HEADER TRANSFERASE 16-JUL-15 5CMF
TITLE GTA MUTANT WITH MERCURY - E303A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 64-345);
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 EC: 2.4.1.40,2.4.1.37;
COMPND 12 ENGINEERED: YES;
COMPND 13 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: ABO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HUMAN ABO(H) BLOOD GROUP SYSTEM, GLYCOSYLTRANSFERASE, DOUBLE TURN
KEYWDS 2 MOTIF, CATALYTIC DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.L.GAGNON,R.J.BLACKLER
REVDAT 6 27-SEP-23 5CMF 1 REMARK
REVDAT 5 07-MAR-18 5CMF 1 REMARK
REVDAT 4 19-APR-17 5CMF 1 JRNL
REVDAT 3 11-JAN-17 5CMF 1 JRNL
REVDAT 2 07-DEC-16 5CMF 1 JRNL
REVDAT 1 20-JUL-16 5CMF 0
JRNL AUTH R.J.BLACKLER,S.M.GAGNON,R.POLAKOWSKI,N.L.ROSE,R.B.ZHENG,
JRNL AUTH 2 J.A.LETTS,A.R.JOHAL,B.SCHUMAN,S.N.BORISOVA,M.M.PALCIC,
JRNL AUTH 3 S.V.EVANS
JRNL TITL GLYCOSYLTRANSFER IN MUTANTS OF PUTATIVE CATALYTIC RESIDUE
JRNL TITL 2 GLU303 OF THE HUMAN ABO(H) A AND B BLOOD GROUP
JRNL TITL 3 GLYCOSYLTRANSFERASES GTA AND GTB PROCEEDS THROUGH A LABILE
JRNL TITL 4 ACTIVE SITE.
JRNL REF GLYCOBIOLOGY V. 27 370 2017
JRNL REFN ESSN 1460-2423
JRNL PMID 27979997
JRNL DOI 10.1093/GLYCOB/CWW117
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 20666
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1113
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1471
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3930
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.3900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2128
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 118
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.87000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : 0.57000
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): 0.187
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.967
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2186 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2088 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2970 ; 1.190 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4779 ; 0.730 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 260 ; 6.083 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 102 ;33.026 ;22.647
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 356 ;13.552 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;16.391 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 328 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2436 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 537 ; 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): 1047 ; 1.685 ; 3.967
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1046 ; 1.686 ; 3.965
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1306 ; 2.687 ; 5.930
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 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 5CMF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211813.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : NULL
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : D*TREK 8.0SSI
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21791
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 (%) : 94.9
REMARK 200 DATA REDUNDANCY : 3.860
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.45
REMARK 200 R MERGE FOR SHELL (I) : 0.30900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1LZ0
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: 10 UL DROPS WITH 6-8 MG/ML PROTEIN, 70
REMARK 280 MM N-(2-ACETAMIDO)-2-IMINODIACETIC ACID (ADA) PH 7.5, 50 MM,
REMARK 280 SODIUM ACETATE PH 4.6, 40 MM NACL, 5-8 MM MNCL2, 2.5% (V/V) 2-
REMARK 280 METHYL-2,4-PENTANEDIOL (MPD), 5%(V/V) GLYCEROL, 2%(W/V) PEG 4000,
REMARK 280 AND 0.3-0.5 MM 3-CHLOROMERCURI-2-METHOXYPROPYLUREA SUSPENDED
REMARK 280 OVER 1 ML OF A RESEVOIR SOLUTION: 50 MM ADA PH 7.5, 10 MM MNCL2,
REMARK 280 100 MM AMMONIUM SULFATE, 5%(V/V) MPD, 10%(V/V) GLYCEROL, AND 8-
REMARK 280 10%(W/V) PEG 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
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 39.48500
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 39.48500
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 26.20500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.20500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.48500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.20500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.50000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.48500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.20500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.50000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 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 X 571 LIES ON A SPECIAL POSITION.
