HEADER TRANSFERASE 16-MAR-12 4E6U
TITLE STRUCTURE OF LPXA FROM ACINETOBACTER BAUMANNII AT 1.4A RESOLUTION (P63
TITLE 2 FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-
COMPND 3 ACYLTRANSFERASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: UDP-N-ACETYLGLUCOSAMINE ACYLTRANSFERASE;
COMPND 6 EC: 2.3.1.129;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER BAUMANNII;
SOURCE 3 ORGANISM_TAXID: 470;
SOURCE 4 GENE: LPXA, ABTW07_2294;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: BL21 (DE3)
KEYWDS LIPOPOLYSACCARIDE SYNTHESIS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BADGER,B.CHIE-LEON,C.LOGAN,V.SRIDHAR,B.SANKARAN,P.H.ZWART,
AUTHOR 2 V.NIENABER
REVDAT 2 28-FEB-24 4E6U 1 REMARK SEQADV
REVDAT 1 12-DEC-12 4E6U 0
JRNL AUTH J.BADGER,B.CHIE-LEON,C.LOGAN,V.SRIDHAR,B.SANKARAN,P.H.ZWART,
JRNL AUTH 2 V.NIENABER
JRNL TITL STRUCTURE DETERMINATION OF LPXA FROM THE
JRNL TITL 2 LIPOPOLYSACCHARIDE-SYNTHESIS PATHWAY OF ACINETOBACTER
JRNL TITL 3 BAUMANNII.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 68 1477 2012
JRNL REFN ESSN 1744-3091
JRNL PMID 23192027
JRNL DOI 10.1107/S174430911204571X
REMARK 2
REMARK 2 RESOLUTION. 1.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 70122
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3720
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) : 1.41
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.45
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5150
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE SET COUNT : 230
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1931
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 293
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.25000
REMARK 3 B12 (A**2) : 0.08000
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): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.050
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.031
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.758
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2060 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2772 ; 1.291 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 257 ; 6.344 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;40.268 ;25.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;11.773 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;15.730 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1511 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1269 ; 0.885 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2063 ; 1.556 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 791 ; 2.055 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 709 ; 3.365 ; 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 : 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 4E6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071242.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73881
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.410
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.30
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.59100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: 4E6T
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2UL OF 25MG/ML PROTEIN, 2UL OF 1.8M
