HEADER TRANSFERASE 14-SEP-16 5LVV
TITLE HUMAN OGT IN COMPLEX WITH UDP AND FUSED SUBSTRATE PEPTIDE (TAB1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-
COMPND 3 ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT,UDP-N-
COMPND 4 ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA
COMPND 5 SUBUNIT;
COMPND 6 CHAIN: A;
COMPND 7 SYNONYM: O-GLCNAC TRANSFERASE SUBUNIT P110,O-LINKED N-
COMPND 8 ACETYLGLUCOSAMINE TRANSFERASE 110 KDA SUBUNIT,OGT,O-GLCNAC
COMPND 9 TRANSFERASE SUBUNIT P110,O-LINKED N-ACETYLGLUCOSAMINE TRANSFERASE 110
COMPND 10 KDA SUBUNIT,OGT;
COMPND 11 EC: 2.4.1.255,2.4.1.255;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: OGT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: PLYSIS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS GLYCOSYLATION, SIGNALLING, O-GLCNAC, O-GLCNAC TRANSFERASE, SUBSTRATE
KEYWDS 2 RECOGNITION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.RAIMI
REVDAT 4 17-JAN-24 5LVV 1 HETSYN
REVDAT 3 29-JUL-20 5LVV 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 20-FEB-19 5LVV 1 REMARK LINK
REVDAT 1 12-JUL-17 5LVV 0
JRNL AUTH K.RAFIE,O.RAIMI,A.T.FERENBACH,V.S.BORODKIN,V.KAPURIA,
JRNL AUTH 2 D.M.F.VAN AALTEN
JRNL TITL RECOGNITION OF A GLYCOSYLATION SUBSTRATE BY THE O-GLCNAC
JRNL TITL 2 TRANSFERASE TPR REPEATS.
JRNL REF OPEN BIOL V. 7 2017
JRNL REFN ESSN 2046-2441
JRNL PMID 28659383
JRNL DOI 10.1098/RSOB.170078
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 34136
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) : 0.193
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1795
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) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2482
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.4330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5664
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.43000
REMARK 3 B22 (A**2) : 2.43000
REMARK 3 B33 (A**2) : -7.89000
REMARK 3 B12 (A**2) : 1.22000
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): 0.361
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.260
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.239
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.758
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5867 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5582 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7964 ; 1.783 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12861 ; 1.052 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 718 ; 6.675 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 266 ;38.753 ;24.511
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 994 ;16.780 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;19.698 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 885 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6613 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1338 ; 0.002 ; 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): 2878 ; 5.026 ; 6.969
