMARK 3 L13: 0.2693 L23: 0.1732
REMARK 3 S TENSOR
REMARK 3 S11: 0.0254 S12: 0.1954 S13: -0.1032
REMARK 3 S21: -0.0244 S22: 0.0215 S23: -0.0593
REMARK 3 S31: 0.0023 S32: -0.0229 S33: -0.0469
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 : A 366 A 380
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0133 1.9002 8.7140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0198 T22: 0.0465
REMARK 3 T33: 0.0308 T12: 0.0599
REMARK 3 T13: -0.0775 T23: -0.1525
REMARK 3 L TENSOR
REMARK 3 L11: 1.7998 L22: 0.2358
REMARK 3 L33: 6.0100 L12: -0.4356
REMARK 3 L13: -2.6028 L23: 1.1710
REMARK 3 S TENSOR
REMARK 3 S11: 0.1679 S12: 0.5722 S13: -0.8409
REMARK 3 S21: -0.4009 S22: 0.2757 S23: -0.3135
REMARK 3 S31: 0.4192 S32: 0.6253 S33: -0.4436
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: THE FIRST 37 AA OF THE POLYPEPTIDE
REMARK 3 CHAIN WERE NOT MODELLED DUE TO POOR ELECTRON DENSITY. ATOM
REMARK 3 RECORD CONTAINS RESIDUAL B FACTORS ONLY.
REMARK 4
REMARK 4 2WWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1290041457.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27909
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 75.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2WW5
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.43500
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 ASN A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 GLU A 4
REMARK 465 VAL A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 THR A 8
REMARK 465 SER A 9
REMARK 465 GLN A 10
REMARK 465 ASP A 11
REMARK 465 THR A 12
REMARK 465 THR A 13
REMARK 465 THR A 14
REMARK 465 ALA A 15
REMARK 465 SER A 16
REMARK 465 SER A 17
REMARK 465 SER A 18
REMARK 465 SER A 19
REMARK 465 GLU A 20
REMARK 465 GLN A 21
REMARK 465 ASN A 22
REMARK 465 GLN A 23
REMARK 465 SER A 24
REMARK 465 SER A 25
REMARK 465 ASN A 26
REMARK 465 LYS A 27
REMARK 465 THR A 28
REMARK 465 GLN A 29
REMARK 465 THR A 30
REMARK 465 SER A 31
REMARK 465 ALA A 32
REMARK 465 GLU A 33
REMARK 465 VAL A 34
REMARK 465 GLN A 35
REMARK 465 THR A 36
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 ALA A 38 96.37 -173.43
REMARK 500 ASP A 43 79.85 -113.52
REMARK 500 ASP A 51 -93.81 -58.41
REMARK 500 ASP A 219 -83.56 -140.69
REMARK 500 ARG A 259 30.40 -93.51
REMARK 500 THR A 265 -162.02 -119.02
REMARK 500 SER A 303 104.91 -42.70
REMARK 500 GLU A 333 -12.84 -142.33
REMARK 500 THR A 413 -105.68 -111.70
REMARK 500 ARG A 414 4.32 -67.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GLN A 618
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AL" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WW5 RELATED DB: PDB
REMARK 900 3D-STRUCTURE OF THE MODULAR AUTOLYSIN LYTC FROM STREPTOCOCCUS
REMARK 900 PNEUMONIAE AT 1.6 A RESOLUTION
REMARK 900 RELATED ID: 2WWC RELATED DB: PDB
REMARK 900 3D-STRUCTURE OF THE MODULAR AUTOLYSIN LYTC FROM STREPTOCOCCUS
REMARK 900 PNEUMONIAE IN COMPLEX WITH SYNTHETIC PEPTIDOGLYCAN LIGAND
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ENTRY ACCESSION CODE CORRESPONDS TO THE IMMATURE PROTEIN
REMARK 999 WHICH POSSESSES A SIGNAL PEPTIDE OF 33 AMINO-ACIDS BUT THE
REMARK 999 STRUCTURE HERE REPORTED CORRESPONDS TO THE MATURE FORM.
REMARK 999 THE FIRST AMINO-ACID OF THE MATURE PROTEIN IS REFERED AS
REMARK 999 TO RESIDUE 1.