REMARK 280 LISO4, 0.1M HEPES 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K, PH 7.5
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 59.53150
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 59.53150
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 59.53150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 37.87550
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -65.60229
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 75.75100
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 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 457 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 459 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 526 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 561 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 601 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 668 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 GLY A -2
REMARK 465 ALA A -1
REMARK 465 GLY A 0
REMARK 465 THR A 1
REMARK 465 SER A 2
REMARK 465 ASN A 3
REMARK 465 HIS A 4
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 LYS A 75 CE NZ
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 ARG A 202 CD NE CZ NH1 NH2
REMARK 470 ARG A 203 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 LYS A 208 CG CD CE NZ
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 HIS A 44 -163.87 -72.86
REMARK 500 ASP A 104 -99.45 -104.87
REMARK 500 PHE A 161 -3.37 74.30
REMARK 500 TYR A 183 -2.74 70.66
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 EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO 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 EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 311
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E6T RELATED DB: PDB
REMARK 900 RELATED ID: 4E75 RELATED DB: PDB
REMARK 900 RELATED ID: 4E79 RELATED DB: PDB
DBREF 4E6U A 2 262 UNP F0QHB3 F0QHB3_ACIBD 2 262
SEQADV 4E6U GLY A -2 UNP F0QHB3 EXPRESSION TAG
SEQADV 4E6U ALA A -1 UNP F0QHB3 EXPRESSION TAG
SEQADV 4E6U GLY A 0 UNP F0QHB3 EXPRESSION TAG
SEQADV 4E6U THR A 1 UNP F0QHB3 EXPRESSION TAG
SEQRES 1 A 265 GLY ALA GLY THR SER ASN HIS ASP LEU ILE HIS SER THR
SEQRES 2 A 265 ALA ILE ILE ASP PRO SER ALA VAL ILE ALA SER ASP VAL
SEQRES 3 A 265 GLN ILE GLY PRO TYR CYS ILE ILE GLY PRO GLN VAL THR
SEQRES 4 A 265 ILE GLY ALA GLY THR LYS LEU HIS SER HIS VAL VAL VAL
SEQRES 5 A 265 GLY GLY PHE THR ARG ILE GLY GLN ASN ASN GLU ILE PHE
SEQRES 6 A 265 GLN PHE ALA SER VAL GLY GLU VAL CYS GLN ASP LEU LYS
SEQRES 7 A 265 TYR LYS GLY GLU GLU THR TRP LEU GLU ILE GLY ASN ASN
SEQRES 8 A 265 ASN LEU ILE ARG GLU HIS CYS SER LEU HIS ARG GLY THR
SEQRES 9 A 265 VAL GLN ASP ASN ALA LEU THR LYS ILE GLY SER HIS ASN
SEQRES 10 A 265 LEU LEU MET VAL ASN THR HIS ILE ALA HIS ASP CYS ILE
SEQRES 11 A 265 VAL GLY ASP HIS ASN ILE PHE ALA ASN ASN VAL GLY VAL
SEQRES 12 A 265 ALA GLY HIS VAL HIS ILE GLY ASP HIS VAL ILE VAL GLY
SEQRES 13 A 265 GLY ASN SER GLY ILE HIS GLN PHE CYS LYS ILE ASP SER
SEQRES 14 A 265 TYR SER MET ILE GLY GLY ALA SER LEU ILE LEU LYS ASP
SEQRES 15 A 265 VAL PRO ALA TYR VAL MET ALA SER GLY ASN PRO ALA HIS
SEQRES 16 A 265 ALA PHE GLY ILE ASN ILE GLU GLY MET ARG ARG LYS GLY
SEQRES 17 A 265 TRP SER LYS ASN THR ILE GLN GLY LEU ARG GLU ALA TYR
SEQRES 18 A 265 LYS LEU ILE PHE LYS SER GLY LEU THR SER VAL GLN ALA
