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HEADER LYASE 01-AUG-12 4GEC
TITLE CRYSTAL STRUCTURE OF E.COLI MENH R124A 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_R124AMUTANT, 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, MUTANT R124A, MENH MUTANT
KEYWDS 3 R124A, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M JOHNSTON,E.N.BAKER,Z.GUO,M.JIANG
REVDAT 2 15-MAY-13 4GEC 1 JRNL
REVDAT 1 08-MAY-13 4GEC 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. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 54795
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2792
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.13
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3958
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2448
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3743
REMARK 3 BIN R VALUE (WORKING SET) : 0.2433
REMARK 3 BIN FREE R VALUE : 0.2708
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.43
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 215
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 : 5923
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 232
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.71330
REMARK 3 B22 (A**2) : -3.71330
REMARK 3 B33 (A**2) : 7.42650
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) : 0.32
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.22
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.19
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.22
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.19
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 : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6087 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8267 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2735 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 150 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 917 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6087 ; 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 : 742 ; 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 : 7679 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.23
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.06
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 4GEC 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 RCSB074076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-10
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) : 0.953692
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 : 54795
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 117.444
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 14.900
REMARK 200 R MERGE (I) : 0.19000
REMARK 200 R SYM (I) : 0.19000
REMARK 200 FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.20
REMARK 200 R MERGE FOR SHELL (I) : 1.84700
REMARK 200 R SYM FOR SHELL (I) : 1.84700
REMARK 200 FOR SHELL : 1.800
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 (%): 72.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.41
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: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 57.57200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 57.57200
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 234.88750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 57.57200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 117.44375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 57.57200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 352.33125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 57.57200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 352.33125
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.57200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.44375
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 57.57200
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 57.57200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 234.88750
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 57.57200
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 57.57200
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 234.88750
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 57.57200
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 352.33125
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 57.57200
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 117.44375
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 57.57200
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 117.44375
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 57.57200
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 352.33125
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 57.57200
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 57.57200
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 234.88750
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: 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 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: 3
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: 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 LEU A -5
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 VAL B -4
REMARK 465 PRO B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
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 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 -1.33 79.75
REMARK 500 SER A 86 -106.88 47.48
REMARK 500 ALA A 197 39.64 -79.90
REMARK 500 SER B 24 -11.79 73.96
REMARK 500 PHE B 37 56.81 -90.20
REMARK 500 SER B 86 -107.43 46.78
REMARK 500 SER C 24 -4.41 75.73
REMARK 500 SER C 86 -102.36 51.46
REMARK 500 ASP C 190 95.97 -65.71
REMARK 500 ALA C 218 -3.05 -59.63
REMARK 500
REMARK 500 REMARK: NULL
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 GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 302
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: 4GEG RELATED DB: PDB
REMARK 900 E. COLI MENH Y85F MUTANT STRUCTURE
DBREF 4GEC A 1 252 UNP P37355 MENH_ECOLI 1 252
DBREF 4GEC B 1 252 UNP P37355 MENH_ECOLI 1 252
DBREF 4GEC C 1 252 UNP P37355 MENH_ECOLI 1 252
