HEADER TRANSFERASE/TRANSFERASE INHIBITOR 21-SEP-11 3TWD
TITLE GLMUC1 IN COMPLEX WITH AN ANTIBACTERIAL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL PROTEIN GLMU;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 233-452;
COMPND 5 SYNONYM: UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE, N-
COMPND 6 ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLUCOSAMINE-1-
COMPND 7 PHOSPHATE N-ACETYLTRANSFERASE;
COMPND 8 EC: 2.7.7.23, 2.3.1.157;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: GLMU, YIEA, B3730, JW3708;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACETYL TRANSFERASE, URIDYL TRANSFERASE, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LAHIRI,L.OTTERBEIN
REVDAT 4 28-FEB-24 3TWD 1 REMARK SEQADV
REVDAT 3 14-DEC-11 3TWD 1 JRNL
REVDAT 2 26-OCT-11 3TWD 1 JRNL
REVDAT 1 19-OCT-11 3TWD 0
JRNL AUTH E.T.BUURMAN,B.ANDREWS,N.GAO,J.HU,T.A.KEATING,S.LAHIRI,
JRNL AUTH 2 L.R.OTTERBEIN,A.D.PATTEN,S.S.STOKES,A.B.SHAPIRO
JRNL TITL IN VITRO VALIDATION OF ACETYLTRANSFERASE ACTIVITY OF GLMU AS
JRNL TITL 2 AN ANTIBACTERIAL TARGET IN HAEMOPHILUS INFLUENZAE.
JRNL REF J.BIOL.CHEM. V. 286 40734 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21984832
JRNL DOI 10.1074/JBC.M111.274068
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0034
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 38936
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) : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1945
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2051
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3294
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 388
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : -0.01000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.082
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3514 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2298 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4778 ; 1.396 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5620 ; 0.866 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 462 ; 6.344 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;32.618 ;23.803
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 584 ;13.412 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;14.311 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 548 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4012 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 676 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 678 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2452 ; 0.207 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1753 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2026 ; 0.079 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 299 ; 0.159 ; 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): 35 ; 0.132 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 148 ; 0.291 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 42 ; 0.125 ; 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): 2323 ; 0.840 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 946 ; 0.199 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3604 ; 1.102 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1361 ; 2.247 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1174 ; 3.447 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 232 A 453
REMARK 3 RESIDUE RANGE : B 232 B 453
REMARK 3 RESIDUE RANGE : A 2 A 2
REMARK 3 RESIDUE RANGE : B 1 B 1
REMARK 3 RESIDUE RANGE : A 1 A 1
REMARK 3 RESIDUE RANGE : B 454 B 454
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8083 -0.1358 0.0117
REMARK 3 T TENSOR
REMARK 3 T11: -0.0280 T22: -0.0127
REMARK 3 T33: -0.0087 T12: -0.0004
REMARK 3 T13: 0.0017 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.1017 L22: 0.3552
REMARK 3 L33: 0.0598 L12: 0.0032
REMARK 3 L13: 0.0055 L23: 0.0013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: -0.0026 S13: -0.0019
REMARK 3 S21: 0.0032 S22: 0.0031 S23: 0.0068
REMARK 3 S31: 0.0021 S32: 0.0023 S33: -0.0067
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3TWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068002.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.5
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 : RIGAKU FR-E+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 69.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19-22% (W/V) PEG3350, 100MM PCTP PH
REMARK 280 5.5 AND 400MM AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
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 69.92500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 69.92500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.92500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 40.26300
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -69.73756
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 80.52600
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 80.52600
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 40.26300
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 69.73756
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 29530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -214.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 40.26300
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -69.73756
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 80.52600
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 80.52600
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 69.92500
REMARK 350 BIOMT1 5 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 69.92500
REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 40.26300
REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 -69.73756
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 69.92500
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 A 460 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 478 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 509 LIES ON A SPECIAL POSITION.
