HEADER LYASE 12-MAR-04 1SO4
TITLE CRYSTAL STRUCTURE OF K64A MUTANT OF 3-KETO-L-GULONATE 6-PHOSPHATE
TITLE 2 DECARBOXYLASE WITH BOUND L-THREONOHYDROXAMATE 4-PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-KETO-L-GULONATE 6-PHOSPHATE DECARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HEXULOSE-6-PHOSPHATE SYNTHASE; HUMPS; D-ARABINO 3-HEXULOSE
COMPND 5 6-PHOSPHATE FORMALDEHYDE LYASE;
COMPND 6 EC: 4.1.2.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ULAD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TIM BARREL; BETA BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.L.WISE,W.S.YEW,J.A.GERLT,I.RAYMENT
REVDAT 3 27-OCT-21 1SO4 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1SO4 1 VERSN
REVDAT 1 08-JUN-04 1SO4 0
JRNL AUTH E.L.WISE,W.S.YEW,J.A.GERLT,I.RAYMENT
JRNL TITL EVOLUTION OF ENZYMATIC ACTIVITIES IN THE OROTIDINE
JRNL TITL 2 5'-MONOPHOSPHATE DECARBOXYLASE SUPRAFAMILY: CRYSTALLOGRAPHIC
JRNL TITL 3 EVIDENCE FOR A PROTON RELAY SYSTEM IN THE ACTIVE SITE OF
JRNL TITL 4 3-KETO-L-GULONATE 6-PHOSPHATE DECARBOXYLASE(,)
JRNL REF BIOCHEMISTRY V. 43 6438 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15157078
JRNL DOI 10.1021/BI0497392
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 49331
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.400
REMARK 3 FREE R VALUE TEST SET COUNT : 3135
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3264
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 563
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.01000
REMARK 3 B22 (A**2) : 1.59000
REMARK 3 B33 (A**2) : -0.52000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.714
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
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): 3352 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3118 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4554 ; 1.610 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7198 ; 1.413 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 426 ; 6.197 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 527 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3749 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 677 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 744 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3802 ; 0.251 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2051 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 393 ; 0.182 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 65 ; 0.296 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.147 ; 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): 2119 ; 0.936 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3384 ; 1.606 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1233 ; 2.561 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1170 ; 4.046 ; 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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021866.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.961
