HEADER TRANSFERASE 25-JUN-09 3I0G
TITLE CRYSTAL STRUCTURE OF GTB C80S/C196S + DA + UDP-GAL
CAVEAT 3I0G GAL A 359 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABO GLYCOSYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 59 TO 344;
COMPND 5 EC: 2.4.1.37;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GTB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCW(DELTA)LAC
KEYWDS GTB, GLYCOSYLTRANSFERASE, ABO BLOOD GROUP, RETAINING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SCHUMAN,M.PERSSON,R.C.LANDRY,R.POLAKOWSKI,J.T.WEADGE,N.O.L.SETO,
AUTHOR 2 S.BORISOVA,M.M.PALCIC,S.V.EVANS
REVDAT 5 06-SEP-23 3I0G 1 REMARK
REVDAT 4 13-OCT-21 3I0G 1 SEQADV HETSYN
REVDAT 3 29-JUL-20 3I0G 1 CAVEAT COMPND REMARK HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 06-OCT-10 3I0G 1 JRNL
REVDAT 1 11-AUG-10 3I0G 0
JRNL AUTH B.SCHUMAN,M.PERSSON,R.C.LANDRY,R.POLAKOWSKI,J.T.WEADGE,
JRNL AUTH 2 N.O.SETO,S.N.BORISOVA,M.M.PALCIC,S.V.EVANS
JRNL TITL CYSTEINE-TO-SERINE MUTANTS DRAMATICALLY REORDER THE ACTIVE
JRNL TITL 2 SITE OF HUMAN ABO(H) BLOOD GROUP B GLYCOSYLTRANSFERASE
JRNL TITL 3 WITHOUT AFFECTING ACTIVITY: STRUCTURAL INSIGHTS INTO
JRNL TITL 4 COOPERATIVE SUBSTRATE BINDING
JRNL REF J.MOL.BIOL. V. 402 399 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20655926
JRNL DOI 10.1016/J.JMB.2010.07.036
REMARK 2
REMARK 2 RESOLUTION. 1.40 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 55954
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2993
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3126
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.7470
REMARK 3 BIN FREE R VALUE SET COUNT : 177
REMARK 3 BIN FREE R VALUE : 0.7590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2183
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 344
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
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): 0.068
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.982
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2354 ; 0.030 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3208 ; 2.572 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 266 ; 6.619 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 111 ;31.602 ;22.703
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 376 ;13.225 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;20.694 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 361 ; 0.166 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1752 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1151 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1605 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 215 ; 0.128 ; 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): 53 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.198 ; 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): 1340 ; 1.429 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2180 ; 2.286 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1014 ; 3.450 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1028 ; 5.332 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3I0G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000053808.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 MICROMAX-002
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : OSMIC BLUE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.1SSI
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27621
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 19.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 4.550
REMARK 200 R MERGE (I) : 0.07400
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) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.22
REMARK 200 R MERGE FOR SHELL (I) : 0.31700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MOLECULAR REPLACEMENT
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1LZ7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35MM SODIUM ACETATE PH 4.6, 45 MM ADA,
REMARK 280 30MM SODIUM CHLORIDE, 3-4 MM MAGNESIUM CHLORIDE, 3-3.5% PEG 4000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 279.15K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 39.72700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.72700
