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HEADER LYASE 01-AUG-12 4GEG
TITLE CRYSTAL STRUCTURE OF E.COLI MENH Y85F MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE
COMPND 3 SYNTHASE;
COMPND 4 CHAIN: A, B, C;
COMPND 5 SYNONYM: SHCHC SYNTHASE;
COMPND 6 EC: 4.2.99.20;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B2263, JW2258, MENH, MENH_Y85FMUTANT, YFBB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM
KEYWDS MENAQUINONE BIOSYNTHESIS, ALPHA BETA HYDROLASE, 2-SUCCINYL-6-HYDROXY-
KEYWDS 2 2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE, MENH Y85F MUTANT, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M JOHNSTON,E.N.BAKER,Z.GUO,M.JIANG
REVDAT 2 15-MAY-13 4GEG 1 JRNL
REVDAT 1 08-MAY-13 4GEG 0
JRNL AUTH J.M.JOHNSTON,M.JIANG,Z.GUO,E.N.BAKER
JRNL TITL CRYSTAL STRUCTURES OF E. COLI NATIVE MENH AND TWO ACTIVE
JRNL TITL 2 SITE MUTANTS.
JRNL REF PLOS ONE V. 8 61325 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 23637813
JRNL DOI 10.1371/JOURNAL.PONE.0061325
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 34093
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1723
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.57
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.77
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2838
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2158
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2679
REMARK 3 BIN R VALUE (WORKING SET) : 0.2117
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 159
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5959
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 419
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.56280
REMARK 3 B22 (A**2) : -2.23740
REMARK 3 B33 (A**2) : 2.80010
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.29530
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.43
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.27
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.39
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.27
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.843
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6164 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8370 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2764 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 149 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 923 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6164 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 745 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 7428 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.92
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.08
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GEG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB074080.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953695
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34116
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.489
REMARK 200 RESOLUTION RANGE LOW (A) : 124.587
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.32400
REMARK 200 R SYM (I) : 0.32400
REMARK 200 FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.95400
REMARK 200 R SYM FOR SHELL (I) : 0.95400
REMARK 200 FOR SHELL : 2.000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, AMMONIUM SULFATE,