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62079
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.575
REMARK 200 RESOLUTION RANGE LOW (A) : 91.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 42.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 5000 METHYL ETHER, 100 MM BTP
REMARK 280 PH 7.0, 5 MM MGCL2, MICROBATCH, TEMPERATURE 293K
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 61.48800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.48800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.95000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 122.97600
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2443 LIES ON A SPECIAL POSITION.
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 465 SER A 2
REMARK 465 GLY A 216
REMARK 465 MET B 1
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 GLU A 213 CG CD OE1 OE2
REMARK 470 SER B 2 OG
REMARK 470 TYR B 116 OH
REMARK 470 GLU B 120 CG CD OE1 OE2
REMARK 470 GLU B 150 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 2433 O HOH B 2563 1.93
REMARK 500 N SER B 2 O HOH B 2558 1.96
REMARK 500 O HOH B 2522 O HOH B 2562 2.06
REMARK 500 OD1 ASP B 100 O HOH B 2538 2.08
REMARK 500 OE2 GLU B 27 O HOH B 2557 2.09
REMARK 500 O HOH A 2451 O HOH A 2575 2.16
REMARK 500 O HOH A 2340 O HOH A 2577 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 30 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 82 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP B 11 58.29 -95.41
REMARK 500 ASN B 80 20.49 80.75
REMARK 500 TYR B 116 49.29 -95.46
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 MG A2300 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 33 OE2
REMARK 620 2 ASP A 62 OD2 98.1
REMARK 620 3 TX4 A1301 O1 169.7 91.7
REMARK 620 4 TX4 A1301 O2 91.0 170.9 79.2
REMARK 620 5 HOH A2576 O 85.1 93.4 91.2 86.8
REMARK 620 6 HOH A2587 O 94.3 90.5 88.8 89.4 176.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1300 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 33 OE2
REMARK 620 2 ASP B 62 OD2 95.8
REMARK 620 3 TX4 B2301 O1 171.6 92.5
REMARK 620 4 TX4 B2301 O2 92.9 171.2 78.7
REMARK 620 5 HOH B2556 O 92.1 88.7 88.9 90.0
REMARK 620 6 HOH B2569 O 88.8 93.5 89.9 87.6 177.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TX4 A 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TX4 B 2301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q6L RELATED DB: PDB
REMARK 900 RELATED ID: 1Q6O RELATED DB: PDB
REMARK 900 RELATED ID: 1Q6Q RELATED DB: PDB
REMARK 900 RELATED ID: 1Q6R RELATED DB: PDB
REMARK 900 RELATED ID: 1SO3 RELATED DB: PDB
REMARK 900 RELATED ID: 1SO5 RELATED DB: PDB
REMARK 900 RELATED ID: 1SO6 RELATED DB: PDB
DBREF 1SO4 A 1 216 UNP P39304 SGAH_ECOLI 1 216
DBREF 1SO4 B 1 216 UNP P39304 SGAH_ECOLI 1 216
SEQADV 1SO4 ALA A 64 UNP P39304 LYS 64 ENGINEERED MUTATION
