HEADER ISOMERASE 19-NOV-07 3BEO
TITLE A STRUCTURAL BASIS FOR THE ALLOSTERIC REGULATION OF NON-HYDROLYZING
TITLE 2 UDP-GLCNAC 2-EPIMERASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.1.3.14;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_TAXID: 1392;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EPIMERASE, UDP-GLCNAC, ALLOSTERIC, REGULATION, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.VELLOSO,S.S.BHASKARAN,R.SCHUCH,V.A.FISCHETTI,C.E.STEBBINS
REVDAT 3 21-FEB-24 3BEO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 3BEO 1 VERSN
REVDAT 1 19-FEB-08 3BEO 0
JRNL AUTH L.M.VELLOSO,S.S.BHASKARAN,R.SCHUCH,V.A.FISCHETTI,
JRNL AUTH 2 C.E.STEBBINS
JRNL TITL A STRUCTURAL BASIS FOR THE ALLOSTERIC REGULATION OF
JRNL TITL 2 NON-HYDROLYSING UDP-GLCNAC 2-EPIMERASES.
JRNL REF EMBO REP. V. 9 199 2008
JRNL REFN ISSN 1469-221X
JRNL PMID 18188181
JRNL DOI 10.1038/SJ.EMBOR.7401154
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 106401
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5305
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7332
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 419
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5896
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 128
REMARK 3 SOLVENT ATOMS : 577
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.47000
REMARK 3 B22 (A**2) : 0.40000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.146
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.308
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.913
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6127 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4119 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8322 ; 1.757 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10112 ; 1.090 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 746 ; 6.217 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 270 ;37.848 ;24.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1092 ;12.505 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;15.883 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 971 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6641 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1123 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1330 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4462 ; 0.210 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2929 ; 0.167 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3033 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 389 ; 0.229 ; 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 ; 0.270 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 35 ; 0.352 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.313 ; 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): 4874 ; 1.671 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1503 ; 0.801 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6087 ; 2.011 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2651 ; 3.352 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2235 ; 4.360 ; 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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A -1 A 185 1