REMARK 280 LITHIUM SULFATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 125.24950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.79450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 125.24950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.79450
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, 3
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 MET B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 SER B -8
REMARK 465 SER B -7
REMARK 465 GLY B -6
REMARK 465 LEU B -5
REMARK 465 PHE B 252
REMARK 465 MET C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 SER C -8
REMARK 465 SER C -7
REMARK 465 GLY C -6
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 ARG A -2 CG CD NE CZ NH1 NH2
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 SER A 24 0.04 82.69
REMARK 500 PHE A 37 54.05 -100.47
REMARK 500 SER A 86 -110.05 42.50
REMARK 500 SER B 24 -1.69 80.50
REMARK 500 SER B 86 -102.00 48.44
REMARK 500 ALA B 221 41.20 -83.09
REMARK 500 SER C 24 -8.76 93.29
REMARK 500 PHE C 37 53.30 -105.05
REMARK 500 SER C 86 -104.03 51.17
REMARK 500 THR C 137 -36.58 -136.00
REMARK 500 ASP C 223 73.90 -64.89
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 B 474 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B 475 DISTANCE = 5.77 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 310
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GDM RELATED DB: PDB
REMARK 900 NATIVE E. COLI MENH STRUCTURE
REMARK 900 RELATED ID: 4GEC RELATED DB: PDB
REMARK 900 E. COLI MENH R124A MUTANT STRUCTURE
DBREF 4GEG A 1 252 UNP P37355 MENH_ECOLI 1 252
DBREF 4GEG B 1 252 UNP P37355 MENH_ECOLI 1 252
DBREF 4GEG C 1 252 UNP P37355 MENH_ECOLI 1 252
SEQADV 4GEG MET A -15 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS A -14 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS A -13 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS A -12 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS A -11 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS A -10 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS A -9 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER A -8 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER A -7 UNP P37355 EXPRESSION TAG
SEQADV 4GEG GLY A -6 UNP P37355 EXPRESSION TAG
SEQADV 4GEG LEU A -5 UNP P37355 EXPRESSION TAG
SEQADV 4GEG VAL A -4 UNP P37355 EXPRESSION TAG
SEQADV 4GEG PRO A -3 UNP P37355 EXPRESSION TAG
SEQADV 4GEG ARG A -2 UNP P37355 EXPRESSION TAG
SEQADV 4GEG GLY A -1 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER A 0 UNP P37355 EXPRESSION TAG
SEQADV 4GEG PHE A 85 UNP P37355 TYR 85 ENGINEERED MUTATION
SEQADV 4GEG MET B -15 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS B -14 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS B -13 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS B -12 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS B -11 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS B -10 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS B -9 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER B -8 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER B -7 UNP P37355 EXPRESSION TAG
SEQADV 4GEG GLY B -6 UNP P37355 EXPRESSION TAG
SEQADV 4GEG LEU B -5 UNP P37355 EXPRESSION TAG
SEQADV 4GEG VAL B -4 UNP P37355 EXPRESSION TAG
SEQADV 4GEG PRO B -3 UNP P37355 EXPRESSION TAG
SEQADV 4GEG ARG B -2 UNP P37355 EXPRESSION TAG
SEQADV 4GEG GLY B -1 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER B 0 UNP P37355 EXPRESSION TAG