REMARK 375 HOH X 618 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 ALA X 177
REMARK 465 TYR X 178
REMARK 465 LYS X 179
REMARK 465 ARG X 180
REMARK 465 TRP X 181
REMARK 465 GLN X 182
REMARK 465 ASP X 183
REMARK 465 VAL X 184
REMARK 465 SER X 185
REMARK 465 MET X 186
REMARK 465 ARG X 187
REMARK 465 ARG X 188
REMARK 465 MET X 189
REMARK 465 GLU X 190
REMARK 465 MET X 191
REMARK 465 ILE X 192
REMARK 465 SER X 193
REMARK 465 ASP X 194
REMARK 465 ALA X 298
REMARK 465 VAL X 299
REMARK 465 TRP X 300
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 ARG X 176 CG CD NE CZ NH1 NH2
REMARK 470 PHE X 195 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU X 297 CG CD OE1 OE2
REMARK 470 HIS X 301 CG ND1 CD2 CE1 NE2
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 X 596 O HOH X 596 4555 2.19
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 X 124 -117.09 45.38
REMARK 500 LEU X 324 96.39 -161.30
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 HG X 401 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR X 119 OG1
REMARK 620 2 CYS X 209 SG 83.8
REMARK 620 3 HOH X 617 O 114.7 161.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HG X 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HG X 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HG X 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HG X 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CMG RELATED DB: PDB
REMARK 900 RELATED ID: 5CMH RELATED DB: PDB
REMARK 900 RELATED ID: 5CMI RELATED DB: PDB
REMARK 900 RELATED ID: 5CMJ RELATED DB: PDB
REMARK 900 RELATED ID: 5CQL RELATED DB: PDB
REMARK 900 RELATED ID: 5CQM RELATED DB: PDB
REMARK 900 RELATED ID: 5CQN RELATED DB: PDB
REMARK 900 RELATED ID: 5CQO RELATED DB: PDB
REMARK 900 RELATED ID: 5CQP RELATED DB: PDB
DBREF 5CMF X 64 345 UNP P16442 BGAT_HUMAN 64 345
SEQADV 5CMF PHE X 62 UNP P16442 EXPRESSION TAG
SEQADV 5CMF MET X 63 UNP P16442 EXPRESSION TAG
SEQADV 5CMF ALA X 303 UNP P16442 GLU 303 ENGINEERED MUTATION
SEQRES 1 X 284 PHE MET VAL SER LEU PRO ARG MET VAL TYR PRO GLN PRO
SEQRES 2 X 284 LYS VAL LEU THR PRO CYS ARG LYS ASP VAL LEU VAL VAL
SEQRES 3 X 284 THR PRO TRP LEU ALA PRO ILE VAL TRP GLU GLY THR PHE
SEQRES 4 X 284 ASN ILE ASP ILE LEU ASN GLU GLN PHE ARG LEU GLN ASN
SEQRES 5 X 284 THR THR ILE GLY LEU THR VAL PHE ALA ILE LYS LYS TYR
SEQRES 6 X 284 VAL ALA PHE LEU LYS LEU PHE LEU GLU THR ALA GLU LYS
SEQRES 7 X 284 HIS PHE MET VAL GLY HIS ARG VAL HIS TYR TYR VAL PHE
SEQRES 8 X 284 THR ASP GLN PRO ALA ALA VAL PRO ARG VAL THR LEU GLY
SEQRES 9 X 284 THR GLY ARG GLN LEU SER VAL LEU GLU VAL ARG ALA TYR
SEQRES 10 X 284 LYS ARG TRP GLN ASP VAL SER MET ARG ARG MET GLU MET
