HEADER TRANSFERASE 19-AUG-13 4C2S
TITLE CRYSTAL STRUCTURE OF THE FUCOSYLGALACTOSIDE ALPHA N-
TITLE 2 ACETYLGALACTOSAMINYLTRANSFERASE (GTA P156L MUTANT) IN COMPLEX WITH
TITLE 3 UDP AND DEOXY-H-ANTIGEN ACCEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EXTRACELLULAR CATALYTIC DOMAIN, RESIDUES 64-354;
COMPND 5 SYNONYM: FUCOSYLGLYCOPROTEIN 3-ALPHA-GALACTOSYLTRANSFERASE,
COMPND 6 FUCOSYLGLYCOPROTEIN ALPHA-N-ACETYLGALACTOSAMINYLTRANSFERASE,
COMPND 7 GLYCOPROTEIN-FUCOSYLGALACTOSIDE ALPHA-N-
COMPND 8 ACETYLGALACTOSAMINYLTRANSFERASE, GLYCOPROTEIN-FUCOSYLGALACTOSIDE
COMPND 9 ALPHA-GALACTOSYLTRANSFERASE, HISTO-BLOOD GROUP A TRANSFERASE, A
COMPND 10 TRANSFERASE, HISTO-BLOOD GROUP B TRANSFERASE, B TRANSFERASE, NAGAT,
COMPND 11 FUCOSYLGLYCOPROTEIN ALPHA-N-ACETYLGALACTOSAMINYLTRANSFERASE SOLUBLE
COMPND 12 FORM;
COMPND 13 EC: 2.4.1.40, 2.4.1.37;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS GTA, ABO, BLOOD GROUP ANTIGEN, GLYCOSYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.WEADGE,M.PALCIC,A.HENRIKSEN
REVDAT 6 20-DEC-23 4C2S 1 HETSYN
REVDAT 5 29-JUL-20 4C2S 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 17-JAN-18 4C2S 1 REMARK
REVDAT 3 23-OCT-13 4C2S 1 REVDAT
REVDAT 2 16-OCT-13 4C2S 1 AUTHOR REVDAT JRNL
REVDAT 1 11-SEP-13 4C2S 0
JRNL AUTH J.T.WEADGE,M.PALCIC,A.HENRIKSEN
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE HUMAN
JRNL TITL 2 BLOOD GROUP A AND B GALACTOSYLTRANSFERASES POSESSING THE
JRNL TITL 3 PRO156LEU MUTATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 20949
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1120
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) : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1438
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.1520
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.2080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4726
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : -0.38000
REMARK 3 B33 (A**2) : 0.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.31000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.164
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.127
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4964 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4680 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6744 ; 1.376 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10706 ; 0.876 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 579 ; 6.115 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 236 ;33.209 ;22.797
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 805 ;14.835 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;15.983 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 737 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5493 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1223 ; 0.001 ; 0.020
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): 2321 ; 0.799 ; 1.252
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2320 ; 0.799 ; 1.252
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2899 ; 1.202 ; 1.877
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2642 ; 0.847 ; 1.263
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.938
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : H,-K,-L
REMARK 3 TWIN FRACTION : 0.062