SEQADV 4GEC MET A -15 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS A -14 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS A -13 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS A -12 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS A -11 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS A -10 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS A -9 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER A -8 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER A -7 UNP P37355 EXPRESSION TAG
SEQADV 4GEC GLY A -6 UNP P37355 EXPRESSION TAG
SEQADV 4GEC LEU A -5 UNP P37355 EXPRESSION TAG
SEQADV 4GEC VAL A -4 UNP P37355 EXPRESSION TAG
SEQADV 4GEC PRO A -3 UNP P37355 EXPRESSION TAG
SEQADV 4GEC ARG A -2 UNP P37355 EXPRESSION TAG
SEQADV 4GEC GLY A -1 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER A 0 UNP P37355 EXPRESSION TAG
SEQADV 4GEC ALA A 124 UNP P37355 ARG 124 ENGINEERED MUTATION
SEQADV 4GEC MET B -15 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS B -14 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS B -13 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS B -12 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS B -11 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS B -10 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS B -9 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER B -8 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER B -7 UNP P37355 EXPRESSION TAG
SEQADV 4GEC GLY B -6 UNP P37355 EXPRESSION TAG
SEQADV 4GEC LEU B -5 UNP P37355 EXPRESSION TAG
SEQADV 4GEC VAL B -4 UNP P37355 EXPRESSION TAG
SEQADV 4GEC PRO B -3 UNP P37355 EXPRESSION TAG
SEQADV 4GEC ARG B -2 UNP P37355 EXPRESSION TAG
SEQADV 4GEC GLY B -1 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER B 0 UNP P37355 EXPRESSION TAG
SEQADV 4GEC ALA B 124 UNP P37355 ARG 124 ENGINEERED MUTATION
SEQADV 4GEC MET C -15 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS C -14 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS C -13 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS C -12 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS C -11 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS C -10 UNP P37355 EXPRESSION TAG
SEQADV 4GEC HIS C -9 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER C -8 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER C -7 UNP P37355 EXPRESSION TAG
SEQADV 4GEC GLY C -6 UNP P37355 EXPRESSION TAG
SEQADV 4GEC LEU C -5 UNP P37355 EXPRESSION TAG
SEQADV 4GEC VAL C -4 UNP P37355 EXPRESSION TAG
SEQADV 4GEC PRO C -3 UNP P37355 EXPRESSION TAG
SEQADV 4GEC ARG C -2 UNP P37355 EXPRESSION TAG
SEQADV 4GEC GLY C -1 UNP P37355 EXPRESSION TAG
SEQADV 4GEC SER C 0 UNP P37355 EXPRESSION TAG
SEQADV 4GEC ALA C 124 UNP P37355 ARG 124 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 TYR 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 ALA 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 TYR 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 ALA 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 TYR 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 ALA 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 GOL A 303 6
HET CL A 304 1
HET EDO A 305 4
HET SO4 B 301 5
HET CL B 302 1
HET SO4 C 301 5
HET CL C 302 1
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 6 GOL C3 H8 O3
FORMUL 7 CL 3(CL 1-)
FORMUL 8 EDO C2 H6 O2
FORMUL 13 HOH *232(H2 O)
HELIX 1 1 TRP A 30 GLU A 35 1 6
HELIX 2 2 ALA A 36 ALA A 38 5 3
HELIX 3 3 HIS A 50 ALA A 54 5 5
HELIX 4 4 GLY A 60 TYR A 75 1 16
HELIX 5 5 SER A 86 GLY A 99 1 14
HELIX 6 6 ASN A 117 GLU A 138 1 22
HELIX 7 7 PRO A 139 TYR A 148 1 10
HELIX 8 8 GLN A 149 ALA A 154 5 6
HELIX 9 9 ASN A 157 SER A 169 1 13
HELIX 10 10 ASN A 172 THR A 183 1 12
HELIX 11 11 LEU A 191 ALA A 197 1 7
HELIX 12 12 ASP A 210 GLU A 219 1 10
HELIX 13 13 ASN A 233 ASN A 238 1 6
HELIX 14 14 ASN A 238 ARG A 251 1 14
HELIX 15 15 TRP B 30 GLU B 35 1 6
HELIX 16 16 HIS B 50 ALA B 54 5 5
HELIX 17 17 GLY B 60 TYR B 75 1 16
HELIX 18 18 SER B 86 GLY B 99 1 14
HELIX 19 19 ASN B 117 GLU B 138 1 22
HELIX 20 20 PRO B 139 TYR B 148 1 10
HELIX 21 21 GLN B 149 ALA B 154 5 6
HELIX 22 22 ASN B 157 SER B 169 1 13
HELIX 23 23 ASN B 172 THR B 183 1 12
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 ASN C 76 1 17
HELIX 31 31 SER C 86 GLY C 99 1 14
HELIX 32 32 ASN C 117 GLU C 138 1 22
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 SER C 184 GLN C 188 5 5
HELIX 38 38 LEU C 191 ALA C 197 1 7
HELIX 39 39 ASP C 210 ALA C 218 1 9
HELIX 40 40 ASN C 233 ASN C 238 1 6
HELIX 41 41 ASN C 238 PHE C 252 1 15
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 TYR A 85 1 O TRP A 81 N VAL A 18
SHEET 5 A 7 LEU A 103 GLU A 109 1 O CYS A 104 N PHE A 80
SHEET 6 A 7 ALA A 201 GLY A 207 1 O LEU A 205 N VAL A 108
SHEET 7 A 7 ASP A 223 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 TYR B 85 1 O VAL B 83 N VAL B 18
SHEET 5 B 7 LEU B 103 GLU B 109 1 O CYS B 104 N PHE B 80
SHEET 6 B 7 ALA B 201 GLY B 207 1 O TYR B 203 N VAL B 106
SHEET 7 B 7 ASP B 223 ILE B 227 1 O HIS B 225 N TYR B 204
SHEET 1 C 7 ALA C 5 LYS C 8 0
SHEET 2 C 7 SER C 41 VAL C 45 -1 O TYR C 44 N GLN C 6
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 TYR C 85 1 O VAL C 83 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 PHE C 202 GLY C 207 1 O LEU C 205 N VAL C 108
SHEET 7 C 7 ASP C 223 ILE C 227 1 O HIS C 225 N TYR C 204
CISPEP 1 GLY C -6 LEU C -5 0 0.22
SITE 1 AC1 5 LYS A 8 HIS A 9 PRO C 15 TRP C 81
SITE 2 AC1 5 CYS C 104
SITE 1 AC2 6 SER A 86 LEU A 87 ARG A 90 HOH A 401
SITE 2 AC2 6 HOH A 408 HOH A 451
SITE 1 AC3 6 ARG A 198 PHE A 200 ALA A 201 PHE A 202
SITE 2 AC3 6 HOH A 422 HIS B 9
SITE 1 AC4 6 TYR A 85 TYR A 148 ARG A 168 ASN A 233
SITE 2 AC4 6 HOH A 434 HOH A 493
SITE 1 AC5 7 ALA A 36 ALA A 247 ARG A 251 ALA B 36
SITE 2 AC5 7 PHE B 37 ALA B 247 ARG B 251
SITE 1 AC6 6 SER B 86 LEU B 87 ARG B 90 HOH B 437
SITE 2 AC6 6 HOH B 446 HOH B 449
SITE 1 AC7 4 TYR B 85 TYR B 148 ARG B 168 ASN B 233
SITE 1 AC8 4 SER C 86 LEU C 87 ARG C 90 HOH C 401
SITE 1 AC9 4 TYR C 85 TYR C 148 ARG C 168 ASN C 233
CRYST1 115.144 115.144 469.775 90.00 90.00 90.00 I 41 2 2 48
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 0.008685 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008685 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002129 0.00000
TER 1977 PHE A 252
TER 3931 PHE B 252
TER 5926 PHE C 252
MASTER 399 0 9 41 21 0 15 6 6188 3 30 63
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