SEQADV 1SO4 ALA B 64 UNP P39304 LYS 64 ENGINEERED MUTATION
SEQRES 1 A 216 MET SER LEU PRO MET LEU GLN VAL ALA LEU ASP ASN GLN
SEQRES 2 A 216 THR MET ASP SER ALA TYR GLU THR THR ARG LEU ILE ALA
SEQRES 3 A 216 GLU GLU VAL ASP ILE ILE GLU VAL GLY THR ILE LEU CYS
SEQRES 4 A 216 VAL GLY GLU GLY VAL ARG ALA VAL ARG ASP LEU LYS ALA
SEQRES 5 A 216 LEU TYR PRO HIS LYS ILE VAL LEU ALA ASP ALA ALA ILE
SEQRES 6 A 216 ALA ASP ALA GLY LYS ILE LEU SER ARG MET CYS PHE GLU
SEQRES 7 A 216 ALA ASN ALA ASP TRP VAL THR VAL ILE CYS CYS ALA ASP
SEQRES 8 A 216 ILE ASN THR ALA LYS GLY ALA LEU ASP VAL ALA LYS GLU
SEQRES 9 A 216 PHE ASN GLY ASP VAL GLN ILE GLU LEU THR GLY TYR TRP
SEQRES 10 A 216 THR TRP GLU GLN ALA GLN GLN TRP ARG ASP ALA GLY ILE
SEQRES 11 A 216 GLY GLN VAL VAL TYR HIS ARG SER ARG ASP ALA GLN ALA
SEQRES 12 A 216 ALA GLY VAL ALA TRP GLY GLU ALA ASP ILE THR ALA ILE
SEQRES 13 A 216 LYS ARG LEU SER ASP MET GLY PHE LYS VAL THR VAL THR
SEQRES 14 A 216 GLY GLY LEU ALA LEU GLU ASP LEU PRO LEU PHE LYS GLY
SEQRES 15 A 216 ILE PRO ILE HIS VAL PHE ILE ALA GLY ARG SER ILE ARG
SEQRES 16 A 216 ASP ALA ALA SER PRO VAL GLU ALA ALA ARG GLN PHE LYS
SEQRES 17 A 216 ARG SER ILE ALA GLU LEU TRP GLY
SEQRES 1 B 216 MET SER LEU PRO MET LEU GLN VAL ALA LEU ASP ASN GLN
SEQRES 2 B 216 THR MET ASP SER ALA TYR GLU THR THR ARG LEU ILE ALA
SEQRES 3 B 216 GLU GLU VAL ASP ILE ILE GLU VAL GLY THR ILE LEU CYS
SEQRES 4 B 216 VAL GLY GLU GLY VAL ARG ALA VAL ARG ASP LEU LYS ALA
SEQRES 5 B 216 LEU TYR PRO HIS LYS ILE VAL LEU ALA ASP ALA ALA ILE
SEQRES 6 B 216 ALA ASP ALA GLY LYS ILE LEU SER ARG MET CYS PHE GLU
SEQRES 7 B 216 ALA ASN ALA ASP TRP VAL THR VAL ILE CYS CYS ALA ASP
SEQRES 8 B 216 ILE ASN THR ALA LYS GLY ALA LEU ASP VAL ALA LYS GLU
SEQRES 9 B 216 PHE ASN GLY ASP VAL GLN ILE GLU LEU THR GLY TYR TRP
SEQRES 10 B 216 THR TRP GLU GLN ALA GLN GLN TRP ARG ASP ALA GLY ILE
SEQRES 11 B 216 GLY GLN VAL VAL TYR HIS ARG SER ARG ASP ALA GLN ALA
SEQRES 12 B 216 ALA GLY VAL ALA TRP GLY GLU ALA ASP ILE THR ALA ILE
SEQRES 13 B 216 LYS ARG LEU SER ASP MET GLY PHE LYS VAL THR VAL THR
SEQRES 14 B 216 GLY GLY LEU ALA LEU GLU ASP LEU PRO LEU PHE LYS GLY
SEQRES 15 B 216 ILE PRO ILE HIS VAL PHE ILE ALA GLY ARG SER ILE ARG
SEQRES 16 B 216 ASP ALA ALA SER PRO VAL GLU ALA ALA ARG GLN PHE LYS
SEQRES 17 B 216 ARG SER ILE ALA GLU LEU TRP GLY
HET MG A2300 1
HET TX4 A1301 14
HET MG B1300 1
HET TX4 B2301 14
HETNAM MG MAGNESIUM ION
HETNAM TX4 L-THREONOHYDROXAMATE 4-PHOSPHATE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 TX4 2(C4 H12 N O8 P)
FORMUL 7 HOH *563(H2 O)
HELIX 1 1 THR A 14 ALA A 26 1 13
HELIX 2 2 GLU A 27 VAL A 29 5 3
HELIX 3 3 GLY A 35 GLY A 43 1 9
HELIX 4 4 VAL A 44 TYR A 54 1 11
HELIX 5 5 ALA A 68 ALA A 79 1 12
HELIX 6 6 ASP A 91 PHE A 105 1 15
HELIX 7 7 THR A 118 ALA A 128 1 11
HELIX 8 8 SER A 138 ALA A 144 1 7
HELIX 9 9 GLY A 149 MET A 162 1 14
HELIX 10 10 ALA A 173 LYS A 181 5 9
HELIX 11 11 GLY A 191 ASP A 196 1 6