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. U VALUES WERE REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4C2S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1290058075.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0379
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH 165
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21693
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.460
REMARK 200 RESOLUTION RANGE LOW (A) : 54.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2Y7A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MM MOPS PH 7.0, 1 MM MNCL2, 1 MM
REMARK 280 DTT, 0.1 M AMSO4, 10% (W/V) PEG 3350
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 73.75500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.30500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.75500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.30500
REMARK 290 SMTRY3 4 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: 8380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 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 PRO A 354
REMARK 465 MET B 63
REMARK 465 PRO B 354
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 MET A 63 CB CG SD CE
REMARK 470 VAL A 64 CB CG1 CG2
REMARK 470 ARG A 198 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 200 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 201 CB CG CD1 CD2
REMARK 470 SER A 202 OG
REMARK 470 ARG B 176 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG B 198 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 199 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 200 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 201 CB CG CD1 CD2
REMARK 470 SER B 202 OG
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 NH1 ARG A 282 O HOH A 2039 2.10
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 122 72.05 -118.23
REMARK 500 LYS A 124 -118.88 53.64
REMARK 500 PHE A 200 -108.22 -11.26
REMARK 500 PHE A 236 -15.96 -147.35
REMARK 500 THR A 245 47.71 -88.75
REMARK 500 PHE A 269 101.50 -161.99
REMARK 500 HIS A 301 -129.17 58.32
REMARK 500 PRO A 321 -19.49 -46.93
REMARK 500 LEU A 324 104.62 -160.26
REMARK 500 CYS B 80 -70.71 -52.97
REMARK 500 LYS B 124 -125.97 54.38
REMARK 500 ARG B 187 0.91 -69.36
REMARK 500 PHE B 200 -39.09 65.62
REMARK 500 LEU B 201 -73.11 154.20
REMARK 500 SER B 202 -74.84 47.12
REMARK 500 THR B 245 55.00 -92.83
REMARK 500 ASP B 262 -60.55 -98.04
REMARK 500 PHE B 269 97.34 -161.25
REMARK 500 HIS B 301 -117.54 59.63
REMARK 500 TRP B 332 81.48 -150.53
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 MN A 406 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 211 OD2
REMARK 620 2 ASP A 213 OD2 151.6
REMARK 620 3 ASP A 213 OD1 97.3 54.9
REMARK 620 4 UDP A 475 O1A 91.1 87.6 75.8
REMARK 620 5 UDP A 475 O1B 99.4 108.9 156.4 87.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 406 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 211 OD2
REMARK 620 2 ASP B 213 OD1 108.5
REMARK 620 3 UDP B 475 O1B 98.4 150.4
REMARK 620 4 UDP B 475 O1A 94.3 76.1 90.2
REMARK 620 N 1 2 3
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ENGINEERED P156L MUTATION AND ENGINEERED EXPRESSION TAG
REMARK 999 INTRODUCING M63
DBREF 4C2S A 64 354 UNP P16442 BGAT_HUMAN 64 354
DBREF 4C2S B 64 354 UNP P16442 BGAT_HUMAN 64 354
SEQADV 4C2S MET A 63 UNP P16442 EXPRESSION TAG
