HEADER HYDROLASE 11-JUL-06 2IXV
TITLE CRYSTAL STRUCTURE OF THE MODULAR CPL-1 ENDOLYSIN COMPLEXED WITH A
TITLE 2 PEPTIDOGLYCAN ANALOGUE (E94Q MUTANT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CPL-1, ENDOLYSIN, MURAMIDASE, CP-1 LYSIN;
COMPND 5 EC: 3.2.1.17;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PHAGE CP-1;
SOURCE 3 ORGANISM_COMMON: CP-1 BACTERIOPHAGE;
SOURCE 4 ORGANISM_TAXID: 10747;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH1;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 536056
KEYWDS ANTIMICROBIAL, MUEIN HYDROLASE, BACTERIOLYTIC ENZYME, PNEUMOCOCCAL
KEYWDS 2 CELL WALL DEGRADATION, LYSOZYME, HYDROLASE, GLYCOSIDASE,
KEYWDS 3 MULTIMODULAR
EXPDTA X-RAY DIFFRACTION
AUTHOR I.PEREZ-DORADO,J.A.HERMOSO
REVDAT 7 13-DEC-23 2IXV 1 HETSYN LINK
REVDAT 6 29-JUL-20 2IXV 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 01-JUL-20 2IXV 1 COMPND REMARK HET HETNAM
REVDAT 5 2 1 FORMUL LINK SITE ATOM
REVDAT 4 10-APR-19 2IXV 1 SOURCE LINK
REVDAT 3 24-FEB-09 2IXV 1 VERSN
REVDAT 2 28-AUG-07 2IXV 1 JRNL
REVDAT 1 03-JUL-07 2IXV 0
JRNL AUTH I.PEREZ-DORADO,N.E.CAMPILLO,B.MONTERROSO,D.HESEK,M.LEE,
JRNL AUTH 2 J.A.PAEZ,P.GARCIA,M.MARTINEZ-RIPOLL,J.L.GARCIA,S.MOBASHERY,
JRNL AUTH 3 M.MENENDEZ,J.A.HERMOSO
JRNL TITL ELUCIDATION OF THE MOLECULAR RECOGNITION OF BACTERIAL CELL
JRNL TITL 2 WALL BY MODULAR PNEUMOCOCCAL PHAGE ENDOLYSIN CPL-1.
JRNL REF J.BIOL.CHEM. V. 282 24990 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17581815
JRNL DOI 10.1074/JBC.M704317200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.HERMOSO,B.MONTERROSO,A.ALBERT,B.GALAN,O.AHRAZEM,
REMARK 1 AUTH 2 P.GARCIA,M.MARTINEZ-RIPOLL,J.L.GARCIA,M.MENENDEZ
REMARK 1 TITL STRUCTURAL BASIS FOR SELECTIVE RECOGNITION OF PNEUMOCOCCAL
REMARK 1 TITL 2 CELL WALL BY MODULAR ENDOLYSIN FROM PHAGE CP-1
REMARK 1 REF STRUCTURE (LONDON) V. 11 1 2003
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 14527392
REMARK 1 DOI 10.1016/J.STR.2003.09.005
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.MONTERROSO,A.ALBERT,M.MARTINEZ-RIPOLL,P.GARCIA,J.L.GARCIA,
REMARK 1 AUTH 2 M.MENENDEZ,J.A.HERMOSO
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK 1 TITL 2 THE COMPLETE MODULAR ENDOLYSIN FROM CP-1, A PHAGE INFECTING
REMARK 1 TITL 3 STREPTOCOCCUS PNEUMONIAE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 1487 2002
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 12198311
REMARK 1 DOI 10.1107/S0907444902011563
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1734679.420
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 35314
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 SET) : 0.223
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2490
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5410
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 441
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2763
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.87000
REMARK 3 B22 (A**2) : -3.23000
REMARK 3 B33 (A**2) : -0.64000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.710
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.420 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.040 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.040 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 50.38