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 26.27250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.63850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.27250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.63850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.72700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.27250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.63850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.72700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.27250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.63850
REMARK 290 SMTRY3 8 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: 5540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -39.72700
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 69
REMARK 465 ALA A 177
REMARK 465 TYR A 178
REMARK 465 LYS A 179
REMARK 465 ARG A 180
REMARK 465 TRP A 181
REMARK 465 GLN A 182
REMARK 465 ASP A 183
REMARK 465 VAL A 184
REMARK 465 LYS A 346
REMARK 465 ASN A 347
REMARK 465 HIS A 348
REMARK 465 GLN A 349
REMARK 465 ALA A 350
REMARK 465 VAL A 351
REMARK 465 ARG A 352
REMARK 465 ASN A 353
REMARK 465 PRO A 354
REMARK 465 GLU A 355
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 191 CG SD CE
REMARK 470 SER A 240 CB OG
REMARK 470 ILE A 296 CB CG1 CG2 CD1
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 PB UDP A 358 O1 GAL A 359 1.63
REMARK 500 O HOH A 391 O HOH A 480 1.71
REMARK 500 O HOH A 433 O HOH A 485 1.80
REMARK 500 N SER A 185 O HOH A 477 1.87
REMARK 500 CE MET A 288 O HOH A 499 1.94
REMARK 500 CA SER A 240 O HOH A 521 1.98
REMARK 500 O2B UDP A 358 O1 GAL A 359 2.10
REMARK 500 O HOH A 53 O HOH A 377 2.11
REMARK 500 CG GLU A 197 O HOH A 436 2.15
REMARK 500 O3B UDP A 358 O1 GAL A 359 2.15
REMARK 500 NH2 ARG A 146 O HOH A 552 2.17
REMARK 500 CE LYS A 139 O HOH A 558 2.17
REMARK 500 CD ARG A 188 O HOH A 488 2.18
REMARK 500 CG ARG A 188 O HOH A 488 2.19
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 A 497 O HOH A 497 4555 2.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL A 127 CB VAL A 127 CG1 -0.133
REMARK 500 LYS A 338 CE LYS A 338 NZ 0.180
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 ARG A 110 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 154 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 211 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 213 CB - CG - OD1 ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASP A 213 CB - CG - OD2 ANGL. DEV. = 15.7 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP A 218 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 241 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 241 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 PHE A 244 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 PHE A 269 CB - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG A 282 NE - CZ - NH2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP A 302 CB - CG - OD1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 337 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 340 NE - CZ - NH1 ANGL. DEV. = 4.3 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 LYS A 124 -127.92 56.60
REMARK 500 THR A 245 47.60 -86.96
REMARK 500 PHE A 269 100.87 -163.75
REMARK 500 HIS A 301 -136.09 54.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 BHG B 1
REMARK 610 UDP A 358
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 2 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 211 OD2
REMARK 620 2 ASP A 213 OD2 93.1
REMARK 620 3 UDP A 358 O1A 100.2 85.9
REMARK 620 4 HOH A 378 O 127.8 134.8 102.1
REMARK 620 5 HOH A 422 O 88.1 102.9 167.6 65.5
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LZ7 RELATED DB: PDB
REMARK 900 GTB
REMARK 900 RELATED ID: 3I0C RELATED DB: PDB
REMARK 900 GTB C80S/C196S UNLIGANDED
REMARK 900 RELATED ID: 3I0D RELATED DB: PDB
REMARK 900 GTB C80S/C196S + UDP
REMARK 900 RELATED ID: 3I0E RELATED DB: PDB
REMARK 900 GTB C80S/C196S + H ANTIGEN
REMARK 900 RELATED ID: 3I0F RELATED DB: PDB
REMARK 900 GTB C80S/C196S + UDP + H ANTIGEN
REMARK 900 RELATED ID: 3I0H RELATED DB: PDB
REMARK 900 GTB C80S/C196S/C209S UNLIGANDED
REMARK 900 RELATED ID: 3I0I RELATED DB: PDB
REMARK 900 GTB C80S/C196S/C209S + UDP
