HEADER HYDROLASE 14-SEP-05 2B0P
TITLE TRUNCATED S. AUREUS LYTM, P212121 CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCYL-GLYCINE ENDOPEPTIDASE LYTM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AUTOLYSIN LYTM;
COMPND 5 EC: 3.4.24.75;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: LYTM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS LYTM, LYSOSTAPHIN, PEPTIDOGLYCAN AMIDASE, PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FIRCZUK,A.MUCHA,M.BOCHTLER
REVDAT 4 23-AUG-23 2B0P 1 REMARK LINK
REVDAT 3 13-JUL-11 2B0P 1 VERSN
REVDAT 2 25-MAR-08 2B0P 1 REMARK VERSN
REVDAT 1 10-JAN-06 2B0P 0
JRNL AUTH M.FIRCZUK,A.MUCHA,M.BOCHTLER
JRNL TITL CRYSTAL STRUCTURES OF ACTIVE LYTM.
JRNL REF J.MOL.BIOL. V. 354 578 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16269153
JRNL DOI 10.1016/J.JMB.2005.09.082
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.G.ODINTSOV,I.SABALA,M.MARCYJANIAK,M.BOCHTLER
REMARK 1 TITL LATENT LYTM AT 1.3A RESOLUTION.
REMARK 1 REF J.MOL.BIOL. V. 335 775 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 14687573
REMARK 1 DOI 10.1016/J.JMB.2003.11.009
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39977
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2082
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2849
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 170
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1980
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 385
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 13.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.04000
REMARK 3 B22 (A**2) : -0.46000
REMARK 3 B33 (A**2) : -1.58000
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): 0.077
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.205
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2051 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1653 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2787 ; 1.703 ; 1.909
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3858 ; 4.003 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 256 ; 7.232 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 274 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2396 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 426 ; 0.015 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 365 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1856 ; 0.296 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 997 ; 0.114 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 260 ; 0.174 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.094 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 5 ; 0.082 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 39 ; 0.332 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.212 ; 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): 1275 ; 1.075 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2014 ; 1.668 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 776 ; 2.616 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 773 ; 3.884 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 188 A 316
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2780 -3.7800 0.3210
REMARK 3 T TENSOR
REMARK 3 T11: 0.0002 T22: 0.1962
REMARK 3 T33: 0.1806 T12: 0.0046
REMARK 3 T13: -0.0037 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.2403 L22: 1.0336
REMARK 3 L33: 1.2332 L12: 0.0854
REMARK 3 L13: 0.1711 L23: 0.4367
REMARK 3 S TENSOR
REMARK 3 S11: 0.0103 S12: -0.0477 S13: 0.0174
REMARK 3 S21: 0.0006 S22: -0.0058 S23: -0.0420
REMARK 3 S31: 0.0404 S32: -0.0278 S33: -0.0045
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 188 B 316