REMARK 3 1 B -1 B 185 1
REMARK 3 2 A 186 A 196 6
REMARK 3 2 B 186 B 196 6
REMARK 3 3 A 197 A 371 1
REMARK 3 3 B 197 B 371 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4814 ; 0.030 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 A (A): 137 ; 0.190 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 4814 ; 0.180 ; 0.500
REMARK 3 LOOSE THERMAL 1 A (A**2): 137 ; 1.920 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 372 A 372 4
REMARK 3 1 B 372 B 372 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 56 ; 0.050 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 56 ; 0.750 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1081 A 1081 4
REMARK 3 1 B 1081 B 1081 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 34 ; 0.300 ; 0.500
REMARK 3 MEDIUM THERMAL 3 A (A**2): 34 ; 0.630 ; 2.000
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 : 1.20
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 3BEO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045425.
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 : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107005
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.001
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08700
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) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.34600
REMARK 200 R SYM FOR SHELL (I) : 0.34600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000-6000, 100MM TRIS-HCL, 0.2M
REMARK 280 LI2SO4, PH 8.5, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 94.08250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6590 ANGSTROM**2
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 187 CA CB CG CD CE NZ
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 1111 O HOH A 1246 1.35
REMARK 500 O HOH A 1314 O HOH A 1355 1.44
REMARK 500 OG1 THR B 184 O HOH B 1417 1.54
REMARK 500 O HOH B 1255 O HOH B 1473 1.67
REMARK 500 O HOH B 1213 O HOH B 1258 1.99
REMARK 500 O HOH A 1281 O HOH A 1344 2.00
REMARK 500 NZ LYS A 183 O HOH A 1276 2.02
REMARK 500 O HOH A 1181 O HOH A 1317 2.15
REMARK 500 O HOH A 1337 O HOH B 1303 2.17
REMARK 500 O HOH B 1293 O HOH B 1332 2.18
REMARK 500 O HOH B 1372 O HOH B 1472 2.18
REMARK 500 O HOH B 1342 O HOH B 1397 2.19
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 LYS A 187 CA - C - O ANGL. DEV. = -19.0 DEGREES
REMARK 500 ARG A 360 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU B 80 CB - CG - CD2 ANGL. DEV. = -10.8 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 ARG A 45 -77.46 -107.89
REMARK 500 ASP A 100 25.28 -152.22
REMARK 500 GLU A 122 61.89 72.88
REMARK 500 SER A 132 96.06 -160.11
REMARK 500 HIS A 209 2.51 -160.09
REMARK 500 ARG A 309 59.56 -116.54
REMARK 500 ARG B 45 -75.51 -103.42
REMARK 500 ASP B 100 22.24 -150.52
REMARK 500 GLU B 122 59.94 77.65
REMARK 500 HIS B 209 5.13 -156.87
REMARK 500 LEU B 303 59.72 -91.74
REMARK 500 ARG B 309 60.30 -114.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LYS A 187 23.95
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 UD1 A 372
