HEADER ISOMERASE 20-JAN-05 2BI7
TITLE UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE OXIDISED FAD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-GALACTOPYRANOSE MUTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.4.99.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PHISTEV
KEYWDS FAD, FLAVOPROTEIN, ISOMERASE, LIPOPOLYSACCHARIDE BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BEIS,V.SRIKANNATHASAN,J.NAISMITH
REVDAT 6 13-DEC-23 2BI7 1 REMARK
REVDAT 5 28-JUN-17 2BI7 1 REMARK
REVDAT 4 25-MAR-15 2BI7 1 TITLE JRNL REMARK
REVDAT 3 13-JUL-11 2BI7 1 VERSN
REVDAT 2 24-FEB-09 2BI7 1 VERSN
REVDAT 1 05-MAY-05 2BI7 0
SPRSDE 05-MAY-05 2BI7 1USJ
JRNL AUTH K.BEIS,V.SRIKANNATHASAN,H.LIU,S.W.B.FULLERTON,V.A.BAMFORD,
JRNL AUTH 2 D.A.R.SANDERS,C.WHITFIELD,M.R.MCNEIL,J.H.NAISMITH
JRNL TITL CRYSTAL STRUCTURES OF MYCOBACTERIA TUBERCULOSIS AND
JRNL TITL 2 KLEBSIELLA PNEUMONIAE UDP-GALACTOPYRANOSE MUTASE IN THE
JRNL TITL 3 OXIDISED STATE AND KLEBSIELLA PNEUMONIAE UDP-GALACTOPYRANOSE
JRNL TITL 4 MUTASE IN THE (ACTIVE) REDUCED STATE.
JRNL REF J.MOL.BIOL. V. 348 971 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15843027
JRNL DOI 10.1016/J.JMB.2005.02.057
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.A.SANDERS,A.G.STAINES,S.A.MCMAHON,M.R.MCNEIL,C.WHITFIELD,
REMARK 1 AUTH 2 J.H.NAISMITH
REMARK 1 TITL UDP-GALACTOPYRANOSE MUTASE HAS A NOVEL STRUCTURE AND
REMARK 1 TITL 2 MECHANISM
REMARK 1 REF NAT.STRUCT.BIOL. V. 8 858 2001
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 11573090
REMARK 1 DOI 10.1038/NSB1001-858
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0007
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 24352
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1293
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 733
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3118
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.27000
REMARK 3 B12 (A**2) : 0.09000
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): 0.223
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.194
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3260 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4426 ; 1.203 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 382 ; 5.567 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 167 ;36.531 ;23.952
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 532 ;15.493 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;18.947 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 459 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2527 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1429 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2210 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 216 ; 0.158 ; 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): 34 ; 0.145 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.261 ; 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): 1963 ; 0.613 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3082 ; 1.023 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1554 ; 1.623 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1344 ; 2.390 ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 389
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4000 25.3420 11.4210
REMARK 3 T TENSOR
REMARK 3 T11: -0.0775 T22: 0.0039
REMARK 3 T33: -0.0651 T12: 0.0515