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7030 -13.1700 -26.4790
REMARK 3 T TENSOR
REMARK 3 T11: 0.0200 T22: 0.1818
REMARK 3 T33: 0.1888 T12: -0.0073
REMARK 3 T13: 0.0020 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.4382 L22: 0.8072
REMARK 3 L33: 0.7195 L12: 0.0199
REMARK 3 L13: -0.0222 L23: 0.0179
REMARK 3 S TENSOR
REMARK 3 S11: 0.0107 S12: 0.0297 S13: -0.0326
REMARK 3 S21: 0.0168 S22: 0.0011 S23: -0.0022
REMARK 3 S31: 0.0082 S32: -0.0135 S33: -0.0119
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2B0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034529.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42130
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.25600
REMARK 200 R SYM FOR SHELL (I) : 0.25600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: 1QWY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 CACODYLATE, 0.1 M SODIUM ACETATE, PH 6.8, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 294K
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 16.04650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.02450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.13050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.02450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.04650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.13050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 183
REMARK 465 ALA A 184
REMARK 465 HIS A 185
REMARK 465 ALA A 186
REMARK 465 LYS A 187
REMARK 465 MET B 183
REMARK 465 ALA B 184
REMARK 465 HIS B 185
REMARK 465 ALA B 186
REMARK 465 LYS B 187
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP B 228 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 253 59.41 -94.70
REMARK 500 ASN A 262 -121.58 -87.15
REMARK 500 ALA B 234 105.40 -161.38
REMARK 500 ASN B 262 -114.93 -89.90
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 ZN A 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 210 NE2
REMARK 620 2 ASP A 214 OD1 103.3
REMARK 620 3 HIS A 293 ND1 105.8 103.7
REMARK 620 4 CAC A 500 O2 99.2 136.5 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 210 NE2
REMARK 620 2 ASP B 214 OD1 103.0
REMARK 620 3 HIS B 293 ND1 104.9 103.0
REMARK 620 4 CAC B 501 O2 102.8 133.0 107.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QWY RELATED DB: PDB
REMARK 900 FULL-LENGTH LYTM
REMARK 900 RELATED ID: 2B13 RELATED DB: PDB
REMARK 900 TRUNCATED LYTM, DIFFERENT CRYSTAL FORM
REMARK 900 RELATED ID: 2B44 RELATED DB: PDB
REMARK 900 TRUNCATED S. AUREUS LYTM, P 32 2 1 CRYSTAL FORM
DBREF 2B0P A 185 316 UNP O33599 LYTM_STAAU 185 316
DBREF 2B0P B 185 316 UNP O33599 LYTM_STAAU 185 316
SEQRES 1 A 134 MET ALA HIS ALA LYS ASP ALA SER TRP LEU THR SER ARG
SEQRES 2 A 134 LYS GLN LEU GLN PRO TYR GLY GLN TYR HIS GLY GLY GLY
SEQRES 3 A 134 ALA HIS TYR GLY VAL ASP TYR ALA MET PRO GLU ASN SER
SEQRES 4 A 134 PRO VAL TYR SER LEU THR ASP GLY THR VAL VAL GLN ALA
SEQRES 5 A 134 GLY TRP SER ASN TYR GLY GLY GLY ASN GLN VAL THR ILE
SEQRES 6 A 134 LYS GLU ALA ASN SER ASN ASN TYR GLN TRP TYR MET HIS
SEQRES 7 A 134 ASN ASN ARG LEU THR VAL SER ALA GLY ASP LYS VAL LYS
SEQRES 8 A 134 ALA GLY ASP GLN ILE ALA TYR SER GLY SER THR GLY ASN
SEQRES 9 A 134 SER THR ALA PRO HIS VAL HIS PHE GLN ARG MET SER GLY
SEQRES 10 A 134 GLY ILE GLY ASN GLN TYR ALA VAL ASP PRO THR SER TYR
SEQRES 11 A 134 LEU GLN SER ARG
SEQRES 1 B 134 MET ALA HIS ALA LYS ASP ALA SER TRP LEU THR SER ARG
SEQRES 2 B 134 LYS GLN LEU GLN PRO TYR GLY GLN TYR HIS GLY GLY GLY
SEQRES 3 B 134 ALA HIS TYR GLY VAL ASP TYR ALA MET PRO GLU ASN SER
SEQRES 4 B 134 PRO VAL TYR SER LEU THR ASP GLY THR VAL VAL GLN ALA