SEQRES 19 A 265 ILE ASP GLN ILE LYS SER GLU ILE LEU PRO SER VAL PRO
SEQRES 20 A 265 GLU ALA GLN LEU LEU ILE ASP SER LEU GLU GLN SER GLU
SEQRES 21 A 265 ARG GLY ILE VAL ARG
HET SO4 A 301 5
HET SO4 A 302 5
HET EDO A 303 4
HET EDO A 304 4
HET EDO A 305 4
HET EDO A 306 4
HET EDO A 307 4
HET EDO A 308 4
HET EDO A 309 4
HET EDO A 310 4
HET EDO A 311 4
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 EDO 9(C2 H6 O2)
FORMUL 13 HOH *293(H2 O)
HELIX 1 1 ASN A 197 LYS A 204 1 8
HELIX 2 2 SER A 207 LYS A 223 1 17
HELIX 3 3 THR A 227 ILE A 239 1 13
HELIX 4 4 VAL A 243 GLU A 245 5 3
HELIX 5 5 ALA A 246 SER A 256 1 11
SHEET 1 A 9 ILE A 12 ILE A 13 0
SHEET 2 A 9 ILE A 30 ILE A 31 1 O ILE A 31 N ILE A 12
SHEET 3 A 9 VAL A 48 VAL A 49 1 O VAL A 49 N ILE A 30
SHEET 4 A 9 SER A 66 GLU A 69 1 O VAL A 67 N VAL A 48
SHEET 5 A 9 SER A 96 HIS A 98 1 O LEU A 97 N SER A 66
SHEET 6 A 9 HIS A 121 ILE A 122 1 O ILE A 122 N SER A 96
SHEET 7 A 9 GLY A 139 VAL A 140 1 O VAL A 140 N HIS A 121
SHEET 8 A 9 GLY A 157 ILE A 158 1 O ILE A 158 N GLY A 139
SHEET 9 A 9 LEU A 175 ILE A 176 1 O ILE A 176 N GLY A 157
SHEET 1 B 8 VAL A 18 ILE A 19 0
SHEET 2 B 8 VAL A 35 ILE A 37 1 O VAL A 35 N VAL A 18
SHEET 3 B 8 THR A 53 ILE A 55 1 O ILE A 55 N THR A 36
SHEET 4 B 8 TRP A 82 ILE A 85 1 O ILE A 85 N ARG A 54
SHEET 5 B 8 LEU A 107 ILE A 110 1 O THR A 108 N GLU A 84
SHEET 6 B 8 ILE A 127 VAL A 128 1 O VAL A 128 N LYS A 109
SHEET 7 B 8 HIS A 145 ILE A 146 1 O ILE A 146 N ILE A 127
SHEET 8 B 8 LYS A 163 ILE A 164 1 O ILE A 164 N HIS A 145
SHEET 1 C10 GLN A 24 ILE A 25 0
SHEET 2 C10 LYS A 42 LEU A 43 1 O LEU A 43 N GLN A 24
SHEET 3 C10 GLU A 60 ILE A 61 1 O ILE A 61 N LYS A 42
SHEET 4 C10 LEU A 90 ILE A 91 1 O ILE A 91 N GLU A 60
SHEET 5 C10 LEU A 115 LEU A 116 1 O LEU A 116 N LEU A 90
SHEET 6 C10 ILE A 133 PHE A 134 1 O PHE A 134 N LEU A 115
SHEET 7 C10 ILE A 151 VAL A 152 1 O VAL A 152 N ILE A 133
SHEET 8 C10 MET A 169 ILE A 170 1 O ILE A 170 N ILE A 151
SHEET 9 C10 VAL A 184 SER A 187 1 O ALA A 186 N MET A 169
SHEET 10 C10 HIS A 192 ILE A 196 -1 O PHE A 194 N MET A 185
CISPEP 1 ASN A 189 PRO A 190 0 2.55
SITE 1 AC1 4 SER A 207 ASN A 209 THR A 210 HOH A 553
SITE 1 AC2 10 LYS A 42 HIS A 44 HOH A 413 HOH A 416
SITE 2 AC2 10 HOH A 418 HOH A 436 HOH A 437 HOH A 454
SITE 3 AC2 10 HOH A 531 HOH A 592
SITE 1 AC3 5 SER A 228 GLY A 259 ILE A 260 ARG A 262
SITE 2 AC3 5 HOH A 488
SITE 1 AC4 8 GLY A 139 ALA A 141 GLY A 157 ILE A 158
SITE 2 AC4 8 EDO A 309 HOH A 465 HOH A 602 HOH A 684
SITE 1 AC5 7 GLN A 72 ASP A 73 HIS A 124 EDO A 309
SITE 2 AC5 7 HOH A 406 HOH A 421 HOH A 619
SITE 1 AC6 3 GLN A 72 ASP A 73 LEU A 74
SITE 1 AC7 4 GLY A 40 ASN A 58 ASN A 59 HOH A 426
SITE 1 AC8 3 HIS A 159 GLN A 160 ARG A 258
SITE 1 AC9 5 MET A 117 ASN A 136 EDO A 304 EDO A 305
SITE 2 AC9 5 HOH A 585
SITE 1 BC1 7 ILE A 7 ALA A 20 VAL A 23 GLY A 225
SITE 2 BC1 7 THR A 227 GLN A 230 HOH A 603
SITE 1 BC2 7 ILE A 127 GLY A 129 ILE A 146 GLY A 147
SITE 2 BC2 7 HOH A 425 HOH A 534 HOH A 538
CRYST1 75.751 75.751 119.063 90.00 90.00 120.00 P 63 6
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 0.013201 0.007622 0.000000 0.00000
SCALE2 0.000000 0.015243 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008399 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
