HEADER HYDROLASE 22-SEP-05 2B44
TITLE TRUNCATED S. AUREUS LYTM, P 32 2 1 CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCYL-GLYCINE ENDOPEPTIDASE LYTM;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TRUNCATED LYTM;
COMPND 5 SYNONYM: AUTOLYSIN LYTM;
COMPND 6 EC: 3.4.24.75;
COMPND 7 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 3 23-AUG-23 2B44 1 REMARK SEQADV LINK
REVDAT 2 25-MAR-08 2B44 1 REMARK VERSN
REVDAT 1 10-JAN-06 2B44 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 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 49103
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) : 0.181
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2599
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) : 1.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3582
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 203
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1972
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 188
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.25000
REMARK 3 B22 (A**2) : 0.25000
REMARK 3 B33 (A**2) : -0.37000
REMARK 3 B12 (A**2) : 0.12000
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): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.673
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2091 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1668 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2847 ; 1.592 ; 1.905
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3903 ; 3.997 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 264 ; 7.596 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;34.598 ;24.762
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 289 ;14.679 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;29.571 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 278 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2442 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 434 ; 0.008 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 352 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1446 ; 0.230 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 986 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 954 ; 0.113 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 171 ; 0.140 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 8 ; 0.055 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.103 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 21 ; 0.252 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.134 ; 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): 1635 ; 1.566 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 561 ; 0.033 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2053 ; 1.684 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 983 ; 3.149 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 794 ; 3.645 ; 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 : NULL
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 : 1.20
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. THE LOOP REGION A204-A210 BREAKS THE CRYSTALLOGRAPHIC
REMARK 3 TWO-FOLD SYMMERTY IN P3(2)21 SPACEGROUP, THEREFORE IT IS MODELED
REMARK 3 AS DOUBLE CONFORMATION. THUS, IF ONE CONFORMATION IS CHOSEN FOR
REMARK 3 ONE LOOP, THEN THE OTHER CONFORMATION IS REQUIRED FOR THE
REMARK 3 SYMMETRY MATE.
REMARK 4
REMARK 4 2B44 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034650.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51861
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
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 (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24400
REMARK 200 R SYM FOR SHELL (I) : 0.24400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
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 (%): 76.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 2.0 M MONOAMMONIUM
REMARK 280 DIHYDROGEN PHOSPHATE, PH 4.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.69200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.34600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 34.34600
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.69200
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 ALA A 184
REMARK 465 HIS A 185
REMARK 465 SER A 315
REMARK 465 ARG A 316
REMARK 465 ALA B 184
REMARK 465 HIS B 185
REMARK 465 SER B 315
REMARK 465 ARG B 316
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 239 -117.89 -114.17
REMARK 500 ASN A 262 -123.53 -88.79
REMARK 500 ASN B 262 -127.29 -89.75