REMARK 3 T13: 0.0419 T23: -0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 1.4028 L22: 1.3837
REMARK 3 L33: 1.5392 L12: -0.8536
REMARK 3 L13: 0.9652 L23: -0.8216
REMARK 3 S TENSOR
REMARK 3 S11: 0.1147 S12: 0.2800 S13: 0.1048
REMARK 3 S21: -0.1707 S22: -0.1156 S23: -0.1368
REMARK 3 S31: 0.1321 S32: 0.2668 S33: 0.0009
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 2BI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1290022539.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 6.50
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 2160
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 74.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 16.60
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6
REMARK 200 DATA REDUNDANCY IN SHELL : 9.10
REMARK 200 R MERGE FOR SHELL (I) : 0.17000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
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: PDB ENTRY 1I8T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH6.5, 50MM CACL2, 30%
REMARK 280 PEG550, PH 6.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 66.52867
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 33.26433
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.26433
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 66.52867
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 FUNCTION: INVOLVED IN THE CONVERSION OF UDP-GALP INTO UDP-GALF
REMARK 400 THROUGH A 2-KETO INTERMEDIATE
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 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 2 CB CG CD CE NZ
REMARK 470 GLU A 372 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 OD1 ASP A 262 O HOH A 2094 0.58
REMARK 500 CG ASP A 262 O HOH A 2094 1.83
REMARK 500 SG CYS A 272 O HOH A 2101 2.16
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 ASN A 51 18.35 58.83
REMARK 500 SER A 127 42.02 -100.26
REMARK 500 PHE A 179 46.54 -90.59
REMARK 500 GLU A 307 -166.46 -109.77
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 FAD A 1385
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WAM RELATED DB: PDB
REMARK 900 STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE
REMARK 900 WITH FADH-
REMARK 900 RELATED ID: 2BI8 RELATED DB: PDB
REMARK 900 UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE WITH REDUCED
REMARK 900 FAD
DBREF 2BI7 A 1 384 UNP Q48485 GLF1_KLEPN 1 384
SEQRES 1 A 384 MET LYS SER LYS LYS ILE LEU ILE VAL GLY ALA GLY PHE
SEQRES 2 A 384 SER GLY ALA VAL ILE GLY ARG GLN LEU ALA GLU LYS GLY
SEQRES 3 A 384 HIS GLN VAL HIS ILE ILE ASP GLN ARG ASP HIS ILE GLY
SEQRES 4 A 384 GLY ASN SER TYR ASP ALA ARG ASP SER GLU THR ASN VAL
SEQRES 5 A 384 MET VAL HIS VAL TYR GLY PRO HIS ILE PHE HIS THR ASP
SEQRES 6 A 384 ASN GLU THR VAL TRP ASN TYR VAL ASN LYS HIS ALA GLU
SEQRES 7 A 384 MET MET PRO TYR VAL ASN ARG VAL LYS ALA THR VAL ASN
SEQRES 8 A 384 GLY GLN VAL PHE SER LEU PRO ILE ASN LEU HIS THR ILE
SEQRES 9 A 384 ASN GLN PHE PHE SER LYS THR CYS SER PRO ASP GLU ALA
SEQRES 10 A 384 ARG ALA LEU ILE ALA GLU LYS GLY ASP SER THR ILE ALA
SEQRES 11 A 384 ASP PRO GLN THR PHE GLU GLU GLU ALA LEU ARG PHE ILE
SEQRES 12 A 384 GLY LYS GLU LEU TYR GLU ALA PHE PHE LYS GLY TYR THR
SEQRES 13 A 384 ILE LYS GLN TRP GLY MET GLN PRO SER GLU LEU PRO ALA
SEQRES 14 A 384 SER ILE LEU LYS ARG LEU PRO VAL ARG PHE ASN TYR ASP
SEQRES 15 A 384 ASP ASN TYR PHE ASN HIS LYS PHE GLN GLY MET PRO LYS