DBREF 2WWD A 1 468 UNP Q9Z4J8 Q9Z4J8_STRPN 34 501
SEQRES 1 A 468 ASN GLU THR GLU VAL ALA LYS THR SER GLN ASP THR THR
SEQRES 2 A 468 THR ALA SER SER SER SER GLU GLN ASN GLN SER SER ASN
SEQRES 3 A 468 LYS THR GLN THR SER ALA GLU VAL GLN THR ASN ALA ALA
SEQRES 4 A 468 ALA TYR TRP ASP GLY ASP TYR TYR VAL LYS ASP ASP GLY
SEQRES 5 A 468 SER LYS ALA GLN SER GLU TRP ILE PHE ASP ASN TYR TYR
SEQRES 6 A 468 LYS ALA TRP PHE TYR ILE ASN SER ASP GLY ARG TYR SER
SEQRES 7 A 468 GLN ASN GLU TRP HIS GLY ASN TYR TYR LEU LYS SER GLY
SEQRES 8 A 468 GLY TYR MET ALA GLN ASN GLU TRP ILE TYR ASP SER ASN
SEQRES 9 A 468 TYR LYS SER TRP PHE TYR LEU LYS SER ASP GLY ALA TYR
SEQRES 10 A 468 ALA HIS GLN GLU TRP GLN LEU ILE GLY ASN LYS TRP TYR
SEQRES 11 A 468 TYR PHE LYS LYS TRP GLY TYR MET ALA LYS SER GLN TRP
SEQRES 12 A 468 GLN GLY SER TYR PHE LEU ASN GLY GLN GLY ALA MET ILE
SEQRES 13 A 468 GLN ASN GLU TRP LEU TYR ASP PRO ALA TYR SER ALA TYR
SEQRES 14 A 468 PHE TYR LEU LYS SER ASP GLY THR TYR ALA ASN GLN GLU
SEQRES 15 A 468 TRP GLN LYS VAL GLY GLY LYS TRP TYR TYR PHE LYS LYS
SEQRES 16 A 468 TRP GLY TYR MET ALA ARG ASN GLU TRP GLN GLY ASN TYR
SEQRES 17 A 468 TYR LEU THR GLY SER GLY ALA MET ALA THR ASP GLU VAL
SEQRES 18 A 468 ILE MET ASP GLY ALA ARG TYR ILE PHE ALA ALA SER GLY
SEQRES 19 A 468 GLU LEU LYS GLU LYS LYS ASP LEU ASN VAL GLY TRP VAL
SEQRES 20 A 468 HIS ARG ASP GLY LYS ARG TYR PHE PHE ASN ASN ARG GLU
SEQRES 21 A 468 GLU GLN VAL GLY THR GLU HIS ALA LYS LYS ILE ILE ASP
SEQRES 22 A 468 ILE SER GLU HIS ASN GLY ARG ILE ASN ASP TRP LYS LYS
SEQRES 23 A 468 VAL ILE ASP GLU ASN GLU VAL ASP GLY VAL ILE VAL ARG
SEQRES 24 A 468 LEU GLY TYR SER GLY LYS GLU ASP LYS GLU LEU ALA HIS
SEQRES 25 A 468 ASN ILE LYS GLU LEU ASN ARG LEU GLY ILE PRO TYR GLY
SEQRES 26 A 468 VAL TYR LEU TYR THR TYR ALA GLU ASN GLU THR ASP ALA
SEQRES 27 A 468 GLU ASN ASP ALA LYS GLN THR ILE GLU LEU ILE LYS LYS
SEQRES 28 A 468 TYR ASN MET ASN LEU SER TYR PRO ILE TYR TYR ASP VAL
SEQRES 29 A 468 GLU ASN TRP GLU TYR VAL ASN LYS SER LYS ARG ALA PRO
SEQRES 30 A 468 SER ASP THR ASP THR TRP VAL LYS ILE ILE ASN LYS TYR
SEQRES 31 A 468 MET ASP THR MET LYS GLN ALA GLY TYR GLN ASN VAL TYR
SEQRES 32 A 468 VAL TYR SER TYR ARG SER LEU LEU GLN THR ARG LEU LYS
SEQRES 33 A 468 HIS PRO ASP ILE LEU LYS HIS VAL ASN TRP VAL ALA ALA
SEQRES 34 A 468 TYR THR ASN ALA LEU GLU TRP GLU ASN PRO TYR TYR SER
SEQRES 35 A 468 GLY GLU LYS GLY TRP GLN TYR THR SER SER GLU TYR MET
SEQRES 36 A 468 LYS GLY ILE GLN GLY ARG VAL ASP VAL SER VAL TRP TYR
HET MUB B 1 19
HET NAG B 2 14
HET GOL A 601 6
HET GOL A 602 6
HET GOL A 603 6
HET GOL A 604 6
HET GOL A 605 6
HET GOL A 606 6
HET GOL A 607 6
HET CHT A 608 7
HET CHT A 609 7
HET CHT A 610 7
HET CHT A 611 7
HET CHT A 612 7
HET CHT A 613 7
HET CHT A 614 7
HET ALA A 617 5
HET GLN A 618 9