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A 1081
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UD1 B 372
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 1081
DBREF 3BEO A 1 371 UNP Q81K32 Q81K32_BACAN 1 371
DBREF 3BEO B 1 371 UNP Q81K32 Q81K32_BACAN 1 371
SEQADV 3BEO GLY A -3 UNP Q81K32 EXPRESSION TAG
SEQADV 3BEO PRO A -2 UNP Q81K32 EXPRESSION TAG
SEQADV 3BEO VAL A -1 UNP Q81K32 EXPRESSION TAG
SEQADV 3BEO ASP A 0 UNP Q81K32 EXPRESSION TAG
SEQADV 3BEO GLY B -3 UNP Q81K32 EXPRESSION TAG
SEQADV 3BEO PRO B -2 UNP Q81K32 EXPRESSION TAG
SEQADV 3BEO VAL B -1 UNP Q81K32 EXPRESSION TAG
SEQADV 3BEO ASP B 0 UNP Q81K32 EXPRESSION TAG
SEQRES 1 A 375 GLY PRO VAL ASP MET THR GLU ARG LEU LYS VAL MET THR
SEQRES 2 A 375 ILE PHE GLY THR ARG PRO GLU ALA ILE LYS MET ALA PRO
SEQRES 3 A 375 LEU VAL LEU GLU LEU GLN LYS HIS PRO GLU LYS ILE GLU
SEQRES 4 A 375 SER ILE VAL THR VAL THR ALA GLN HIS ARG GLN MET LEU
SEQRES 5 A 375 ASP GLN VAL LEU SER ILE PHE GLY ILE THR PRO ASP PHE
SEQRES 6 A 375 ASP LEU ASN ILE MET LYS ASP ARG GLN THR LEU ILE ASP
SEQRES 7 A 375 ILE THR THR ARG GLY LEU GLU GLY LEU ASP LYS VAL MET
SEQRES 8 A 375 LYS GLU ALA LYS PRO ASP ILE VAL LEU VAL HIS GLY ASP
SEQRES 9 A 375 THR THR THR THR PHE ILE ALA SER LEU ALA ALA PHE TYR
SEQRES 10 A 375 ASN GLN ILE PRO VAL GLY HIS VAL GLU ALA GLY LEU ARG
SEQRES 11 A 375 THR TRP ASP LYS TYR SER PRO TYR PRO GLU GLU MET ASN
SEQRES 12 A 375 ARG GLN LEU THR GLY VAL MET ALA ASP LEU HIS PHE SER
SEQRES 13 A 375 PRO THR ALA LYS SER ALA THR ASN LEU GLN LYS GLU ASN
SEQRES 14 A 375 LYS ASP GLU SER ARG ILE PHE ILE THR GLY ASN THR ALA
SEQRES 15 A 375 ILE ASP ALA LEU LYS THR THR VAL LYS GLU THR TYR SER
SEQRES 16 A 375 HIS PRO VAL LEU GLU LYS LEU GLY ASN ASN ARG LEU VAL
SEQRES 17 A 375 LEU MET THR ALA HIS ARG ARG GLU ASN LEU GLY GLU PRO
SEQRES 18 A 375 MET ARG ASN MET PHE ARG ALA ILE LYS ARG LEU VAL ASP
SEQRES 19 A 375 LYS HIS GLU ASP VAL GLN VAL VAL TYR PRO VAL HIS MET
SEQRES 20 A 375 ASN PRO VAL VAL ARG GLU THR ALA ASN ASP ILE LEU GLY
SEQRES 21 A 375 ASP TYR GLY ARG ILE HIS LEU ILE GLU PRO LEU ASP VAL
SEQRES 22 A 375 ILE ASP PHE HIS ASN VAL ALA ALA ARG SER TYR LEU MET
SEQRES 23 A 375 LEU THR ASP SER GLY GLY VAL GLN GLU GLU ALA PRO SER
SEQRES 24 A 375 LEU GLY VAL PRO VAL LEU VAL LEU ARG ASP THR THR GLU
SEQRES 25 A 375 ARG PRO GLU GLY ILE GLU ALA GLY THR LEU LYS LEU ALA
SEQRES 26 A 375 GLY THR ASP GLU GLU THR ILE PHE SER LEU ALA ASP GLU
SEQRES 27 A 375 LEU LEU SER ASP LYS GLU ALA HIS ASP LYS MET SER LYS
SEQRES 28 A 375 ALA SER ASN PRO TYR GLY ASP GLY ARG ALA SER GLU ARG
SEQRES 29 A 375 ILE VAL GLU ALA ILE LEU LYS HIS PHE ASN LYS
SEQRES 1 B 375 GLY PRO VAL ASP MET THR GLU ARG LEU LYS VAL MET THR
SEQRES 2 B 375 ILE PHE GLY THR ARG PRO GLU ALA ILE LYS MET ALA PRO
SEQRES 3 B 375 LEU VAL LEU GLU LEU GLN LYS HIS PRO GLU LYS ILE GLU
SEQRES 4 B 375 SER ILE VAL THR VAL THR ALA GLN HIS ARG GLN MET LEU
SEQRES 5 B 375 ASP GLN VAL LEU SER ILE PHE GLY ILE THR PRO ASP PHE
SEQRES 6 B 375 ASP LEU ASN ILE MET LYS ASP ARG GLN THR LEU ILE ASP
SEQRES 7 B 375 ILE THR THR ARG GLY LEU GLU GLY LEU ASP LYS VAL MET
SEQRES 8 B 375 LYS GLU ALA LYS PRO ASP ILE VAL LEU VAL HIS GLY ASP