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 A 507 O HOH B 517 1.92
REMARK 500 O HOH B 3 O HOH B 525 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 178 O HOH B 178 2655 1.06
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 ALA A 390 -48.62 -130.92
REMARK 500 ASN A 434 18.28 59.13
REMARK 500 SER B 439 72.36 -154.07
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 B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOB A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOB B 454
DBREF 3TWD A 233 452 UNP P0ACC7 GLMU_ECOLI 233 452
DBREF 3TWD B 233 452 UNP P0ACC7 GLMU_ECOLI 233 452
SEQADV 3TWD ALA A 232 UNP P0ACC7 EXPRESSION TAG
SEQADV 3TWD ALA A 453 UNP P0ACC7 EXPRESSION TAG
SEQADV 3TWD ALA B 232 UNP P0ACC7 EXPRESSION TAG
SEQADV 3TWD ALA B 453 UNP P0ACC7 EXPRESSION TAG
SEQRES 1 A 222 ALA SER ARG LEU GLU ARG VAL TYR GLN SER GLU GLN ALA
SEQRES 2 A 222 GLU LYS LEU LEU LEU ALA GLY VAL MET LEU ARG ASP PRO
SEQRES 3 A 222 ALA ARG PHE ASP LEU ARG GLY THR LEU THR HIS GLY ARG
SEQRES 4 A 222 ASP VAL GLU ILE ASP THR ASN VAL ILE ILE GLU GLY ASN
SEQRES 5 A 222 VAL THR LEU GLY HIS ARG VAL LYS ILE GLY THR GLY CYS
SEQRES 6 A 222 VAL ILE LYS ASN SER VAL ILE GLY ASP ASP CYS GLU ILE
SEQRES 7 A 222 SER PRO TYR THR VAL VAL GLU ASP ALA ASN LEU ALA ALA
SEQRES 8 A 222 ALA CYS THR ILE GLY PRO PHE ALA ARG LEU ARG PRO GLY
SEQRES 9 A 222 ALA GLU LEU LEU GLU GLY ALA HIS VAL GLY ASN PHE VAL
SEQRES 10 A 222 GLU MET LYS LYS ALA ARG LEU GLY LYS GLY SER LYS ALA
SEQRES 11 A 222 GLY HIS LEU THR TYR LEU GLY ASP ALA GLU ILE GLY ASP
SEQRES 12 A 222 ASN VAL ASN ILE GLY ALA GLY THR ILE THR CYS ASN TYR
SEQRES 13 A 222 ASP GLY ALA ASN LYS PHE LYS THR ILE ILE GLY ASP ASP
SEQRES 14 A 222 VAL PHE VAL GLY SER ASP THR GLN LEU VAL ALA PRO VAL
SEQRES 15 A 222 THR VAL GLY LYS GLY ALA THR ILE ALA ALA GLY THR THR
SEQRES 16 A 222 VAL THR ARG ASN VAL GLY GLU ASN ALA LEU ALA ILE SER
SEQRES 17 A 222 ARG VAL PRO GLN THR GLN LYS GLU GLY TRP ARG ARG PRO
SEQRES 18 A 222 ALA
SEQRES 1 B 222 ALA SER ARG LEU GLU ARG VAL TYR GLN SER GLU GLN ALA
SEQRES 2 B 222 GLU LYS LEU LEU LEU ALA GLY VAL MET LEU ARG ASP PRO
SEQRES 3 B 222 ALA ARG PHE ASP LEU ARG GLY THR LEU THR HIS GLY ARG
SEQRES 4 B 222 ASP VAL GLU ILE ASP THR ASN VAL ILE ILE GLU GLY ASN
SEQRES 5 B 222 VAL THR LEU GLY HIS ARG VAL LYS ILE GLY THR GLY CYS
SEQRES 6 B 222 VAL ILE LYS ASN SER VAL ILE GLY ASP ASP CYS GLU ILE
SEQRES 7 B 222 SER PRO TYR THR VAL VAL GLU ASP ALA ASN LEU ALA ALA
SEQRES 8 B 222 ALA CYS THR ILE GLY PRO PHE ALA ARG LEU ARG PRO GLY
SEQRES 9 B 222 ALA GLU LEU LEU GLU GLY ALA HIS VAL GLY ASN PHE VAL