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2877 ; 5.026 ; 6.967
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3594 ; 7.253 ;10.447
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3595 ; 7.253 ;10.450
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2989 ; 5.650 ; 7.430
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2988 ; 5.649 ; 7.430
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4371 ; 8.146 ;10.923
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6377 ;10.244 ;54.605
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6376 ;10.245 ;54.606
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 : NULL
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 5LVV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 49.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 19.20
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 3PE4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM FORMATE, 0.1M TRIS PH 8.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 122.40000
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 244.80000
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 183.60000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 306.00000
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 61.20000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 122.40000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 244.80000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 306.00000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 183.60000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 61.20000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL
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 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 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 MET A 746
REMARK 465 LYS A 747
REMARK 465 CYS A 748
REMARK 465 PRO A 749
REMARK 465 ASP A 750
REMARK 465 GLY A 751
REMARK 465 GLY A 752
REMARK 465 ASP A 753
REMARK 465 ASN A 754
REMARK 465 ALA A 755
REMARK 465 ASP A 756
REMARK 465 SER A 757
REMARK 465 SER A 758
REMARK 465 ASN A 759
REMARK 465 THR A 760
REMARK 465 ALA A 761
REMARK 465 LEU A 762
REMARK 465 PRO A 1029
REMARK 465 VAL A 1030
REMARK 465 GLU A 1031
REMARK 465 VAL A 1032
REMARK 465 THR A 1033
REMARK 465 GLU A 1034
REMARK 465 SER A 1035
REMARK 465 ALA A 1036
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 A 328 NH1
REMARK 470 GLU A 345 OE2
REMARK 470 MET A 391 CE
REMARK 470 MET A 398 CE
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 604 OG SER A 606 0.83
REMARK 500 OG SER A 301 C1 NAG A 1204 0.83
REMARK 500 OG SER A 298 C1 NAG A 1203 1.08
REMARK 500 O GLN A 990 OG SER A 994 1.32
REMARK 500 OE2 GLU A 335 NH2 ARG A 338 1.38
REMARK 500 OD1 ASP A 587 OG1 THR A 589 1.54