SEQRES 9 B 375 THR THR THR THR PHE ILE ALA SER LEU ALA ALA PHE TYR
SEQRES 10 B 375 ASN GLN ILE PRO VAL GLY HIS VAL GLU ALA GLY LEU ARG
SEQRES 11 B 375 THR TRP ASP LYS TYR SER PRO TYR PRO GLU GLU MET ASN
SEQRES 12 B 375 ARG GLN LEU THR GLY VAL MET ALA ASP LEU HIS PHE SER
SEQRES 13 B 375 PRO THR ALA LYS SER ALA THR ASN LEU GLN LYS GLU ASN
SEQRES 14 B 375 LYS ASP GLU SER ARG ILE PHE ILE THR GLY ASN THR ALA
SEQRES 15 B 375 ILE ASP ALA LEU LYS THR THR VAL LYS GLU THR TYR SER
SEQRES 16 B 375 HIS PRO VAL LEU GLU LYS LEU GLY ASN ASN ARG LEU VAL
SEQRES 17 B 375 LEU MET THR ALA HIS ARG ARG GLU ASN LEU GLY GLU PRO
SEQRES 18 B 375 MET ARG ASN MET PHE ARG ALA ILE LYS ARG LEU VAL ASP
SEQRES 19 B 375 LYS HIS GLU ASP VAL GLN VAL VAL TYR PRO VAL HIS MET
SEQRES 20 B 375 ASN PRO VAL VAL ARG GLU THR ALA ASN ASP ILE LEU GLY
SEQRES 21 B 375 ASP TYR GLY ARG ILE HIS LEU ILE GLU PRO LEU ASP VAL
SEQRES 22 B 375 ILE ASP PHE HIS ASN VAL ALA ALA ARG SER TYR LEU MET
SEQRES 23 B 375 LEU THR ASP SER GLY GLY VAL GLN GLU GLU ALA PRO SER
SEQRES 24 B 375 LEU GLY VAL PRO VAL LEU VAL LEU ARG ASP THR THR GLU
SEQRES 25 B 375 ARG PRO GLU GLY ILE GLU ALA GLY THR LEU LYS LEU ALA
SEQRES 26 B 375 GLY THR ASP GLU GLU THR ILE PHE SER LEU ALA ASP GLU
SEQRES 27 B 375 LEU LEU SER ASP LYS GLU ALA HIS ASP LYS MET SER LYS
SEQRES 28 B 375 ALA SER ASN PRO TYR GLY ASP GLY ARG ALA SER GLU ARG
SEQRES 29 B 375 ILE VAL GLU ALA ILE LEU LYS HIS PHE ASN LYS
HET UD1 A 372 39
HET UDP A1081 25
HET UD1 B 372 39
HET UDP B1081 25
HETNAM UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
HETNAM UDP URIDINE-5'-DIPHOSPHATE
FORMUL 3 UD1 2(C17 H27 N3 O17 P2)
FORMUL 4 UDP 2(C9 H14 N2 O12 P2)
FORMUL 7 HOH *577(H2 O)
HELIX 1 1 THR A 13 GLN A 28 1 16
HELIX 2 2 ARG A 45 GLY A 56 1 12
HELIX 3 3 THR A 71 LYS A 91 1 21
HELIX 4 4 THR A 101 ASN A 114 1 14
HELIX 5 5 PRO A 135 ALA A 147 1 13
HELIX 6 6 THR A 154 GLU A 164 1 11
HELIX 7 7 ASP A 167 SER A 169 5 3
HELIX 8 8 ASN A 176 VAL A 186 1 11
HELIX 9 9 HIS A 192 LYS A 197 1 6
HELIX 10 10 ARG A 210 LEU A 214 5 5
HELIX 11 11 GLY A 215 HIS A 232 1 18
HELIX 12 12 ASN A 244 GLY A 256 1 13
HELIX 13 13 ASP A 268 ARG A 278 1 11
HELIX 14 14 SER A 286 ALA A 293 1 8
HELIX 15 15 PRO A 294 GLY A 297 5 4
HELIX 16 16 ARG A 309 ALA A 315 1 7
HELIX 17 17 ASP A 324 ASP A 338 1 15
HELIX 18 18 ASP A 338 SER A 346 1 9
HELIX 19 19 ARG A 356 PHE A 369 1 14
HELIX 20 20 THR B 13 GLN B 28 1 16
HELIX 21 21 ARG B 45 GLY B 56 1 12
HELIX 22 22 THR B 71 LYS B 91 1 21
HELIX 23 23 THR B 101 TYR B 113 1 13
HELIX 24 24 PRO B 135 ALA B 147 1 13
HELIX 25 25 THR B 154 GLU B 164 1 11
HELIX 26 26 ASP B 167 SER B 169 5 3
HELIX 27 27 ASN B 176 VAL B 186 1 11
HELIX 28 28 HIS B 192 LYS B 197 1 6
HELIX 29 29 ARG B 210 LEU B 214 5 5
HELIX 30 30 GLY B 215 HIS B 232 1 18
HELIX 31 31 ASN B 244 GLY B 256 1 13
HELIX 32 32 ASP B 268 ARG B 278 1 11
HELIX 33 33 SER B 286 ALA B 293 1 8
HELIX 34 34 PRO B 294 GLY B 297 5 4
HELIX 35 35 ARG B 309 ALA B 315 1 7
HELIX 36 36 ASP B 324 ASP B 338 1 15
HELIX 37 37 ASP B 338 SER B 346 1 9
HELIX 38 38 ARG B 356 PHE B 369 1 14
SHEET 1 A 7 PHE A 61 ASP A 62 0