SEQRES 10 B 222 GLU MET LYS LYS ALA ARG LEU GLY LYS GLY SER LYS ALA
SEQRES 11 B 222 GLY HIS LEU THR TYR LEU GLY ASP ALA GLU ILE GLY ASP
SEQRES 12 B 222 ASN VAL ASN ILE GLY ALA GLY THR ILE THR CYS ASN TYR
SEQRES 13 B 222 ASP GLY ALA ASN LYS PHE LYS THR ILE ILE GLY ASP ASP
SEQRES 14 B 222 VAL PHE VAL GLY SER ASP THR GLN LEU VAL ALA PRO VAL
SEQRES 15 B 222 THR VAL GLY LYS GLY ALA THR ILE ALA ALA GLY THR THR
SEQRES 16 B 222 VAL THR ARG ASN VAL GLY GLU ASN ALA LEU ALA ILE SER
SEQRES 17 B 222 ARG VAL PRO GLN THR GLN LYS GLU GLY TRP ARG ARG PRO
SEQRES 18 B 222 ALA
HET SO4 A 2 5
HET GOB A 1 35
HET SO4 B 1 5
HET GOB B 454 35
HETNAM SO4 SULFATE ION
HETNAM GOB 4-({5-[(4-AMINOPHENYL)(PHENYL)SULFAMOYL]-2,4-
HETNAM 2 GOB DIMETHOXYPHENYL}AMINO)-4-OXOBUTANOIC ACID
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 GOB 2(C24 H25 N3 O7 S)
FORMUL 7 HOH *388(H2 O)
HELIX 1 1 ALA A 232 ALA A 250 1 19
HELIX 2 2 ASP A 256 ALA A 258 5 3
HELIX 3 3 SER B 233 ALA B 250 1 18
HELIX 4 4 ASP B 256 ALA B 258 5 3
SHEET 1 A 7 VAL A 413 VAL A 415 0
SHEET 2 A 7 THR A 395 ILE A 397 1 N ILE A 396 O VAL A 415
SHEET 3 A 7 LYS A 360 ILE A 372 1 N GLU A 371 O ILE A 397
SHEET 4 A 7 ASN A 377 ILE A 378 1 O ILE A 378 N LYS A 360
SHEET 5 A 7 PHE A 402 VAL A 403 1 O VAL A 403 N ASN A 377
SHEET 6 A 7 THR A 420 ILE A 421 1 O ILE A 421 N PHE A 402
SHEET 7 A 7 LEU A 436 ALA A 437 1 O ALA A 437 N THR A 420
SHEET 1 B 6 LYS A 360 ILE A 372 0
SHEET 2 B 6 HIS A 343 LEU A 355 1 N GLU A 349 O THR A 365
SHEET 3 B 6 GLU A 337 LEU A 338 1 N GLU A 337 O LEU A 355
SHEET 4 B 6 ASN A 319 LEU A 320 1 N ASN A 319 O LEU A 338
SHEET 5 B 6 VAL A 302 ILE A 303 1 N VAL A 302 O LEU A 320
SHEET 6 B 6 VAL A 278 LEU A 286 1 N THR A 285 O ILE A 303
SHEET 1 C11 MET A 253 LEU A 254 0
SHEET 2 C11 GLU A 273 ILE A 274 1 O ILE A 274 N MET A 253
SHEET 3 C11 LYS A 291 ILE A 292 1 O ILE A 292 N GLU A 273
SHEET 4 C11 GLU A 308 ILE A 309 1 O ILE A 309 N LYS A 291
SHEET 5 C11 THR A 325 ILE A 326 1 O ILE A 326 N GLU A 308
SHEET 6 C11 HIS A 343 LEU A 355 1 O VAL A 344 N THR A 325
SHEET 7 C11 ALA A 330 LEU A 332 1 N ARG A 331 O VAL A 348
SHEET 8 C11 VAL A 314 GLU A 316 1 N VAL A 314 O LEU A 332
SHEET 9 C11 VAL A 297 LYS A 299 1 N VAL A 297 O VAL A 315
SHEET 10 C11 VAL A 278 LEU A 286 1 N ILE A 279 O ILE A 298
SHEET 11 C11 PHE A 260 HIS A 268 1 N ARG A 263 O ILE A 280
SHEET 1 D 3 ILE A 383 CYS A 385 0
SHEET 2 D 3 GLN A 408 VAL A 410 1 O LEU A 409 N CYS A 385
SHEET 3 D 3 THR A 426 VAL A 427 1 O VAL A 427 N GLN A 408
SHEET 1 E 7 VAL B 413 VAL B 415 0
SHEET 2 E 7 THR B 395 ILE B 397 1 N ILE B 396 O VAL B 415