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IXV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1290029224.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE MONOCROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40900
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 26.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1H09
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.53650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.53650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 39.98250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.22150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.98250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.22150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.53650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.98250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.22150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.53650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.98250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.22150
REMARK 290 SMTRY3 8 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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 94 TO GLN
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 1
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 5 -0.69 71.78
REMARK 500 SER A 38 -142.25 55.92
REMARK 500 GLN A 94 10.74 -142.45
REMARK 500 SER A 126 -174.20 176.15
REMARK 500 ASP A 193 90.28 -40.07
REMARK 500 THR A 198 77.75 59.65
REMARK 500 LYS A 288 -108.08 60.49
REMARK 500 ASN A 296 24.20 -141.78
REMARK 500 THR A 318 -5.95 -59.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 770 DISTANCE = 5.98 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H09 RELATED DB: PDB
REMARK 900 MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1
REMARK 900 RELATED ID: 1OBA RELATED DB: PDB
REMARK 900 MULTIMODULAR PNEUMOCOCCAL CELL WALL ENDOLYSIN FROM PHAGE CP-1
REMARK 900 COMPLEXED WITH CHOLINE
REMARK 900 RELATED ID: 2IXU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MODULAR CPL-1 ENDOLYSIN COMPLEXED WITH A
REMARK 900 PEPTIDOGLYCAN ANALOGUE (WILD-TYPE ENDOLYSIN)
DBREF 2IXV A 1 339 UNP P15057 LYS_BPCP1 1 339
SEQADV 2IXV GLN A 94 UNP P15057 GLU 94 ENGINEERED MUTATION
SEQRES 1 A 339 MET VAL LYS LYS ASN ASP LEU PHE VAL ASP VAL SER SER
SEQRES 2 A 339 HIS ASN GLY TYR ASP ILE THR GLY ILE LEU GLU GLN MET
SEQRES 3 A 339 GLY THR THR ASN THR ILE ILE LYS ILE SER GLU SER THR
SEQRES 4 A 339 THR TYR LEU ASN PRO CYS LEU SER ALA GLN VAL GLU GLN
SEQRES 5 A 339 SER ASN PRO ILE GLY PHE TYR HIS PHE ALA ARG PHE GLY
SEQRES 6 A 339 GLY ASP VAL ALA GLU ALA GLU ARG GLU ALA GLN PHE PHE
SEQRES 7 A 339 LEU ASP ASN VAL PRO MET GLN VAL LYS TYR LEU VAL LEU
SEQRES 8 A 339 ASP TYR GLN ASP ASP PRO SER GLY ASP ALA GLN ALA ASN
SEQRES 9 A 339 THR ASN ALA CYS LEU ARG PHE MET GLN MET ILE ALA ASP
SEQRES 10 A 339 ALA GLY TYR LYS PRO ILE TYR TYR SER TYR LYS PRO PHE
SEQRES 11 A 339 THR HIS ASP ASN VAL ASP TYR GLN GLN ILE LEU ALA GLN
SEQRES 12 A 339 PHE PRO ASN SER LEU TRP ILE ALA GLY TYR GLY LEU ASN
SEQRES 13 A 339 ASP GLY THR ALA ASN PHE GLU TYR PHE PRO SER MET ASP
SEQRES 14 A 339 GLY ILE ARG TRP TRP GLN TYR SER SER ASN PRO PHE ASP
SEQRES 15 A 339 LYS ASN ILE VAL LEU LEU ASP ASP GLU GLU ASP ASP LYS