REMARK 500 OG SER A 301 C2 NAG A 1204 1.63
REMARK 500 O ASN A 630 OG1 THR A 633 1.64
REMARK 500 OG SER A 298 O5 NAG A 1203 1.70
REMARK 500 CG ASP A 604 OG SER A 606 1.75
REMARK 500 O PHE A 693 OH TYR A 1002 1.80
REMARK 500 CB SER A 301 C1 NAG A 1204 1.83
REMARK 500 OG1 THR A 658 OE1 GLU A 684 1.87
REMARK 500 O HOH A 1318 O HOH A 1323 2.00
REMARK 500 OG SER A 301 N2 NAG A 1204 2.01
REMARK 500 CB LYS A 745 ND2 ASN A 763 2.02
REMARK 500 OD2 ASP A 712 O SER A 715 2.07
REMARK 500 OG SER A 301 O5 NAG A 1204 2.08
REMARK 500 OG SER A 297 O5 NAG A 1202 2.11
REMARK 500 OG1 THR A 940 OG SER A 943 2.11
REMARK 500 O PHE A 734 OG SER A 737 2.12
REMARK 500 O SER A 674 OH TYR A 688 2.17
REMARK 500 OD1 ASN A 393 OH TYR A 408 2.18
REMARK 500 OD1 ASP A 604 CB SER A 606 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 GLU A 349 46.03 -93.13
REMARK 500 GLN A 399 7.94 84.50
REMARK 500 LEU A 653 -54.60 70.99
REMARK 500 HIS A 718 127.35 91.87
REMARK 500 LEU A 885 83.52 158.56
REMARK 500 HIS A 920 -72.20 -112.20
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 NAG A 1203
REMARK 610 NAG A 1204
DBREF 5LVV A 294 311 PDB 5LVV 5LVV 294 311
DBREF 5LVV A 315 1036 UNP O15294 OGT1_HUMAN 199 920
SEQADV 5LVV HIS A 288 PDB EXPRESSION TAG
SEQADV 5LVV HIS A 289 PDB EXPRESSION TAG
SEQADV 5LVV HIS A 290 PDB EXPRESSION TAG
SEQADV 5LVV HIS A 291 PDB EXPRESSION TAG
SEQADV 5LVV HIS A 292 PDB EXPRESSION TAG
SEQADV 5LVV HIS A 293 PDB EXPRESSION TAG
SEQADV 5LVV GLY A 312 PDB LINKER
SEQADV 5LVV GLY A 313 PDB LINKER
SEQADV 5LVV GLY A 314 PDB LINKER
SEQRES 1 A 749 HIS HIS HIS HIS HIS HIS VAL PRO TYR SER SER ALA GLN
SEQRES 2 A 749 SER THR SER LYS THR SER VAL THR LEU SER LEU GLY GLY
SEQRES 3 A 749 GLY THR HIS ALA ASP SER LEU ASN ASN LEU ALA ASN ILE
SEQRES 4 A 749 LYS ARG GLU GLN GLY ASN ILE GLU GLU ALA VAL ARG LEU
SEQRES 5 A 749 TYR ARG LYS ALA LEU GLU VAL PHE PRO GLU PHE ALA ALA
SEQRES 6 A 749 ALA HIS SER ASN LEU ALA SER VAL LEU GLN GLN GLN GLY
SEQRES 7 A 749 LYS LEU GLN GLU ALA LEU MET HIS TYR LYS GLU ALA ILE
SEQRES 8 A 749 ARG ILE SER PRO THR PHE ALA ASP ALA TYR SER ASN MET
SEQRES 9 A 749 GLY ASN THR LEU LYS GLU MET GLN ASP VAL GLN GLY ALA
SEQRES 10 A 749 LEU GLN CYS TYR THR ARG ALA ILE GLN ILE ASN PRO ALA
SEQRES 11 A 749 PHE ALA ASP ALA HIS SER ASN LEU ALA SER ILE HIS LYS
SEQRES 12 A 749 ASP SER GLY ASN ILE PRO GLU ALA ILE ALA SER TYR ARG
SEQRES 13 A 749 THR ALA LEU LYS LEU LYS PRO ASP PHE PRO ASP ALA TYR
SEQRES 14 A 749 CYS ASN LEU ALA HIS CYS LEU GLN ILE VAL CYS ASP TRP
SEQRES 15 A 749 THR ASP TYR ASP GLU ARG MET LYS LYS LEU VAL SER ILE
SEQRES 16 A 749 VAL ALA ASP GLN LEU GLU LYS ASN ARG LEU PRO SER VAL
SEQRES 17 A 749 HIS PRO HIS HIS SER MET LEU TYR PRO LEU SER HIS GLY
SEQRES 18 A 749 PHE ARG LYS ALA ILE ALA GLU ARG HIS GLY ASN LEU CYS
SEQRES 19 A 749 LEU ASP LYS ILE ASN VAL LEU HIS LYS PRO PRO TYR GLU
SEQRES 20 A 749 HIS PRO LYS ASP LEU LYS LEU SER ASP GLY ARG LEU ARG