SEQRES 5 B 134 GLY TRP SER ASN TYR GLY GLY GLY ASN GLN VAL THR ILE
SEQRES 6 B 134 LYS GLU ALA ASN SER ASN ASN TYR GLN TRP TYR MET HIS
SEQRES 7 B 134 ASN ASN ARG LEU THR VAL SER ALA GLY ASP LYS VAL LYS
SEQRES 8 B 134 ALA GLY ASP GLN ILE ALA TYR SER GLY SER THR GLY ASN
SEQRES 9 B 134 SER THR ALA PRO HIS VAL HIS PHE GLN ARG MET SER GLY
SEQRES 10 B 134 GLY ILE GLY ASN GLN TYR ALA VAL ASP PRO THR SER TYR
SEQRES 11 B 134 LEU GLN SER ARG
HET ZN A 400 1
HET CAC A 500 5
HET ACT A 700 4
HET ACT A 702 4
HET ZN B 401 1
HET CAC B 501 5
HET ACT B 701 4
HETNAM ZN ZINC ION
HETNAM CAC CACODYLATE ION
HETNAM ACT ACETATE ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CAC 2(C2 H6 AS O2 1-)
FORMUL 5 ACT 3(C2 H3 O2 1-)
FORMUL 10 HOH *385(H2 O)
HELIX 1 1 ALA A 189 SER A 194 1 6
HELIX 2 2 GLY A 302 GLN A 304 5 3
HELIX 3 3 PRO A 309 ARG A 316 1 8
HELIX 4 4 ALA B 189 SER B 194 1 6
HELIX 5 5 GLY B 302 GLN B 304 5 3
HELIX 6 6 PRO B 309 SER B 315 1 7
SHEET 1 A 7 GLN A 197 GLN A 199 0
SHEET 2 A 7 VAL A 213 ALA A 216 -1 O ASP A 214 N GLN A 199
SHEET 3 A 7 HIS A 291 SER A 298 -1 O VAL A 292 N TYR A 215
SHEET 4 A 7 ASN A 254 ASN A 261 -1 N TYR A 255 O MET A 297
SHEET 5 A 7 GLY A 242 GLU A 249 -1 N GLU A 249 O ASN A 254
SHEET 6 A 7 GLY A 229 SER A 237 -1 N THR A 230 O LYS A 248
SHEET 7 A 7 LYS A 271 VAL A 272 -1 O VAL A 272 N GLY A 229
SHEET 1 B 4 GLN A 197 GLN A 199 0
SHEET 2 B 4 VAL A 213 ALA A 216 -1 O ASP A 214 N GLN A 199
SHEET 3 B 4 HIS A 291 SER A 298 -1 O VAL A 292 N TYR A 215
SHEET 4 B 4 ALA A 306 VAL A 307 -1 O VAL A 307 N ARG A 296
SHEET 1 C 2 GLY A 202 GLN A 203 0
SHEET 2 C 2 ALA A 209 HIS A 210 -1 O HIS A 210 N GLY A 202
SHEET 1 D 2 PRO A 222 TYR A 224 0
SHEET 2 D 2 GLN A 277 TYR A 280 -1 O ILE A 278 N VAL A 223
SHEET 1 E 7 GLN B 197 GLN B 199 0
SHEET 2 E 7 VAL B 213 ALA B 216 -1 O ASP B 214 N GLN B 199
SHEET 3 E 7 HIS B 291 SER B 298 -1 O VAL B 292 N TYR B 215
SHEET 4 E 7 ASN B 254 ASN B 261 -1 N TYR B 255 O MET B 297
SHEET 5 E 7 GLY B 242 GLU B 249 -1 N GLU B 249 O ASN B 254
SHEET 6 E 7 GLY B 229 SER B 237 -1 N THR B 230 O LYS B 248
SHEET 7 E 7 LYS B 271 VAL B 272 -1 O VAL B 272 N GLY B 229
SHEET 1 F 4 GLN B 197 GLN B 199 0
SHEET 2 F 4 VAL B 213 ALA B 216 -1 O ASP B 214 N GLN B 199
SHEET 3 F 4 HIS B 291 SER B 298 -1 O VAL B 292 N TYR B 215
SHEET 4 F 4 ALA B 306 VAL B 307 -1 O VAL B 307 N ARG B 296
SHEET 1 G 2 GLY B 202 GLN B 203 0
SHEET 2 G 2 ALA B 209 HIS B 210 -1 O HIS B 210 N GLY B 202
SHEET 1 H 2 PRO B 222 TYR B 224 0
SHEET 2 H 2 GLN B 277 TYR B 280 -1 O ALA B 279 N VAL B 223
LINK NE2 HIS A 210 ZN ZN A 400 1555 1555 2.08
LINK OD1 ASP A 214 ZN ZN A 400 1555 1555 1.99
LINK ND1 HIS A 293 ZN ZN A 400 1555 1555 2.12
LINK ZN ZN A 400 O2 CAC A 500 1555 1555 1.95
LINK NE2 HIS B 210 ZN ZN B 401 1555 1555 2.10
LINK OD1 ASP B 214 ZN ZN B 401 1555 1555 2.05
LINK ND1 HIS B 293 ZN ZN B 401 1555 1555 2.06
LINK ZN ZN B 401 O2 CAC B 501 1555 1555 1.88
SITE 1 AC1 4 HIS A 210 ASP A 214 HIS A 293 CAC A 500
SITE 1 AC2 8 TYR A 204 HIS A 210 ASP A 214 HIS A 260
SITE 2 AC2 8 ASN A 286 HIS A 291 HIS A 293 ZN A 400
SITE 1 AC3 3 ASN A 220 ARG A 263 HOH A 716
SITE 1 AC4 6 LYS A 248 ALA A 250 ASN A 251 HOH A 731
SITE 2 AC4 6 HOH A 778 SER B 311
SITE 1 AC5 4 HIS B 210 ASP B 214 HIS B 293 CAC B 501
SITE 1 AC6 8 TYR B 204 HIS B 210 ASP B 214 HIS B 260
SITE 2 AC6 8 ASN B 286 HIS B 291 HIS B 293 ZN B 401
SITE 1 AC7 5 ASN B 220 ARG B 263 TYR B 280 HOH B 719
SITE 2 AC7 5 HOH B 832
CRYST1 32.093 78.261 102.049 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 0.031159 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012778 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009799 0.00000
(ATOM LINES ARE NOT SHOWN.)
END