HETNAM MUB N-ACETYL-ALPHA-MURAMIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
HETNAM CHT CHOLINE ION
HETNAM ALA ALANINE
HETNAM GLN GLUTAMINE
HETSYN MUB N-ACETYL-MURAMIC ACID; N-ACETYLMURAMIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 MUB C11 H19 N O8
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 GOL 7(C3 H8 O3)
FORMUL 10 CHT 7(C5 H14 N O 1+)
FORMUL 17 ALA C3 H7 N O2
FORMUL 18 GLN C5 H10 N2 O3
FORMUL 19 HOH *136(H2 O)
HELIX 1 1 LYS A 133 TYR A 137 5 5
HELIX 2 2 LYS A 194 TYR A 198 5 5
HELIX 3 3 SER A 275 GLY A 279 5 5
HELIX 4 4 ASP A 283 ASN A 291 1 9
HELIX 5 5 GLU A 309 GLY A 321 1 13
HELIX 6 6 ASN A 334 TYR A 352 1 19
HELIX 7 7 ASP A 379 ALA A 397 1 19
HELIX 8 8 ARG A 408 THR A 413 1 6
HELIX 9 9 HIS A 417 LYS A 422 1 6
SHEET 1 AA 2 TYR A 41 ASP A 43 0
SHEET 2 AA 2 TYR A 46 VAL A 48 -1 O TYR A 46 N ASP A 43
SHEET 1 AB 2 GLU A 58 ASP A 62 0
SHEET 2 AB 2 ALA A 67 ILE A 71 -1 O ALA A 67 N ASP A 62
SHEET 1 AC 2 GLU A 81 HIS A 83 0
SHEET 2 AC 2 TYR A 86 LEU A 88 -1 O TYR A 86 N HIS A 83
SHEET 1 AD 2 GLU A 98 ASP A 102 0
SHEET 2 AD 2 SER A 107 LEU A 111 -1 O SER A 107 N ASP A 102
SHEET 1 AE 2 GLU A 121 ILE A 125 0
SHEET 2 AE 2 LYS A 128 PHE A 132 -1 O LYS A 128 N ILE A 125
SHEET 1 AF 2 GLN A 142 GLN A 144 0
SHEET 2 AF 2 TYR A 147 LEU A 149 -1 O TYR A 147 N GLN A 144
SHEET 1 AG 2 GLU A 159 ASP A 163 0
SHEET 2 AG 2 ALA A 168 LEU A 172 -1 O ALA A 168 N ASP A 163
SHEET 1 AH 2 GLU A 182 VAL A 186 0
SHEET 2 AH 2 LYS A 189 PHE A 193 -1 O LYS A 189 N VAL A 186
SHEET 1 AI 2 GLU A 203 GLN A 205 0
SHEET 2 AI 2 TYR A 208 LEU A 210 -1 O TYR A 208 N GLN A 205
SHEET 1 AJ 3 GLU A 220 MET A 223 0
SHEET 2 AJ 3 ALA A 226 PHE A 230 -1 O ALA A 226 N MET A 223
SHEET 3 AJ 3 LEU A 236 ASP A 241 -1 N LYS A 237 O ILE A 229
SHEET 1 AK 3 GLY A 245 ARG A 249 0
SHEET 2 AK 3 LYS A 252 PHE A 256 -1 O LYS A 252 N ARG A 249
SHEET 3 AK 3 GLN A 262 VAL A 263 -1 O VAL A 263 N PHE A 255
SHEET 1 AL 9 LYS A 269 ILE A 274 0
SHEET 2 AL 9 VAL A 462 TYR A 468 -1 O ASP A 463 N ASP A 273
SHEET 3 AL 9 LYS A 445 GLU A 453 -1 O LYS A 445 N TYR A 468
SHEET 4 AL 9 VAL A 424 ALA A 428 1 O ASN A 425 N GLY A 446
SHEET 5 AL 9 VAL A 402 TYR A 407 1 O VAL A 404 N ASN A 425
SHEET 6 AL 9 ILE A 360 ASP A 363 1 O ILE A 360 N TYR A 403
SHEET 7 AL 9 TYR A 324 TYR A 329 1 O VAL A 326 N TYR A 361
SHEET 8 AL 9 GLY A 295 TYR A 302 1 O VAL A 296 N GLY A 325
SHEET 9 AL 9 LYS A 269 ILE A 274 0
LINK C ALA A 617 N GLN A 618 1555 1555 1.34
LINK N ALA A 617 C10 MUB B 1 1555 1555 1.33
LINK O4 MUB B 1 C1 NAG B 2 1555 1555 1.43
CRYST1 59.400 66.870 77.920 90.00 105.77 90.00 P 1 21 1 2
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 0.016835 0.000000 0.004754 0.00000
SCALE2 0.000000 0.014954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013336 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