SEQRES 16 A 384 CYS GLY TYR THR GLN MET ILE LYS SER ILE LEU ASN HIS
SEQRES 17 A 384 GLU ASN ILE LYS VAL ASP LEU GLN ARG GLU PHE ILE VAL
SEQRES 18 A 384 GLU GLU ARG THR HIS TYR ASP HIS VAL PHE TYR SER GLY
SEQRES 19 A 384 PRO LEU ASP ALA PHE TYR GLY TYR GLN TYR GLY ARG LEU
SEQRES 20 A 384 GLY TYR ARG THR LEU ASP PHE LYS LYS PHE THR TYR GLN
SEQRES 21 A 384 GLY ASP TYR GLN GLY CYS ALA VAL MET ASN TYR CYS SER
SEQRES 22 A 384 VAL ASP VAL PRO TYR THR ARG ILE THR GLU HIS LYS TYR
SEQRES 23 A 384 PHE SER PRO TRP GLU GLN HIS ASP GLY SER VAL CYS TYR
SEQRES 24 A 384 LYS GLU TYR SER ARG ALA CYS GLU GLU ASN ASP ILE PRO
SEQRES 25 A 384 TYR TYR PRO ILE ARG GLN MET GLY GLU MET ALA LEU LEU
SEQRES 26 A 384 GLU LYS TYR LEU SER LEU ALA GLU ASN GLU THR ASN ILE
SEQRES 27 A 384 THR PHE VAL GLY ARG LEU GLY THR TYR ARG TYR LEU ASP
SEQRES 28 A 384 MET ASP VAL THR ILE ALA GLU ALA LEU LYS THR ALA GLU
SEQRES 29 A 384 VAL TYR LEU ASN SER LEU THR GLU ASN GLN PRO MET PRO
SEQRES 30 A 384 VAL PHE THR VAL SER VAL ARG
HET FAD A1385 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 HOH *140(H2 O)
HELIX 1 1 GLY A 12 GLU A 24 1 13
HELIX 2 2 GLY A 39 SER A 42 5 4
HELIX 3 3 ASN A 66 LYS A 75 1 10
HELIX 4 4 ASN A 100 PHE A 108 1 9
HELIX 5 5 SER A 113 GLY A 125 1 13
HELIX 6 6 THR A 134 GLY A 144 1 11
HELIX 7 7 GLY A 144 PHE A 152 1 9
HELIX 8 8 PHE A 152 GLY A 161 1 10
HELIX 9 9 GLN A 163 LEU A 167 5 5
HELIX 10 10 ALA A 169 LEU A 172 5 4
HELIX 11 11 CYS A 196 ASN A 207 1 12
HELIX 12 12 ILE A 220 TYR A 227 5 8
HELIX 13 13 PRO A 235 TYR A 240 1 6
HELIX 14 14 LYS A 285 SER A 288 5 4
HELIX 15 15 GLN A 318 GLU A 333 1 16
HELIX 16 16 VAL A 341 THR A 346 1 6
HELIX 17 17 ASP A 351 GLU A 372 1 22
SHEET 1 AA 5 ILE A 211 LEU A 215 0
SHEET 2 AA 5 GLN A 28 ASP A 33 1 O VAL A 29 N LYS A 212
SHEET 3 AA 5 LYS A 5 VAL A 9 1 O ILE A 6 N HIS A 30
SHEET 4 AA 5 HIS A 229 TYR A 232 1 O HIS A 229 N LEU A 7
SHEET 5 AA 5 ILE A 338 PHE A 340 1 O THR A 339 N TYR A 232
SHEET 1 AB 2 ASP A 44 ARG A 46 0
SHEET 2 AB 2 MET A 53 HIS A 55 -1 O VAL A 54 N ALA A 45
SHEET 1 AC 3 PHE A 62 THR A 64 0
SHEET 2 AC 3 PHE A 190 PRO A 194 -1 O PHE A 190 N THR A 64
SHEET 3 AC 3 MET A 79 PRO A 81 -1 O MET A 80 N MET A 193
SHEET 1 AD 7 GLN A 93 LEU A 97 0
SHEET 2 AD 7 VAL A 86 VAL A 90 -1 O VAL A 86 N LEU A 97
SHEET 3 AD 7 VAL A 268 TYR A 271 1 O VAL A 268 N LYS A 87
SHEET 4 AD 7 ARG A 280 GLU A 283 -1 O ILE A 281 N MET A 269
SHEET 5 AD 7 GLY A 295 ALA A 305 -1 O TYR A 299 N THR A 282
SHEET 6 AD 7 TYR A 249 GLN A 260 -1 O THR A 251 N ARG A 304
SHEET 7 AD 7 TYR A 314 PRO A 315 -1 O TYR A 314 N ARG A 250
CISPEP 1 LEU A 97 PRO A 98 0 0.44
SITE 1 AC1 34 VAL A 9 GLY A 10 GLY A 12 PHE A 13
SITE 2 AC1 34 SER A 14 ASP A 33 GLN A 34 ARG A 35
SITE 3 AC1 34 GLY A 40 ASN A 41 TYR A 57 PRO A 59
SITE 4 AC1 34 HIS A 60 ILE A 61 ARG A 217 GLU A 218
SITE 5 AC1 34 PHE A 219 GLY A 234 LEU A 252 TYR A 313
SITE 6 AC1 34 GLY A 342 ARG A 343 TYR A 349 LEU A 350
SITE 7 AC1 34 ASP A 351 MET A 352 THR A 355 HOH A2011
SITE 8 AC1 34 HOH A2013 HOH A2087 HOH A2129 HOH A2138
SITE 9 AC1 34 HOH A2139 HOH A2140
CRYST1 85.675 85.675 99.793 90.00 90.00 120.00 P 32 2 1 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 0.011672 0.006739 0.000000 0.00000
SCALE2 0.000000 0.013478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010021 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