REMARK 900 RELATED ID: 3I0J RELATED DB: PDB
REMARK 900 GTB C80S/C196S/C209S + H ANTIGEN
REMARK 900 RELATED ID: 3I0K RELATED DB: PDB
REMARK 900 GTB C80S/C196S/C209S + UDP + H ANTIGEN
REMARK 900 RELATED ID: 3I0L RELATED DB: PDB
REMARK 900 GTB C80S/C196S/C209S + DA + UDP-GAL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT GLU 355 IS THE BIOLOGICAL C-TEMINUS
DBREF 3I0G A 69 354 UNP Q70V26 Q70V26_HUMAN 59 344
SEQADV 3I0G SER A 80 UNP Q70V26 CYS 70 ENGINEERED MUTATION
SEQADV 3I0G SER A 196 UNP Q70V26 CYS 186 ENGINEERED MUTATION
SEQADV 3I0G GLU A 355 UNP Q70V26 SEE REMARK 999
SEQRES 1 A 287 MET VAL TYR PRO GLN PRO LYS VAL LEU THR PRO SER ARG
SEQRES 2 A 287 LYS ASP VAL LEU VAL VAL THR PRO TRP LEU ALA PRO ILE
SEQRES 3 A 287 VAL TRP GLU GLY THR PHE ASN ILE ASP ILE LEU ASN GLU
SEQRES 4 A 287 GLN PHE ARG LEU GLN ASN THR THR ILE GLY LEU THR VAL
SEQRES 5 A 287 PHE ALA ILE LYS LYS TYR VAL ALA PHE LEU LYS LEU PHE
SEQRES 6 A 287 LEU GLU THR ALA GLU LYS HIS PHE MET VAL GLY HIS ARG
SEQRES 7 A 287 VAL HIS TYR TYR VAL PHE THR ASP GLN PRO ALA ALA VAL
SEQRES 8 A 287 PRO ARG VAL THR LEU GLY THR GLY ARG GLN LEU SER VAL
SEQRES 9 A 287 LEU GLU VAL GLY ALA TYR LYS ARG TRP GLN ASP VAL SER
SEQRES 10 A 287 MET ARG ARG MET GLU MET ILE SER ASP PHE SER GLU ARG
SEQRES 11 A 287 ARG PHE LEU SER GLU VAL ASP TYR LEU VAL CYS VAL ASP
SEQRES 12 A 287 VAL ASP MET GLU PHE ARG ASP HIS VAL GLY VAL GLU ILE
SEQRES 13 A 287 LEU THR PRO LEU PHE GLY THR LEU HIS PRO SER PHE TYR
SEQRES 14 A 287 GLY SER SER ARG GLU ALA PHE THR TYR GLU ARG ARG PRO
SEQRES 15 A 287 GLN SER GLN ALA TYR ILE PRO LYS ASP GLU GLY ASP PHE
SEQRES 16 A 287 TYR TYR MET GLY ALA PHE PHE GLY GLY SER VAL GLN GLU
SEQRES 17 A 287 VAL GLN ARG LEU THR ARG ALA CYS HIS GLN ALA MET MET
SEQRES 18 A 287 VAL ASP GLN ALA ASN GLY ILE GLU ALA VAL TRP HIS ASP
SEQRES 19 A 287 GLU SER HIS LEU ASN LYS TYR LEU LEU ARG HIS LYS PRO
SEQRES 20 A 287 THR LYS VAL LEU SER PRO GLU TYR LEU TRP ASP GLN GLN
SEQRES 21 A 287 LEU LEU GLY TRP PRO ALA VAL LEU ARG LYS LEU ARG PHE
SEQRES 22 A 287 THR ALA VAL PRO LYS ASN HIS GLN ALA VAL ARG ASN PRO
SEQRES 23 A 287 GLU
HET BHG B 1 17
HET FUC B 2 10
HET MN A 2 1
HET UDP A 357 25
HET UDP A 358 24
HET GAL A 359 12
HETNAM BHG HEXYL BETA-D-GALACTOPYRANOSIDE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM MN MANGANESE (II) ION
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETSYN BHG 2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-
HETSYN 2 BHG TRIOL; HEXYL BETA-D-GALACTOSIDE; HEXYL D-GALACTOSIDE;
HETSYN 3 BHG HEXYL GALACTOSIDE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
FORMUL 2 BHG C12 H24 O6
FORMUL 2 FUC C6 H12 O5
FORMUL 3 MN MN 2+
FORMUL 4 UDP 2(C9 H14 N2 O12 P2)
FORMUL 6 GAL C6 H12 O6
FORMUL 7 HOH *344(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 GLN A 155 VAL A 159 5 5
HELIX 5 5 MET A 186 GLU A 197 1 12
HELIX 6 6 ARG A 198 SER A 202 5 5
HELIX 7 7 GLY A 221 LEU A 225 5 5
HELIX 8 8 SER A 240 PHE A 244 5 5
HELIX 9 9 VAL A 274 ASN A 294 1 21
HELIX 10 10 TRP A 300 HIS A 313 1 14
HELIX 11 11 PRO A 321 LEU A 324 5 4
HELIX 12 12 ASP A 326 GLY A 331 1 6
SHEET 1 A 8 ILE A 94 VAL A 95 0
SHEET 2 A 8 LYS A 317 LEU A 319 1 O VAL A 318 N VAL A 95
SHEET 3 A 8 LEU A 228 THR A 231 1 N GLY A 230 O LEU A 319
SHEET 4 A 8 PHE A 269 SER A 273 -1 O GLY A 271 N PHE A 229
SHEET 5 A 8 TYR A 206 VAL A 210 -1 N CYS A 209 O PHE A 270
SHEET 6 A 8 THR A 115 ALA A 122 1 N GLY A 117 O TYR A 206
SHEET 7 A 8 ARG A 146 THR A 153 1 O TYR A 150 N LEU A 118
SHEET 8 A 8 ARG A 168 GLU A 174 1 O GLN A 169 N TYR A 149
SHEET 1 B 2 MET A 214 PHE A 216 0
SHEET 2 B 2 PHE A 341 ALA A 343 -1 O THR A 342 N GLU A 215
LINK O2 BHG B 1 C1 FUC B 2 1555 1555 1.48
LINK MN MN A 2 OD2 ASP A 211 1555 1555 2.04
LINK MN MN A 2 OD2 ASP A 213 1555 1555 2.46
LINK MN MN A 2 O1A UDP A 358 1555 1555 2.20
LINK MN MN A 2 O HOH A 378 1555 1555 2.19
LINK MN MN A 2 O HOH A 422 1555 1555 2.22
CISPEP 1 VAL A 175 GLY A 176 0 -13.94
CRYST1 52.545 149.277 79.454 90.00 90.00 90.00 C 2 2 21 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 0.019031 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006699 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012586 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