SEQADV 4GEG PHE B 85 UNP P37355 TYR 85 ENGINEERED MUTATION
SEQADV 4GEG MET C -15 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS C -14 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS C -13 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS C -12 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS C -11 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS C -10 UNP P37355 EXPRESSION TAG
SEQADV 4GEG HIS C -9 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER C -8 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER C -7 UNP P37355 EXPRESSION TAG
SEQADV 4GEG GLY C -6 UNP P37355 EXPRESSION TAG
SEQADV 4GEG LEU C -5 UNP P37355 EXPRESSION TAG
SEQADV 4GEG VAL C -4 UNP P37355 EXPRESSION TAG
SEQADV 4GEG PRO C -3 UNP P37355 EXPRESSION TAG
SEQADV 4GEG ARG C -2 UNP P37355 EXPRESSION TAG
SEQADV 4GEG GLY C -1 UNP P37355 EXPRESSION TAG
SEQADV 4GEG SER C 0 UNP P37355 EXPRESSION TAG
SEQADV 4GEG PHE C 85 UNP P37355 TYR 85 ENGINEERED MUTATION
SEQRES 1 A 268 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 A 268 ARG GLY SER MET ILE LEU HIS ALA GLN ALA LYS HIS GLY
SEQRES 3 A 268 LYS PRO GLY LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE
SEQRES 4 A 268 SER GLY ASP CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA
SEQRES 5 A 268 PHE ALA ASP TYR SER ARG LEU TYR VAL ASP LEU PRO GLY
SEQRES 6 A 268 HIS GLY GLY SER ALA ALA ILE SER VAL ASP GLY PHE ASP
SEQRES 7 A 268 ASP VAL THR ASP LEU LEU ARG LYS THR LEU VAL SER TYR
SEQRES 8 A 268 ASN ILE LEU ASP PHE TRP LEU VAL GLY PHE SER LEU GLY
SEQRES 9 A 268 GLY ARG VAL ALA MET MET ALA ALA CYS GLN GLY LEU ALA
SEQRES 10 A 268 GLY LEU CYS GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY
SEQRES 11 A 268 LEU GLN ASN ALA GLU GLN ARG ALA GLU ARG GLN ARG SER
SEQRES 12 A 268 ASP ARG GLN TRP VAL GLN ARG PHE LEU THR GLU PRO LEU
SEQRES 13 A 268 THR ALA VAL PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE
SEQRES 14 A 268 ALA SER LEU ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA
SEQRES 15 A 268 LEU ARG SER ASN ASN ASN GLY ALA THR LEU ALA ALA MET
SEQRES 16 A 268 LEU GLU ALA THR SER LEU ALA VAL GLN PRO ASP LEU ARG
SEQRES 17 A 268 ALA ASN LEU SER ALA ARG THR PHE ALA PHE TYR TYR LEU
SEQRES 18 A 268 CYS GLY GLU ARG ASP SER LYS PHE ARG ALA LEU ALA ALA
SEQRES 19 A 268 GLU LEU ALA ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY
SEQRES 20 A 268 HIS ASN ALA HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA
SEQRES 21 A 268 SER LEU ALA GLN ILE LEU ARG PHE
SEQRES 1 B 268 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 B 268 ARG GLY SER MET ILE LEU HIS ALA GLN ALA LYS HIS GLY
SEQRES 3 B 268 LYS PRO GLY LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE
SEQRES 4 B 268 SER GLY ASP CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA
SEQRES 5 B 268 PHE ALA ASP TYR SER ARG LEU TYR VAL ASP LEU PRO GLY
SEQRES 6 B 268 HIS GLY GLY SER ALA ALA ILE SER VAL ASP GLY PHE ASP
SEQRES 7 B 268 ASP VAL THR ASP LEU LEU ARG LYS THR LEU VAL SER TYR
SEQRES 8 B 268 ASN ILE LEU ASP PHE TRP LEU VAL GLY PHE SER LEU GLY
SEQRES 9 B 268 GLY ARG VAL ALA MET MET ALA ALA CYS GLN GLY LEU ALA
SEQRES 10 B 268 GLY LEU CYS GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY
SEQRES 11 B 268 LEU GLN ASN ALA GLU GLN ARG ALA GLU ARG GLN ARG SER
SEQRES 12 B 268 ASP ARG GLN TRP VAL GLN ARG PHE LEU THR GLU PRO LEU
SEQRES 13 B 268 THR ALA VAL PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE
SEQRES 14 B 268 ALA SER LEU ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA
SEQRES 15 B 268 LEU ARG SER ASN ASN ASN GLY ALA THR LEU ALA ALA MET
SEQRES 16 B 268 LEU GLU ALA THR SER LEU ALA VAL GLN PRO ASP LEU ARG
SEQRES 17 B 268 ALA ASN LEU SER ALA ARG THR PHE ALA PHE TYR TYR LEU
SEQRES 18 B 268 CYS GLY GLU ARG ASP SER LYS PHE ARG ALA LEU ALA ALA
SEQRES 19 B 268 GLU LEU ALA ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY
SEQRES 20 B 268 HIS ASN ALA HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA
SEQRES 21 B 268 SER LEU ALA GLN ILE LEU ARG PHE
SEQRES 1 C 268 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 C 268 ARG GLY SER MET ILE LEU HIS ALA GLN ALA LYS HIS GLY
SEQRES 3 C 268 LYS PRO GLY LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE
SEQRES 4 C 268 SER GLY ASP CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA
SEQRES 5 C 268 PHE ALA ASP TYR SER ARG LEU TYR VAL ASP LEU PRO GLY
SEQRES 6 C 268 HIS GLY GLY SER ALA ALA ILE SER VAL ASP GLY PHE ASP
SEQRES 7 C 268 ASP VAL THR ASP LEU LEU ARG LYS THR LEU VAL SER TYR
SEQRES 8 C 268 ASN ILE LEU ASP PHE TRP LEU VAL GLY PHE SER LEU GLY
SEQRES 9 C 268 GLY ARG VAL ALA MET MET ALA ALA CYS GLN GLY LEU ALA
SEQRES 10 C 268 GLY LEU CYS GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY
SEQRES 11 C 268 LEU GLN ASN ALA GLU GLN ARG ALA GLU ARG GLN ARG SER
SEQRES 12 C 268 ASP ARG GLN TRP VAL GLN ARG PHE LEU THR GLU PRO LEU
SEQRES 13 C 268 THR ALA VAL PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE
SEQRES 14 C 268 ALA SER LEU ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA
SEQRES 15 C 268 LEU ARG SER ASN ASN ASN GLY ALA THR LEU ALA ALA MET
SEQRES 16 C 268 LEU GLU ALA THR SER LEU ALA VAL GLN PRO ASP LEU ARG
SEQRES 17 C 268 ALA ASN LEU SER ALA ARG THR PHE ALA PHE TYR TYR LEU
SEQRES 18 C 268 CYS GLY GLU ARG ASP SER LYS PHE ARG ALA LEU ALA ALA
SEQRES 19 C 268 GLU LEU ALA ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY
SEQRES 20 C 268 HIS ASN ALA HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA
SEQRES 21 C 268 SER LEU ALA GLN ILE LEU ARG PHE
HET SO4 A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET SO4 A 304 5
HET CL A 305 1
HET EDO A 306 4
HET SO4 B 301 5
HET SO4 B 302 5
HET SO4 B 303 5
HET SO4 B 304 5
HET CL B 305 1
HET GOL B 306 6
HET CL B 307 1
HET SO4 C 301 5
HET SO4 C 302 5
HET SO4 C 303 5
HET SO4 C 304 5
HET SO4 C 305 5
HET CL C 306 1
HET CL C 307 1
HET GOL C 308 6
HET CL C 309 1
HET CL C 310 1
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 SO4 13(O4 S 2-)
FORMUL 8 CL 7(CL 1-)
FORMUL 9 EDO C2 H6 O2
FORMUL 15 GOL 2(C3 H8 O3)
FORMUL 27 HOH *419(H2 O)
HELIX 1 1 TRP A 30 GLU A 35 1 6
HELIX 2 2 HIS A 50 ALA A 54 5 5
HELIX 3 3 GLY A 60 TYR A 75 1 16
HELIX 4 4 SER A 86 GLY A 99 1 14
HELIX 5 5 ASN A 117 GLU A 138 1 22
HELIX 6 6 PRO A 139 TYR A 148 1 10
HELIX 7 7 GLN A 149 ALA A 154 5 6
HELIX 8 8 ASN A 157 SER A 169 1 13
HELIX 9 9 ASN A 172 THR A 183 1 12
HELIX 10 10 LEU A 191 ALA A 197 1 7
HELIX 11 11 ASP A 210 GLU A 219 1 10
HELIX 12 12 ASN A 233 ASN A 238 1 6
HELIX 13 13 ASN A 238 ARG A 251 1 14
HELIX 14 14 TRP B 30 GLU B 35 1 6
HELIX 15 15 HIS B 50 ALA B 54 5 5
HELIX 16 16 GLY B 60 TYR B 75 1 16
HELIX 17 17 SER B 86 CYS B 97 1 12
HELIX 18 18 ASN B 117 LEU B 136 1 20
HELIX 19 19 PRO B 139 TYR B 148 1 10
HELIX 20 20 GLN B 149 ALA B 154 5 6
HELIX 21 21 ASN B 157 SER B 169 1 13
HELIX 22 22 ASN B 172 THR B 183 1 12