SHEET 2 A 7 ILE A 34 VAL A 40 1 N VAL A 40 O PHE A 61
SHEET 3 A 7 LEU A 5 PHE A 11 1 N THR A 9 O THR A 39
SHEET 4 A 7 ILE A 94 HIS A 98 1 O LEU A 96 N MET A 8
SHEET 5 A 7 VAL A 118 VAL A 121 1 O VAL A 121 N VAL A 97
SHEET 6 A 7 LEU A 149 SER A 152 1 O LEU A 149 N HIS A 120
SHEET 7 A 7 ILE A 171 ILE A 173 1 O PHE A 172 N HIS A 150
SHEET 1 B 6 ILE A 261 ILE A 264 0
SHEET 2 B 6 VAL A 235 PRO A 240 1 N TYR A 239 O HIS A 262
SHEET 3 B 6 ARG A 202 THR A 207 1 N VAL A 204 O GLN A 236
SHEET 4 B 6 LEU A 281 THR A 284 1 O LEU A 281 N LEU A 205
SHEET 5 B 6 VAL A 300 VAL A 302 1 O LEU A 301 N MET A 282
SHEET 6 B 6 LEU A 318 LEU A 320 1 O LYS A 319 N VAL A 302
SHEET 1 C 7 PHE B 61 ASP B 62 0
SHEET 2 C 7 ILE B 34 VAL B 40 1 N VAL B 40 O PHE B 61
SHEET 3 C 7 LEU B 5 PHE B 11 1 N VAL B 7 O ILE B 37
SHEET 4 C 7 ILE B 94 HIS B 98 1 O LEU B 96 N MET B 8
SHEET 5 C 7 VAL B 118 VAL B 121 1 O VAL B 121 N VAL B 97
SHEET 6 C 7 LEU B 149 SER B 152 1 O PHE B 151 N HIS B 120
SHEET 7 C 7 ILE B 171 ILE B 173 1 O PHE B 172 N HIS B 150
SHEET 1 D 6 ILE B 261 ILE B 264 0
SHEET 2 D 6 VAL B 235 PRO B 240 1 N VAL B 237 O HIS B 262
SHEET 3 D 6 ARG B 202 THR B 207 1 N MET B 206 O VAL B 238
SHEET 4 D 6 LEU B 281 THR B 284 1 O LEU B 281 N LEU B 205
SHEET 5 D 6 VAL B 300 VAL B 302 1 O LEU B 301 N MET B 282
SHEET 6 D 6 LEU B 318 LEU B 320 1 O LYS B 319 N VAL B 302
CISPEP 1 SER A 132 PRO A 133 0 4.27
CISPEP 2 TYR A 134 PRO A 135 0 -1.30
CISPEP 3 SER B 132 PRO B 133 0 2.81
CISPEP 4 TYR B 134 PRO B 135 0 3.03
SITE 1 AC1 29 PRO A 15 GLN A 43 HIS A 44 ARG A 45
SITE 2 AC1 29 GLN A 46 MET A 47 MET A 66 LYS A 67
SITE 3 AC1 29 ASP A 68 ARG A 69 GLN A 70 THR A 101
SITE 4 AC1 29 THR A 102 PRO A 135 GLU A 136 HIS A 209
SITE 5 AC1 29 ARG A 210 ARG A 211 HIS A 242 MET A 243
SITE 6 AC1 29 ASN A 244 PRO A 245 UDP A1081 HOH A1092
SITE 7 AC1 29 HOH A1101 HOH A1181 HOH A1322 HOH A1325
SITE 8 AC1 29 HOH A1341
SITE 1 AC2 20 ARG A 14 PRO A 15 ILE A 18 HIS A 209
SITE 2 AC2 20 ARG A 210 PRO A 240 LEU A 267 VAL A 269
SITE 3 AC2 20 PHE A 272 HIS A 273 SER A 286 GLY A 287
SITE 4 AC2 20 GLY A 288 GLU A 292 UD1 A 372 HOH A1084
SITE 5 AC2 20 HOH A1102 HOH A1127 HOH A1171 HOH A1181
SITE 1 AC3 33 PRO B 15 GLN B 43 HIS B 44 ARG B 45
SITE 2 AC3 33 GLN B 46 MET B 47 MET B 66 LYS B 67
SITE 3 AC3 33 ASP B 68 ARG B 69 GLN B 70 LEU B 72
SITE 4 AC3 33 ILE B 75 THR B 101 THR B 102 PRO B 135
SITE 5 AC3 33 GLU B 136 HIS B 209 ARG B 210 ARG B 211
SITE 6 AC3 33 HIS B 242 MET B 243 ASN B 244 PRO B 245
SITE 7 AC3 33 UDP B1081 HOH B1198 HOH B1209 HOH B1228
SITE 8 AC3 33 HOH B1292 HOH B1295 HOH B1300 HOH B1391
SITE 9 AC3 33 HOH B1413
SITE 1 AC4 20 ARG B 14 PRO B 15 ILE B 18 HIS B 209
SITE 2 AC4 20 ARG B 210 PRO B 240 LEU B 267 VAL B 269
SITE 3 AC4 20 PHE B 272 HIS B 273 SER B 286 GLY B 287
SITE 4 AC4 20 GLY B 288 GLU B 292 UD1 B 372 HOH B1199
SITE 5 AC4 20 HOH B1205 HOH B1236 HOH B1262 HOH B1358
CRYST1 46.404 188.165 61.679 90.00 112.22 90.00 P 1 21 1 4
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 0.021550 0.000000 0.008802 0.00000
SCALE2 0.000000 0.005314 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017513 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