SEQRES 11 X 284 ILE SER ASP PHE CYS GLU ARG ARG PHE LEU SER GLU VAL
SEQRES 12 X 284 ASP TYR LEU VAL CYS VAL ASP VAL ASP MET GLU PHE ARG
SEQRES 13 X 284 ASP HIS VAL GLY VAL GLU ILE LEU THR PRO LEU PHE GLY
SEQRES 14 X 284 THR LEU HIS PRO GLY PHE TYR GLY SER SER ARG GLU ALA
SEQRES 15 X 284 PHE THR TYR GLU ARG ARG PRO GLN SER GLN ALA TYR ILE
SEQRES 16 X 284 PRO LYS ASP GLU GLY ASP PHE TYR TYR LEU GLY GLY PHE
SEQRES 17 X 284 PHE GLY GLY SER VAL GLN GLU VAL GLN ARG LEU THR ARG
SEQRES 18 X 284 ALA CYS HIS GLN ALA MET MET VAL ASP GLN ALA ASN GLY
SEQRES 19 X 284 ILE GLU ALA VAL TRP HIS ASP ALA SER HIS LEU ASN LYS
SEQRES 20 X 284 TYR LEU LEU ARG HIS LYS PRO THR LYS VAL LEU SER PRO
SEQRES 21 X 284 GLU TYR LEU TRP ASP GLN GLN LEU LEU GLY TRP PRO ALA
SEQRES 22 X 284 VAL LEU ARG LYS LEU ARG PHE THR ALA VAL PRO
HET HG X 401 1
HET HG X 402 1
HET HG X 403 1
HET HG X 404 1
HETNAM HG MERCURY (II) ION
FORMUL 2 HG 4(HG 2+)
FORMUL 6 HOH *118(H2 O)
HELIX 1 AA1 ASN X 101 GLN X 112 1 12
HELIX 2 AA2 ILE X 123 ALA X 128 5 6
HELIX 3 AA3 PHE X 129 PHE X 141 1 13
HELIX 4 AA4 GLN X 155 VAL X 159 5 5
HELIX 5 AA5 CYS X 196 VAL X 204 1 9
HELIX 6 AA6 GLY X 221 LEU X 225 5 5
HELIX 7 AA7 SER X 240 PHE X 244 5 5
HELIX 8 AA8 VAL X 274 ASN X 294 1 21
HELIX 9 AA9 ASP X 302 HIS X 313 1 12
HELIX 10 AB1 PRO X 321 LEU X 324 5 4
HELIX 11 AB2 ASP X 326 GLY X 331 1 6
SHEET 1 AA1 8 ILE X 94 VAL X 95 0
SHEET 2 AA1 8 LYS X 317 LEU X 319 1 O VAL X 318 N VAL X 95
SHEET 3 AA1 8 LEU X 228 LEU X 232 1 N GLY X 230 O LEU X 319
SHEET 4 AA1 8 TYR X 265 SER X 273 -1 O GLY X 271 N PHE X 229
SHEET 5 AA1 8 TYR X 206 VAL X 210 -1 N LEU X 207 O GLY X 272
SHEET 6 AA1 8 THR X 115 ALA X 122 1 N THR X 119 O VAL X 208
SHEET 7 AA1 8 ARG X 146 THR X 153 1 O PHE X 152 N ALA X 122
SHEET 8 AA1 8 ARG X 168 GLU X 174 1 O GLN X 169 N TYR X 149
SHEET 1 AA2 2 MET X 214 PHE X 216 0
SHEET 2 AA2 2 PHE X 341 ALA X 343 -1 O THR X 342 N GLU X 215
LINK O GLY X 98 HG HG X 402 1555 1555 2.92
LINK OG1 THR X 119 HG HG X 401 1555 1555 2.94
LINK SG CYS X 209 HG HG X 401 1555 1555 2.48
LINK SG CYS X 284 HG HG X 404 1555 1555 2.31
LINK HG HG X 401 O HOH X 617 1555 1555 2.78
LINK HG HG X 403 O HOH X 551 1555 1555 2.70
SITE 1 AC1 3 THR X 119 CYS X 209 HOH X 617
SITE 1 AC2 2 CYS X 80 GLY X 98
SITE 1 AC3 3 CYS X 209 VAL X 210 HOH X 551
SITE 1 AC4 2 LEU X 280 CYS X 284
CRYST1 52.410 149.000 78.970 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 0.019080 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006711 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012663 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