SEQADV 4C2S LEU A 156 UNP P16442 PRO 156 ENGINEERED MUTATION
SEQADV 4C2S MET B 63 UNP P16442 EXPRESSION TAG
SEQADV 4C2S LEU B 156 UNP P16442 PRO 156 ENGINEERED MUTATION
SEQRES 1 A 292 MET VAL SER LEU PRO ARG MET VAL TYR PRO GLN PRO LYS
SEQRES 2 A 292 VAL LEU THR PRO CYS ARG LYS ASP VAL LEU VAL VAL THR
SEQRES 3 A 292 PRO TRP LEU ALA PRO ILE VAL TRP GLU GLY THR PHE ASN
SEQRES 4 A 292 ILE ASP ILE LEU ASN GLU GLN PHE ARG LEU GLN ASN THR
SEQRES 5 A 292 THR ILE GLY LEU THR VAL PHE ALA ILE LYS LYS TYR VAL
SEQRES 6 A 292 ALA PHE LEU LYS LEU PHE LEU GLU THR ALA GLU LYS HIS
SEQRES 7 A 292 PHE MET VAL GLY HIS ARG VAL HIS TYR TYR VAL PHE THR
SEQRES 8 A 292 ASP GLN LEU ALA ALA VAL PRO ARG VAL THR LEU GLY THR
SEQRES 9 A 292 GLY ARG GLN LEU SER VAL LEU GLU VAL ARG ALA TYR LYS
SEQRES 10 A 292 ARG TRP GLN ASP VAL SER MET ARG ARG MET GLU MET ILE
SEQRES 11 A 292 SER ASP PHE CYS GLU ARG ARG PHE LEU SER GLU VAL ASP
SEQRES 12 A 292 TYR LEU VAL CYS VAL ASP VAL ASP MET GLU PHE ARG ASP
SEQRES 13 A 292 HIS VAL GLY VAL GLU ILE LEU THR PRO LEU PHE GLY THR
SEQRES 14 A 292 LEU HIS PRO GLY PHE TYR GLY SER SER ARG GLU ALA PHE
SEQRES 15 A 292 THR TYR GLU ARG ARG PRO GLN SER GLN ALA TYR ILE PRO
SEQRES 16 A 292 LYS ASP GLU GLY ASP PHE TYR TYR LEU GLY GLY PHE PHE
SEQRES 17 A 292 GLY GLY SER VAL GLN GLU VAL GLN ARG LEU THR ARG ALA
SEQRES 18 A 292 CYS HIS GLN ALA MET MET VAL ASP GLN ALA ASN GLY ILE
SEQRES 19 A 292 GLU ALA VAL TRP HIS ASP GLU SER HIS LEU ASN LYS TYR
SEQRES 20 A 292 LEU LEU ARG HIS LYS PRO THR LYS VAL LEU SER PRO GLU
SEQRES 21 A 292 TYR LEU TRP ASP GLN GLN LEU LEU GLY TRP PRO ALA VAL
SEQRES 22 A 292 LEU ARG LYS LEU ARG PHE THR ALA VAL PRO LYS ASN HIS
SEQRES 23 A 292 GLN ALA VAL ARG ASN PRO
SEQRES 1 B 292 MET VAL SER LEU PRO ARG MET VAL TYR PRO GLN PRO LYS
SEQRES 2 B 292 VAL LEU THR PRO CYS ARG LYS ASP VAL LEU VAL VAL THR
SEQRES 3 B 292 PRO TRP LEU ALA PRO ILE VAL TRP GLU GLY THR PHE ASN
SEQRES 4 B 292 ILE ASP ILE LEU ASN GLU GLN PHE ARG LEU GLN ASN THR
SEQRES 5 B 292 THR ILE GLY LEU THR VAL PHE ALA ILE LYS LYS TYR VAL
SEQRES 6 B 292 ALA PHE LEU LYS LEU PHE LEU GLU THR ALA GLU LYS HIS
SEQRES 7 B 292 PHE MET VAL GLY HIS ARG VAL HIS TYR TYR VAL PHE THR
SEQRES 8 B 292 ASP GLN LEU ALA ALA VAL PRO ARG VAL THR LEU GLY THR
SEQRES 9 B 292 GLY ARG GLN LEU SER VAL LEU GLU VAL ARG ALA TYR LYS
SEQRES 10 B 292 ARG TRP GLN ASP VAL SER MET ARG ARG MET GLU MET ILE
SEQRES 11 B 292 SER ASP PHE CYS GLU ARG ARG PHE LEU SER GLU VAL ASP
SEQRES 12 B 292 TYR LEU VAL CYS VAL ASP VAL ASP MET GLU PHE ARG ASP
SEQRES 13 B 292 HIS VAL GLY VAL GLU ILE LEU THR PRO LEU PHE GLY THR
SEQRES 14 B 292 LEU HIS PRO GLY PHE TYR GLY SER SER ARG GLU ALA PHE
SEQRES 15 B 292 THR TYR GLU ARG ARG PRO GLN SER GLN ALA TYR ILE PRO
SEQRES 16 B 292 LYS ASP GLU GLY ASP PHE TYR TYR LEU GLY GLY PHE PHE
SEQRES 17 B 292 GLY GLY SER VAL GLN GLU VAL GLN ARG LEU THR ARG ALA
SEQRES 18 B 292 CYS HIS GLN ALA MET MET VAL ASP GLN ALA ASN GLY ILE
SEQRES 19 B 292 GLU ALA VAL TRP HIS ASP GLU SER HIS LEU ASN LYS TYR
SEQRES 20 B 292 LEU LEU ARG HIS LYS PRO THR LYS VAL LEU SER PRO GLU
SEQRES 21 B 292 TYR LEU TRP ASP GLN GLN LEU LEU GLY TRP PRO ALA VAL
SEQRES 22 B 292 LEU ARG LYS LEU ARG PHE THR ALA VAL PRO LYS ASN HIS
SEQRES 23 B 292 GLN ALA VAL ARG ASN PRO
HET DLG C 1 17
HET FUC C 2 10
HET DLG D 1 17
HET FUC D 2 10
HET MN A 406 1
HET UDP A 475 25
HET MN B 406 1