SHEET 3 E 7 LYS B 360 ILE B 372 1 N GLU B 371 O ILE B 397
SHEET 4 E 7 ASN B 377 ILE B 378 1 O ILE B 378 N LYS B 360
SHEET 5 E 7 PHE B 402 VAL B 403 1 O VAL B 403 N ASN B 377
SHEET 6 E 7 THR B 420 ILE B 421 1 O ILE B 421 N PHE B 402
SHEET 7 E 7 LEU B 436 ALA B 437 1 O ALA B 437 N THR B 420
SHEET 1 F 6 LYS B 360 ILE B 372 0
SHEET 2 F 6 HIS B 343 LEU B 355 1 N GLY B 345 O ALA B 361
SHEET 3 F 6 ALA B 336 LEU B 338 1 N GLU B 337 O ALA B 353
SHEET 4 F 6 ASN B 319 LEU B 320 1 N ASN B 319 O LEU B 338
SHEET 5 F 6 VAL B 302 ILE B 303 1 N VAL B 302 O LEU B 320
SHEET 6 F 6 VAL B 278 LEU B 286 1 N THR B 285 O ILE B 303
SHEET 1 G11 MET B 253 LEU B 254 0
SHEET 2 G11 GLU B 273 ILE B 274 1 O ILE B 274 N MET B 253
SHEET 3 G11 LYS B 291 ILE B 292 1 O ILE B 292 N GLU B 273
SHEET 4 G11 GLU B 308 ILE B 309 1 O ILE B 309 N LYS B 291
SHEET 5 G11 THR B 325 ILE B 326 1 O ILE B 326 N GLU B 308
SHEET 6 G11 HIS B 343 LEU B 355 1 O VAL B 344 N THR B 325
SHEET 7 G11 ALA B 330 LEU B 332 1 N ARG B 331 O VAL B 348
SHEET 8 G11 VAL B 314 GLU B 316 1 N VAL B 314 O LEU B 332
SHEET 9 G11 VAL B 297 LYS B 299 1 N VAL B 297 O VAL B 315
SHEET 10 G11 VAL B 278 LEU B 286 1 N GLU B 281 O ILE B 298
SHEET 11 G11 PHE B 260 HIS B 268 1 N ARG B 263 O ILE B 280
SHEET 1 H 3 ILE B 383 CYS B 385 0
SHEET 2 H 3 GLN B 408 VAL B 410 1 O LEU B 409 N CYS B 385
SHEET 3 H 3 THR B 426 VAL B 427 1 O VAL B 427 N GLN B 408
CISPEP 1 GLY A 327 PRO A 328 0 -0.72
CISPEP 2 ALA A 411 PRO A 412 0 -4.58
CISPEP 3 GLY B 327 PRO B 328 0 -0.43
CISPEP 4 ALA B 411 PRO B 412 0 -4.52
SITE 1 AC1 9 HOH B 4 HOH B 158 HOH B 183 ARG B 333
SITE 2 AC1 9 LYS B 351 HIS B 363 TYR B 366 ASN B 386
SITE 3 AC1 9 LYS B 392
SITE 1 AC2 9 HOH A 12 HOH A 104 HOH A 142 ARG A 333
SITE 2 AC2 9 LYS A 351 HIS A 363 TYR A 366 ASN A 386
SITE 3 AC2 9 LYS A 392
SITE 1 AC3 18 HOH A 114 HOH A 205 ASN A 377 GLY A 379
SITE 2 AC3 18 ALA A 380 CYS A 385 TYR A 387 ASP A 388
SITE 3 AC3 18 PHE A 402 GLY A 404 SER A 405 VAL A 410
SITE 4 AC3 18 ALA A 411 ALA A 422 ALA A 423 ARG A 440
SITE 5 AC3 18 PRO A 452 HOH A 472
SITE 1 AC4 21 HOH B 116 HOH B 220 ASN B 377 GLY B 379
SITE 2 AC4 21 ALA B 380 CYS B 385 ASN B 386 TYR B 387
SITE 3 AC4 21 ASP B 388 PHE B 402 GLY B 404 SER B 405
SITE 4 AC4 21 VAL B 410 ALA B 411 ALA B 422 ALA B 423
SITE 5 AC4 21 ARG B 440 TRP B 449 PRO B 452 HOH B 455
SITE 6 AC4 21 HOH B 472
CRYST1 80.526 80.526 139.850 90.00 90.00 120.00 P 63 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 0.012418 0.007170 0.000000 0.00000
SCALE2 0.000000 0.014339 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