SEQRES 21 A 749 VAL GLY TYR VAL SER SER ASP PHE GLY ASN HIS PRO THR
SEQRES 22 A 749 SER HIS LEU MET GLN SER ILE PRO GLY MET HIS ASN PRO
SEQRES 23 A 749 ASP LYS PHE GLU VAL PHE CYS TYR ALA LEU SER PRO ASP
SEQRES 24 A 749 ASP GLY THR ASN PHE ARG VAL LYS VAL MET ALA GLU ALA
SEQRES 25 A 749 ASN HIS PHE ILE ASP LEU SER GLN ILE PRO CYS ASN GLY
SEQRES 26 A 749 LYS ALA ALA ASP ARG ILE HIS GLN ASP GLY ILE HIS ILE
SEQRES 27 A 749 LEU VAL ASN MET ASN GLY TYR THR LYS GLY ALA ARG ASN
SEQRES 28 A 749 GLU LEU PHE ALA LEU ARG PRO ALA PRO ILE GLN ALA MET
SEQRES 29 A 749 TRP LEU GLY TYR PRO GLY THR SER GLY ALA LEU PHE MET
SEQRES 30 A 749 ASP TYR ILE ILE THR ASP GLN GLU THR SER PRO ALA GLU
SEQRES 31 A 749 VAL ALA GLU GLN TYR SER GLU LYS LEU ALA TYR MET PRO
SEQRES 32 A 749 HIS THR PHE PHE ILE GLY ASP HIS ALA ASN MET PHE PRO
SEQRES 33 A 749 HIS LEU LYS LYS LYS ALA VAL ILE ASP PHE LYS SER ASN
SEQRES 34 A 749 GLY HIS ILE TYR ASP ASN ARG ILE VAL LEU ASN GLY ILE
SEQRES 35 A 749 ASP LEU LYS ALA PHE LEU ASP SER LEU PRO ASP VAL LYS
SEQRES 36 A 749 ILE VAL LYS MET LYS CYS PRO ASP GLY GLY ASP ASN ALA
SEQRES 37 A 749 ASP SER SER ASN THR ALA LEU ASN MET PRO VAL ILE PRO
SEQRES 38 A 749 MET ASN THR ILE ALA GLU ALA VAL ILE GLU MET ILE ASN
SEQRES 39 A 749 ARG GLY GLN ILE GLN ILE THR ILE ASN GLY PHE SER ILE
SEQRES 40 A 749 SER ASN GLY LEU ALA THR THR GLN ILE ASN ASN LYS ALA
SEQRES 41 A 749 ALA THR GLY GLU GLU VAL PRO ARG THR ILE ILE VAL THR
SEQRES 42 A 749 THR ARG SER GLN TYR GLY LEU PRO GLU ASP ALA ILE VAL
SEQRES 43 A 749 TYR CYS ASN PHE ASN GLN LEU TYR LYS ILE ASP PRO SER
SEQRES 44 A 749 THR LEU GLN MET TRP ALA ASN ILE LEU LYS ARG VAL PRO
SEQRES 45 A 749 ASN SER VAL LEU TRP LEU LEU ARG PHE PRO ALA VAL GLY
SEQRES 46 A 749 GLU PRO ASN ILE GLN GLN TYR ALA GLN ASN MET GLY LEU
SEQRES 47 A 749 PRO GLN ASN ARG ILE ILE PHE SER PRO VAL ALA PRO LYS
SEQRES 48 A 749 GLU GLU HIS VAL ARG ARG GLY GLN LEU ALA ASP VAL CYS
SEQRES 49 A 749 LEU ASP THR PRO LEU CYS ASN GLY HIS THR THR GLY MET
SEQRES 50 A 749 ASP VAL LEU TRP ALA GLY THR PRO MET VAL THR MET PRO
SEQRES 51 A 749 GLY GLU THR LEU ALA SER ARG VAL ALA ALA SER GLN LEU
SEQRES 52 A 749 THR CYS LEU GLY CYS LEU GLU LEU ILE ALA LYS ASN ARG
SEQRES 53 A 749 GLN GLU TYR GLU ASP ILE ALA VAL LYS LEU GLY THR ASP
SEQRES 54 A 749 LEU GLU TYR LEU LYS LYS VAL ARG GLY LYS VAL TRP LYS
SEQRES 55 A 749 GLN ARG ILE SER SER PRO LEU PHE ASN THR LYS GLN TYR
SEQRES 56 A 749 THR MET GLU LEU GLU ARG LEU TYR LEU GLN MET TRP GLU
SEQRES 57 A 749 HIS TYR ALA ALA GLY ASN LYS PRO ASP HIS MET ILE LYS
SEQRES 58 A 749 PRO VAL GLU VAL THR GLU SER ALA
HET UDP A1201 25
HET NAG A1202 14
HET NAG A1203 14
HET NAG A1204 14
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 UDP C9 H14 N2 O12 P2
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 6 HOH *40(H2 O)
HELIX 1 AA1 GLY A 314 GLY A 331 1 18
HELIX 2 AA2 ASN A 332 PHE A 347 1 16
HELIX 3 AA3 PHE A 350 GLN A 364 1 15