HELIX 12 12 SER A 199 TRP A 215 1 17
HELIX 13 13 THR B 14 ALA B 26 1 13
HELIX 14 14 GLU B 27 VAL B 29 5 3
HELIX 15 15 GLY B 35 GLY B 43 1 9
HELIX 16 16 VAL B 44 TYR B 54 1 11
HELIX 17 17 ALA B 68 ALA B 79 1 12
HELIX 18 18 ASP B 91 PHE B 105 1 15
HELIX 19 19 THR B 118 GLY B 129 1 12
HELIX 20 20 SER B 138 ALA B 144 1 7
HELIX 21 21 GLY B 149 MET B 162 1 14
HELIX 22 22 ALA B 173 LYS B 181 5 9
HELIX 23 23 GLY B 191 ASP B 196 1 6
HELIX 24 24 SER B 199 TRP B 215 1 17
SHEET 1 A 9 MET A 5 LEU A 10 0
SHEET 2 A 9 ILE A 31 VAL A 34 1 O GLU A 33 N VAL A 8
SHEET 3 A 9 ILE A 58 ILE A 65 1 O LEU A 60 N VAL A 34
SHEET 4 A 9 TRP A 83 ILE A 87 1 O TRP A 83 N ALA A 61
SHEET 5 A 9 ASP A 108 LEU A 113 1 O GLU A 112 N VAL A 86
SHEET 6 A 9 GLN A 132 HIS A 136 1 O VAL A 134 N LEU A 113
SHEET 7 A 9 LYS A 165 THR A 169 1 O THR A 167 N TYR A 135
SHEET 8 A 9 VAL A 187 ALA A 190 1 O VAL A 187 N VAL A 168
SHEET 9 A 9 MET A 5 LEU A 10 1 N MET A 5 O PHE A 188
SHEET 1 B 9 MET B 5 LEU B 10 0
SHEET 2 B 9 ILE B 31 VAL B 34 1 O GLU B 33 N VAL B 8
SHEET 3 B 9 ILE B 58 ILE B 65 1 O LEU B 60 N VAL B 34
SHEET 4 B 9 TRP B 83 ILE B 87 1 O TRP B 83 N ALA B 61
SHEET 5 B 9 ASP B 108 LEU B 113 1 O GLU B 112 N VAL B 86
SHEET 6 B 9 GLN B 132 HIS B 136 1 O VAL B 134 N LEU B 113
SHEET 7 B 9 LYS B 165 THR B 169 1 O THR B 167 N TYR B 135
SHEET 8 B 9 VAL B 187 ALA B 190 1 O VAL B 187 N VAL B 168
SHEET 9 B 9 MET B 5 LEU B 10 1 N GLN B 7 O ALA B 190
SSBOND 1 CYS A 89 CYS B 89 1555 1555 2.04
LINK OE2 GLU A 33 MG MG A2300 1555 1555 2.03
LINK OD2 ASP A 62 MG MG A2300 1555 1555 2.04
LINK O1 TX4 A1301 MG MG A2300 1555 1555 2.04
LINK O2 TX4 A1301 MG MG A2300 1555 1555 2.11
LINK MG MG A2300 O HOH A2576 1555 1555 2.19
LINK MG MG A2300 O HOH A2587 1555 1555 2.04
LINK OE2 GLU B 33 MG MG B1300 1555 1555 2.01
LINK OD2 ASP B 62 MG MG B1300 1555 1555 2.04
LINK MG MG B1300 O1 TX4 B2301 1555 1555 2.00
LINK MG MG B1300 O2 TX4 B2301 1555 1555 2.13
LINK MG MG B1300 O HOH B2556 1555 1555 2.17
LINK MG MG B1300 O HOH B2569 1555 1555 2.07
SITE 1 AC1 5 GLU B 33 ASP B 62 TX4 B2301 HOH B2556
SITE 2 AC1 5 HOH B2569
SITE 1 AC2 5 GLU A 33 ASP A 62 TX4 A1301 HOH A2576
SITE 2 AC2 5 HOH A2587
SITE 1 AC3 18 ALA A 9 ASP A 11 GLU A 33 ASP A 62
SITE 2 AC3 18 HIS A 136 THR A 169 GLY A 171 GLY A 191
SITE 3 AC3 18 ARG A 192 MG A2300 HOH A2307 HOH A2313
SITE 4 AC3 18 HOH A2337 HOH A2391 HOH A2464 HOH A2576
SITE 5 AC3 18 HOH A2587 ASP B 67
SITE 1 AC4 20 ASP A 67 ALA B 9 ASP B 11 GLU B 33
SITE 2 AC4 20 ASP B 62 HIS B 136 THR B 169 GLY B 171
SITE 3 AC4 20 GLY B 191 ARG B 192 MG B1300 HOH B2302
SITE 4 AC4 20 HOH B2303 HOH B2329 HOH B2343 HOH B2345
SITE 5 AC4 20 HOH B2437 HOH B2489 HOH B2556 HOH B2569
CRYST1 122.976 41.900 91.322 90.00 96.92 90.00 C 1 2 1 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 0.008132 0.000000 0.000987 0.00000
SCALE2 0.000000 0.023866 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011031 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