HELIX 23 23 SER B 184 GLN B 188 5 5
HELIX 24 24 LEU B 191 ALA B 197 1 7
HELIX 25 25 ASP B 210 ALA B 218 1 9
HELIX 26 26 ASN B 233 ASN B 238 1 6
HELIX 27 27 ASN B 238 ARG B 251 1 14
HELIX 28 28 TRP C 30 GLU C 35 1 6
HELIX 29 29 HIS C 50 ALA C 54 5 5
HELIX 30 30 GLY C 60 TYR C 75 1 16
HELIX 31 31 SER C 86 GLY C 99 1 14
HELIX 32 32 ASN C 117 LEU C 136 1 20
HELIX 33 33 PRO C 139 TYR C 148 1 10
HELIX 34 34 GLN C 149 ALA C 154 5 6
HELIX 35 35 ASN C 157 SER C 169 1 13
HELIX 36 36 ASN C 172 THR C 183 1 12
HELIX 37 37 LEU C 191 ALA C 197 1 7
HELIX 38 38 ASP C 210 LEU C 220 1 11
HELIX 39 39 ASN C 233 ASN C 238 1 6
HELIX 40 40 ASN C 238 ARG C 251 1 14
SHEET 1 A 7 ALA A 5 LYS A 8 0
SHEET 2 A 7 SER A 41 VAL A 45 -1 O ARG A 42 N LYS A 8
SHEET 3 A 7 TRP A 16 LEU A 20 1 N PHE A 19 O LEU A 43
SHEET 4 A 7 PHE A 80 PHE A 85 1 O VAL A 83 N VAL A 18
SHEET 5 A 7 LEU A 103 GLU A 109 1 O ILE A 107 N LEU A 82
SHEET 6 A 7 ALA A 201 GLY A 207 1 O LEU A 205 N VAL A 108
SHEET 7 A 7 CYS A 224 ILE A 227 1 O ILE A 227 N CYS A 206
SHEET 1 B 7 ALA B 5 LYS B 8 0
SHEET 2 B 7 SER B 41 VAL B 45 -1 O ARG B 42 N LYS B 8
SHEET 3 B 7 TRP B 16 LEU B 20 1 N LEU B 17 O LEU B 43
SHEET 4 B 7 PHE B 80 PHE B 85 1 O TRP B 81 N TRP B 16
SHEET 5 B 7 LEU B 103 GLU B 109 1 O CYS B 104 N PHE B 80
SHEET 6 B 7 PHE B 202 GLY B 207 1 O TYR B 203 N VAL B 108
SHEET 7 B 7 ASP B 223 ILE B 227 1 O ILE B 227 N CYS B 206
SHEET 1 C 7 ALA C 5 LYS C 8 0
SHEET 2 C 7 SER C 41 VAL C 45 -1 O ARG C 42 N LYS C 8
SHEET 3 C 7 TRP C 16 LEU C 20 1 N LEU C 17 O SER C 41
SHEET 4 C 7 PHE C 80 PHE C 85 1 O TRP C 81 N VAL C 18
SHEET 5 C 7 LEU C 103 GLU C 109 1 O CYS C 104 N PHE C 80
SHEET 6 C 7 ALA C 201 GLY C 207 1 O LEU C 205 N VAL C 108
SHEET 7 C 7 HIS C 225 ILE C 227 1 O ILE C 227 N CYS C 206
SITE 1 AC1 8 SER A 86 LEU A 87 ARG A 90 EDO A 306
SITE 2 AC1 8 HOH A 452 HOH A 503 HOH A 526 HOH A 540
SITE 1 AC2 5 GLY A 60 PHE A 61 ASP A 62 HOH A 401
SITE 2 AC2 5 HOH A 529
SITE 1 AC3 5 ARG A 198 ALA A 201 PHE A 202 TYR A 203
SITE 2 AC3 5 HOH A 511
SITE 1 AC4 4 ALA A 7 LYS A 8 HIS A 9 HOH A 493
SITE 1 AC5 3 TYR A 148 ARG A 168 ASN A 233
SITE 1 AC6 5 ARG A 124 VAL A 152 PHE A 213 SO4 A 301
SITE 2 AC6 5 HOH A 418
SITE 1 AC7 7 SER B 86 LEU B 87 ARG B 90 ARG B 124
SITE 2 AC7 7 HOH B 437 HOH B 441 HOH B 534
SITE 1 AC8 2 ARG B 209 ARG B 229
SITE 1 AC9 4 GLU B 163 LEU B 167 ARG B 236 HOH B 491
SITE 1 BC1 4 HOH A 493 ARG B 198 ALA B 201 PHE B 202
SITE 1 BC2 3 TYR B 148 ARG B 168 ASN B 233
SITE 1 BC3 5 HIS B 9 TYR B 75 PRO B 151 VAL B 152
SITE 2 BC3 5 LYS B 212
SITE 1 BC4 1 GLN B 160
SITE 1 BC5 8 SER C 86 ARG C 90 ARG C 124 HOH C 440
SITE 2 BC5 8 HOH C 443 HOH C 474 HOH C 478 HOH C 511
SITE 1 BC6 2 LYS C 8 HIS C 9
SITE 1 BC7 2 ALA C 101 GLY C 102
SITE 1 BC8 1 ARG C 236
SITE 1 BC9 4 SER C 0 MET C 1 ARG C 126 GLN C 130
SITE 1 CC1 3 GLY B 173 HOH B 429 GLY C 173
SITE 1 CC2 3 TYR C 148 ARG C 168 ASN C 233
SITE 1 CC3 6 ARG C 69 GLY C 99 LEU C 100 ALA C 101
SITE 2 CC3 6 HOH C 505 HOH C 512
SITE 1 CC4 3 HOH C 491 HOH C 499 HOH C 533
SITE 1 CC5 2 LEU C 78 ASP C 79
CRYST1 250.499 41.589 93.081 90.00 95.89 90.00 C 1 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 0.003992 0.000000 0.000412 0.00000
SCALE2 0.000000 0.024045 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010800 0.00000
TER 1990 PHE A 252
TER 3966 ARG B 251
TER 5962 PHE C 252
MASTER 415 0 23 40 21 0 31 6 6466 3 81 63
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