HELIX 4 AA4 LYS A 366 SER A 381 1 16
HELIX 5 AA5 PHE A 384 MET A 398 1 15
HELIX 6 AA6 ASP A 400 ASN A 415 1 16
HELIX 7 AA7 PHE A 418 GLY A 433 1 16
HELIX 8 AA8 ASN A 434 LYS A 449 1 16
HELIX 9 AA9 PHE A 452 VAL A 466 1 15
HELIX 10 AB1 ASP A 471 LYS A 489 1 19
HELIX 11 AB2 HIS A 496 MET A 501 1 6
HELIX 12 AB3 SER A 506 VAL A 527 1 22
HELIX 13 AB4 HIS A 558 GLN A 565 1 8
HELIX 14 AB5 SER A 566 HIS A 571 1 6
HELIX 15 AB6 THR A 589 ALA A 599 1 11
HELIX 16 AB7 SER A 606 ILE A 608 5 3
HELIX 17 AB8 CYS A 610 ASP A 621 1 12
HELIX 18 AB9 ASN A 638 LEU A 643 1 6
HELIX 19 AC1 PRO A 675 TYR A 682 5 8
HELIX 20 AC2 ASP A 697 PHE A 702 1 6
HELIX 21 AC3 PRO A 703 LYS A 706 5 4
HELIX 22 AC4 ASP A 730 SER A 737 1 8
HELIX 23 AC5 ASN A 770 GLY A 783 1 14
HELIX 24 AC6 ALA A 799 ASN A 804 1 6
HELIX 25 AC7 ASN A 804 THR A 809 1 6
HELIX 26 AC8 SER A 823 GLY A 826 5 4
HELIX 27 AC9 GLN A 839 ILE A 843 5 5
HELIX 28 AD1 ASP A 844 VAL A 858 1 15
HELIX 29 AD2 VAL A 871 GLY A 884 1 14
HELIX 30 AD3 PRO A 886 ASN A 888 5 3
HELIX 31 AD4 PRO A 897 ARG A 904 1 8
HELIX 32 AD5 GLY A 905 ALA A 908 5 4
HELIX 33 AD6 HIS A 920 ALA A 929 1 10
HELIX 34 AD7 THR A 940 SER A 943 5 4
HELIX 35 AD8 ARG A 944 GLY A 954 1 11
HELIX 36 AD9 CYS A 955 ILE A 959 5 5
HELIX 37 AE1 ASN A 962 ASP A 976 1 15
HELIX 38 AE2 ASP A 976 SER A 994 1 19
HELIX 39 AE3 ASN A 998 ALA A 1019 1 22
SHEET 1 AA1 7 HIS A 601 ASP A 604 0
SHEET 2 AA1 7 PHE A 576 ALA A 582 1 N CYS A 580 O HIS A 601
SHEET 3 AA1 7 LEU A 546 SER A 552 1 N TYR A 550 O TYR A 581
SHEET 4 AA1 7 ILE A 625 ASN A 628 1 O VAL A 627 N GLY A 549
SHEET 5 AA1 7 ILE A 648 MET A 651 1 O ALA A 650 N ASN A 628
SHEET 6 AA1 7 TYR A 666 ASP A 670 1 O TYR A 666 N MET A 651
SHEET 7 AA1 7 LYS A 685 MET A 689 1 O ALA A 687 N THR A 669
SHEET 1 AA2 7 LYS A 742 VAL A 744 0
SHEET 2 AA2 7 MET A 764 ILE A 767 -1 O MET A 764 N VAL A 744
SHEET 3 AA2 7 ALA A 709 ILE A 711 1 N VAL A 710 O ILE A 767
SHEET 4 AA2 7 ILE A 724 ASN A 727 -1 O LEU A 726 N ALA A 709
SHEET 5 AA2 7 ILE A 817 THR A 821 -1 O ILE A 818 N ASN A 727
SHEET 6 AA2 7 PHE A 792 ASN A 796 1 N SER A 795 O ILE A 817
SHEET 7 AA2 7 GLN A 786 ILE A 789 -1 N ILE A 787 O ILE A 794
SHEET 1 AA3 5 ILE A 890 PRO A 894 0
SHEET 2 AA3 5 VAL A 862 ARG A 867 1 N LEU A 863 O ILE A 891
SHEET 3 AA3 5 VAL A 833 CYS A 835 1 N TYR A 834 O VAL A 862
SHEET 4 AA3 5 VAL A 910 LEU A 912 1 O LEU A 912 N CYS A 835
SHEET 5 AA3 5 MET A 933 VAL A 934 1 O VAL A 934 N CYS A 911
LINK OG SER A 297 C1 NAG A1202 1555 1555 1.23
CISPEP 1 LYS A 714 SER A 715 0 -4.57
CISPEP 2 PHE A 868 PRO A 869 0 -0.05
CISPEP 3 GLY A 884 LEU A 885 0 -5.09
CRYST1 98.533 98.533 367.200 90.00 90.00 120.00 P 61 2 2 12
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 0.010149 0.005859 0.000000 0.00000
SCALE2 0.000000 0.011719 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002723 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