HET UDP B 475 25
HETNAM DLG HEXYL 3-DEOXY-BETA-D-GALACTOPYRANOSIDE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM MN MANGANESE (II) ION
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETSYN DLG HEXYL 3-DEOXY-BETA-D-GALACTOPYRANOSE; 2-HEXYLOXY-6-
HETSYN 2 DLG HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,5-DIOL; HEXYL 3-
HETSYN 3 DLG DEOXY-BETA-D-GALACTOSIDE; HEXYL 3-DEOXY-D-GALACTOSIDE;
HETSYN 4 DLG HEXYL 3-DEOXY-GALACTOSIDE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 3 DLG 2(C12 H24 O5)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 MN 2(MN 2+)
FORMUL 6 UDP 2(C9 H14 N2 O12 P2)
FORMUL 9 HOH *127(H2 O)
HELIX 1 1 ASN A 101 GLN A 112 1 12
HELIX 2 2 ILE A 123 ALA A 128 5 6
HELIX 3 3 PHE A 129 PHE A 141 1 13
HELIX 4 4 ARG A 180 ARG A 187 1 8
HELIX 5 5 ARG A 187 ARG A 199 1 13
HELIX 6 6 GLY A 221 LEU A 225 5 5
HELIX 7 7 SER A 240 PHE A 244 5 5
HELIX 8 8 VAL A 274 ASN A 294 1 21
HELIX 9 9 TRP A 300 HIS A 313 1 14
HELIX 10 10 PRO A 321 LEU A 324 5 4
HELIX 11 11 ASP A 326 GLY A 331 1 6
HELIX 12 12 ASN A 347 ASN A 353 1 7
HELIX 13 13 ASN B 101 GLN B 112 1 12
HELIX 14 14 ILE B 123 ALA B 128 5 6
HELIX 15 15 PHE B 129 PHE B 141 1 13
HELIX 16 16 ARG B 180 ARG B 187 1 8
HELIX 17 17 ARG B 187 PHE B 200 1 14
HELIX 18 18 GLY B 221 LEU B 225 5 5
HELIX 19 19 VAL B 274 ASN B 294 1 21
HELIX 20 20 TRP B 300 HIS B 313 1 14
HELIX 21 21 PRO B 321 LEU B 324 5 4
HELIX 22 22 ASP B 326 GLY B 331 1 6
HELIX 23 23 ASN B 347 ARG B 352 1 6
SHEET 1 AA 8 ILE A 94 VAL A 95 0
SHEET 2 AA 8 LYS A 317 LEU A 319 1 O VAL A 318 N VAL A 95
SHEET 3 AA 8 LEU A 228 THR A 231 1 O GLY A 230 N LEU A 319
SHEET 4 AA 8 PHE A 269 SER A 273 -1 O GLY A 271 N PHE A 229
SHEET 5 AA 8 TYR A 206 VAL A 210 -1 O LEU A 207 N GLY A 272
SHEET 6 AA 8 THR A 115 ALA A 122 1 O GLY A 117 N VAL A 208
SHEET 7 AA 8 ARG A 146 THR A 153 1 O ARG A 146 N ILE A 116
SHEET 8 AA 8 ARG A 168 GLU A 174 1 O GLN A 169 N TYR A 149
SHEET 1 AB 2 MET A 214 PHE A 216 0
SHEET 2 AB 2 PHE A 341 ALA A 343 -1 O THR A 342 N GLU A 215
SHEET 1 BA 8 ILE B 94 VAL B 95 0
SHEET 2 BA 8 LYS B 317 LEU B 319 1 O VAL B 318 N VAL B 95
SHEET 3 BA 8 LEU B 228 LEU B 232 1 O GLY B 230 N LEU B 319
SHEET 4 BA 8 TYR B 265 SER B 273 -1 N LEU B 266 O THR B 231
SHEET 5 BA 8 TYR B 206 VAL B 210 -1 O LEU B 207 N GLY B 272
SHEET 6 BA 8 THR B 115 PHE B 121 1 O GLY B 117 N VAL B 208
SHEET 7 BA 8 ARG B 146 THR B 153 1 O ARG B 146 N ILE B 116
SHEET 8 BA 8 ARG B 168 GLU B 174 1 O GLN B 169 N TYR B 149
SHEET 1 BB 2 MET B 214 PHE B 216 0
SHEET 2 BB 2 PHE B 341 ALA B 343 -1 O THR B 342 N GLU B 215
LINK O2 DLG C 1 C1 FUC C 2 1555 1555 1.44
LINK O2 DLG D 1 C1 FUC D 2 1555 1555 1.45
LINK OD2 ASP A 211 MN MN A 406 1555 1555 1.98
LINK OD2 ASP A 213 MN MN A 406 1555 1555 2.56
LINK OD1 ASP A 213 MN MN A 406 1555 1555 2.17
LINK MN MN A 406 O1A UDP A 475 1555 1555 2.33
LINK MN MN A 406 O1B UDP A 475 1555 1555 1.85
LINK OD2 ASP B 211 MN MN B 406 1555 1555 2.02
LINK OD1 ASP B 213 MN MN B 406 1555 1555 2.20
LINK MN MN B 406 O1B UDP B 475 1555 1555 1.92
LINK MN MN B 406 O1A UDP B 475 1555 1555 2.04
CRYST1 147.510 52.610 80.270 90.00 89.97 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 0.006779 0.000000 -0.000004 0.00000
SCALE2 0.000000 0.019008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012458 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