SEQRES 16 A 339 PRO LYS THR ALA GLY THR TRP LYS GLN ASP SER LYS GLY
SEQRES 17 A 339 TRP TRP PHE ARG ARG ASN ASN GLY SER PHE PRO TYR ASN
SEQRES 18 A 339 LYS TRP GLU LYS ILE GLY GLY VAL TRP TYR TYR PHE ASP
SEQRES 19 A 339 SER LYS GLY TYR CYS LEU THR SER GLU TRP LEU LYS ASP
SEQRES 20 A 339 ASN GLU LYS TRP TYR TYR LEU LYS ASP ASN GLY ALA MET
SEQRES 21 A 339 ALA THR GLY TRP VAL LEU VAL GLY SER GLU TRP TYR TYR
SEQRES 22 A 339 MET ASP ASP SER GLY ALA MET VAL THR GLY TRP VAL LYS
SEQRES 23 A 339 TYR LYS ASN ASN TRP TYR TYR MET THR ASN GLU ARG GLY
SEQRES 24 A 339 ASN MET VAL SER ASN GLU PHE ILE LYS SER GLY LYS GLY
SEQRES 25 A 339 TRP TYR PHE MET ASN THR ASN GLY GLU LEU ALA ASP ASN
SEQRES 26 A 339 PRO SER PHE THR LYS GLU PRO ASP GLY LEU ILE THR VAL
SEQRES 27 A 339 ALA
HET MUB B 1 19
HET NAG B 2 14
HET FMT A 401 3
HET ALA A 404 5
HET DGN A 405 10
HETNAM MUB N-ACETYL-ALPHA-MURAMIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FMT FORMIC ACID
HETNAM ALA ALANINE
HETNAM DGN D-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
FORMUL 2 MUB C11 H19 N O8
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 FMT C H2 O2
FORMUL 4 ALA C3 H7 N O2
FORMUL 5 DGN C5 H10 N2 O3
FORMUL 6 HOH *270(H2 O)
HELIX 1 1 SER A 12 GLY A 16 5 5
HELIX 2 2 ILE A 19 GLY A 27 1 9
HELIX 3 3 CYS A 45 GLN A 52 1 8
HELIX 4 4 ASP A 67 ASN A 81 1 15
HELIX 5 5 ASP A 100 ALA A 118 1 19
HELIX 6 6 LYS A 128 VAL A 135 1 8
HELIX 7 7 ASP A 136 PHE A 144 1 9
HELIX 8 8 ASN A 161 PHE A 165 5 5
HELIX 9 9 ASN A 296 ASN A 300 5 5
SHEET 1 AA11 LEU A 7 VAL A 11 0
SHEET 2 AA11 ASP A 182 VAL A 186 -1 O ASP A 182 N ASP A 10
SHEET 3 AA11 ILE A 171 SER A 177 -1 O TRP A 174 N ILE A 185
SHEET 4 AA11 LEU A 148 ALA A 151 1 O LEU A 148 N ARG A 172
SHEET 5 AA11 LYS A 121 TYR A 127 1 O TYR A 124 N TRP A 149
SHEET 6 AA11 TYR A 88 ASP A 92 1 O LEU A 89 N ILE A 123
SHEET 7 AA11 ASN A 54 PHE A 61 1 O ILE A 56 N TYR A 88
SHEET 8 AA11 ASN A 30 GLU A 37 1 O THR A 31 N ILE A 56
SHEET 9 AA11 LEU A 7 VAL A 11 1 O VAL A 9 N ILE A 32
SHEET 10 AA11 ASP A 182 VAL A 186 -1 O ASP A 182 N ASP A 10
SHEET 11 AA11 LEU A 7 VAL A 11 -1 O PHE A 8 N ASN A 184
SHEET 1 AB 2 GLY A 200 GLN A 204 0
SHEET 2 AB 2 TRP A 209 ARG A 213 -1 O TRP A 210 N LYS A 203
SHEET 1 AC 2 LYS A 222 ILE A 226 0
SHEET 2 AC 2 VAL A 229 PHE A 233 -1 O VAL A 229 N ILE A 226
SHEET 1 AD 2 GLU A 243 ASP A 247 0
SHEET 2 AD 2 LYS A 250 LEU A 254 -1 O LYS A 250 N ASP A 247
SHEET 1 AE 2 GLY A 263 VAL A 267 0
SHEET 2 AE 2 GLU A 270 MET A 274 -1 O GLU A 270 N VAL A 267
SHEET 1 AF 5 GLY A 312 PHE A 315 0
SHEET 2 AF 5 VAL A 302 SER A 309 -1 O ILE A 307 N TYR A 314
SHEET 3 AF 5 ASN A 290 THR A 295 -1 O TRP A 291 N PHE A 306
SHEET 4 AF 5 GLY A 283 TYR A 287 -1 O GLY A 283 N MET A 294
SHEET 5 AF 5 LEU A 335 THR A 337 1 O LEU A 335 N LYS A 286
LINK C ALA A 404 N DGN A 405 1555 1555 1.34
LINK N ALA A 404 C10 MUB B 1 1555 1555 1.34
LINK O4 MUB B 1 C1 NAG B 2 1555 1555 1.39
CISPEP 1 ASN A 179 PRO A 180 0 0.38
CRYST1 79.965 96.443 127.073 90.00 90.00 90.00 C 2 2 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 0.012505 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010369 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007869 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