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 HIS A 210 NE2 0.9
REMARK 620 3 ASP A 214 OD1 106.3 105.6
REMARK 620 4 HIS A 293 ND1 107.8 107.6 108.4
REMARK 620 5 PO4 A 500 O4 105.6 106.5 118.1 110.1
REMARK 620 N 1 2 3 4
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 107.2
REMARK 620 3 HIS B 293 ND1 106.0 108.7
REMARK 620 4 PO4 B 600 O2 105.5 119.0 109.7
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 PO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QWY RELATED DB: PDB
REMARK 900 FULL LENGTH LYTM
REMARK 900 RELATED ID: 2B0P RELATED DB: PDB
REMARK 900 TRUNCATED LYTM, DIFFERENT CRYSTAL FORM
REMARK 900 RELATED ID: 2B13 RELATED DB: PDB
REMARK 900 TRUNCATED LYTM, DIFFERENT CRYSTAL FORM
DBREF 2B44 A 185 316 UNP O33599 LYTM_STAAU 185 316
DBREF 2B44 B 185 316 UNP O33599 LYTM_STAAU 185 316
SEQADV 2B44 ALA A 184 UNP O33599 CLONING ARTIFACT
SEQADV 2B44 ALA B 184 UNP O33599 CLONING ARTIFACT
SEQRES 1 A 133 ALA HIS ALA LYS ASP ALA SER TRP LEU THR SER ARG LYS
SEQRES 2 A 133 GLN LEU GLN PRO TYR GLY GLN TYR HIS GLY GLY GLY ALA
SEQRES 3 A 133 HIS TYR GLY VAL ASP TYR ALA MET PRO GLU ASN SER PRO
SEQRES 4 A 133 VAL TYR SER LEU THR ASP GLY THR VAL VAL GLN ALA GLY
SEQRES 5 A 133 TRP SER ASN TYR GLY GLY GLY ASN GLN VAL THR ILE LYS
SEQRES 6 A 133 GLU ALA ASN SER ASN ASN TYR GLN TRP TYR MET HIS ASN
SEQRES 7 A 133 ASN ARG LEU THR VAL SER ALA GLY ASP LYS VAL LYS ALA
SEQRES 8 A 133 GLY ASP GLN ILE ALA TYR SER GLY SER THR GLY ASN SER
SEQRES 9 A 133 THR ALA PRO HIS VAL HIS PHE GLN ARG MET SER GLY GLY
SEQRES 10 A 133 ILE GLY ASN GLN TYR ALA VAL ASP PRO THR SER TYR LEU
SEQRES 11 A 133 GLN SER ARG
SEQRES 1 B 133 ALA HIS ALA LYS ASP ALA SER TRP LEU THR SER ARG LYS
SEQRES 2 B 133 GLN LEU GLN PRO TYR GLY GLN TYR HIS GLY GLY GLY ALA
SEQRES 3 B 133 HIS TYR GLY VAL ASP TYR ALA MET PRO GLU ASN SER PRO
SEQRES 4 B 133 VAL TYR SER LEU THR ASP GLY THR VAL VAL GLN ALA GLY
SEQRES 5 B 133 TRP SER ASN TYR GLY GLY GLY ASN GLN VAL THR ILE LYS
SEQRES 6 B 133 GLU ALA ASN SER ASN ASN TYR GLN TRP TYR MET HIS ASN
SEQRES 7 B 133 ASN ARG LEU THR VAL SER ALA GLY ASP LYS VAL LYS ALA
SEQRES 8 B 133 GLY ASP GLN ILE ALA TYR SER GLY SER THR GLY ASN SER
SEQRES 9 B 133 THR ALA PRO HIS VAL HIS PHE GLN ARG MET SER GLY GLY
SEQRES 10 B 133 ILE GLY ASN GLN TYR ALA VAL ASP PRO THR SER TYR LEU
SEQRES 11 B 133 GLN SER ARG
HET ZN A 400 1
HET PO4 A 500 5
HET PO4 A 700 5
HET ZN B 401 1
HET PO4 B 600 5
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 PO4 3(O4 P 3-)
FORMUL 8 HOH *188(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 GLN A 314 1 6
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 GLN B 314 1 6
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 PHE A 294 N VAL A 213
SHEET 4 A 7 ASN A 254 ASN A 261 -1 N TRP A 257 O GLN A 295
SHEET 5 A 7 ASN A 243 GLU A 249 -1 N GLU A 249 O ASN A 254
SHEET 6 A 7 GLY A 229 TRP A 236 -1 N GLN A 233 O THR A 246
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 PHE A 294 N VAL A 213
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 PHE B 294 N VAL B 213
SHEET 4 E 7 ASN B 254 ASN B 261 -1 N TYR B 255 O MET B 297
SHEET 5 E 7 ASN B 243 GLU B 249 -1 N ILE B 247 O GLN B 256
SHEET 6 E 7 GLY B 229 TRP B 236 -1 N GLN B 233 O THR B 246
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 PHE B 294 N VAL B 213
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 ILE B 278 N VAL B 223
LINK NE2AHIS A 210 ZN ZN A 400 1555 1555 2.04
LINK NE2BHIS A 210 ZN ZN A 400 1555 1555 2.06
LINK OD1 ASP A 214 ZN ZN A 400 1555 1555 1.98
LINK ND1 HIS A 293 ZN ZN A 400 1555 1555 2.00
LINK ZN ZN A 400 O4 PO4 A 500 1555 1555 2.00
LINK NE2 HIS B 210 ZN ZN B 401 1555 1555 2.11
LINK OD1 ASP B 214 ZN ZN B 401 1555 1555 1.94
LINK ND1 HIS B 293 ZN ZN B 401 1555 1555 2.05
LINK ZN ZN B 401 O2 PO4 B 600 1555 1555 1.92
SITE 1 AC1 4 HIS A 210 ASP A 214 HIS A 293 PO4 A 500
SITE 1 AC2 10 TYR A 204 HIS A 210 ASP A 214 HIS A 260
SITE 2 AC2 10 GLY A 285 ASN A 286 SER A 287 HIS A 291
SITE 3 AC2 10 HIS A 293 ZN A 400
SITE 1 AC3 6 GLN A 233 SER A 237 ASN A 238 TYR A 239
SITE 2 AC3 6 GLN A 244 HOH A 747
SITE 1 AC4 4 HIS B 210 ASP B 214 HIS B 293 PO4 B 600
SITE 1 AC5 10 TYR B 204 HIS B 210 ASP B 214 HIS B 260
SITE 2 AC5 10 GLY B 285 ASN B 286 SER B 287 HIS B 291
SITE 3 AC5 10 HIS B 293 ZN B 401
CRYST1 100.434 100.434 103.038 90.00 90.00 120.00 P 32 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009957 0.005749 0.000000 0.00000
SCALE2 0.000000 0.011497 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
