HEADER LYASE 14-AUG-12 4GLL
TITLE CRYSTAL STRUCTURE OF HUMAN UDP-XYLOSE SYNTHASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-GLUCURONIC ACID DECARBOXYLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SOLUBLE UXS DOMAIN; RESIDUES 85-420;
COMPND 5 SYNONYM: UDP-GLUCURONATE DECARBOXYLASE 1, UGD, UXS-1;
COMPND 6 EC: 4.1.1.35;
COMPND 7 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: UNQ2538/PRO6079, UXS, UXS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS SHORT-CHAIN DEHYDROGENASE/REDUCTASE, DECARBOXYLASE, LYASE, MEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.A.WOOD,S.J.POLIZZI
REVDAT 5 13-SEP-23 4GLL 1 REMARK SEQADV
REVDAT 4 17-JUL-19 4GLL 1 REMARK
REVDAT 3 02-MAY-18 4GLL 1 JRNL
REVDAT 2 14-NOV-12 4GLL 1 JRNL
REVDAT 1 05-SEP-12 4GLL 0
SPRSDE 05-SEP-12 4GLL 4EF7
JRNL AUTH S.J.POLIZZI,R.M.WALSH JR.,W.B.PEEPLES,J.M.LIM,L.WELLS,
JRNL AUTH 2 Z.A.WOOD
JRNL TITL HUMAN UDP-ALPHA-D-XYLOSE SYNTHASE AND ESCHERICHIA COLI ARNA
JRNL TITL 2 CONSERVE A CONFORMATIONAL SHUNT THAT CONTROLS WHETHER XYLOSE
JRNL TITL 3 OR 4-KETO-XYLOSE IS PRODUCED.
JRNL REF BIOCHEMISTRY V. 51 8844 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 23072385
JRNL DOI 10.1021/BI301135B
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0044
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 29894
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1589
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2133
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4837
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 136
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.01000
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): 0.329
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.234
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
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 : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5056 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6865 ; 1.440 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 610 ; 7.899 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 236 ;37.542 ;24.364
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 847 ;19.217 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;20.079 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 748 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3826 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3049 ; 2.911 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4918 ; 4.581 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2007 ; 3.423 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1947 ; 5.189 ; 4.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 2376 ; 0.59 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 2376 ; 4.39 ; 10.00
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: NULL
REMARK 4
REMARK 4 4GLL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074336.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31483
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2B69
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 M AMMONIUM SULFATE, 0.1 M
REMARK 280 MAGNESIUM FORMATE AND 0.15% 1.5K PEG, PH 8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 65.94667
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 32.97333
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 32.97333
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 65.94667
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: 6200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 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 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 84
REMARK 465 GLU A 85
REMARK 465 LYS A 86
REMARK 465 ASP A 87
REMARK 465 LEU A 395
REMARK 465 GLU A 396
REMARK 465 TYR A 397
REMARK 465 GLN A 398
REMARK 465 ALA A 399
REMARK 465 ASN A 400
REMARK 465 ASN A 401
REMARK 465 GLN A 402
REMARK 465 TYR A 403
REMARK 465 ILE A 404
REMARK 465 PRO A 405
REMARK 465 LYS A 406
REMARK 465 PRO A 407
REMARK 465 LYS A 408
REMARK 465 PRO A 409
REMARK 465 ALA A 410
REMARK 465 ARG A 411
REMARK 465 ILE A 412
REMARK 465 LYS A 413
REMARK 465 LYS A 414
REMARK 465 GLY A 415
REMARK 465 ARG A 416
REMARK 465 THR A 417
REMARK 465 ARG A 418
REMARK 465 HIS A 419
REMARK 465 SER A 420
REMARK 465 MET B 84
REMARK 465 GLU B 85
REMARK 465 LYS B 86
REMARK 465 ASP B 87
REMARK 465 PRO B 166
REMARK 465 ASN B 167
REMARK 465 TYR B 168
REMARK 465 MET B 169
REMARK 465 TYR B 170
REMARK 465 ALA B 399
REMARK 465 ASN B 400
REMARK 465 ASN B 401
REMARK 465 GLN B 402
REMARK 465 TYR B 403
REMARK 465 ILE B 404
REMARK 465 PRO B 405
REMARK 465 LYS B 406
REMARK 465 PRO B 407
REMARK 465 LYS B 408
REMARK 465 PRO B 409
REMARK 465 ALA B 410
REMARK 465 ARG B 411
REMARK 465 ILE B 412
REMARK 465 LYS B 413
REMARK 465 LYS B 414
REMARK 465 GLY B 415
REMARK 465 ARG B 416
REMARK 465 THR B 417
REMARK 465 ARG B 418
REMARK 465 HIS B 419
REMARK 465 SER B 420
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 PHE A 99 -73.76 -56.05
REMARK 500 SER A 161 132.46 179.13
REMARK 500 ARG A 265 -1.64 84.06
REMARK 500 PHE B 99 -72.00 -55.49
REMARK 500 ASP B 119 138.85 -174.94
REMARK 500 ALA B 160 98.25 -68.83
REMARK 500 THR B 180 -84.28 -92.44
REMARK 500 PRO B 213 -178.97 -68.73
REMARK 500 ARG B 265 -3.16 92.93
REMARK 500 ASN B 269 59.36 -92.28
REMARK 500 SER B 344 -8.94 -152.43
REMARK 500 GLN B 349 120.17 -171.36
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 NAD A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B69 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH URIDINE DIPHOSPHATE (UDP). THE 2B69
REMARK 900 PROTEIN CONSTRUCT HAS A ~20 AMINO ACID TRUNCATION AT THE C-TERMINUS
REMARK 900 THAT REMOVES A PREDICTED DISORDERED HELIX.
DBREF 4GLL A 85 420 UNP Q8NBZ7 UXS1_HUMAN 85 420
DBREF 4GLL B 85 420 UNP Q8NBZ7 UXS1_HUMAN 85 420
SEQADV 4GLL MET A 84 UNP Q8NBZ7 EXPRESSION TAG
SEQADV 4GLL MET B 84 UNP Q8NBZ7 EXPRESSION TAG
SEQRES 1 A 337 MET GLU LYS ASP ARG LYS ARG ILE LEU ILE THR GLY GLY
SEQRES 2 A 337 ALA GLY PHE VAL GLY SER HIS LEU THR ASP LYS LEU MET
SEQRES 3 A 337 MET ASP GLY HIS GLU VAL THR VAL VAL ASP ASN PHE PHE
SEQRES 4 A 337 THR GLY ARG LYS ARG ASN VAL GLU HIS TRP ILE GLY HIS
SEQRES 5 A 337 GLU ASN PHE GLU LEU ILE ASN HIS ASP VAL VAL GLU PRO
SEQRES 6 A 337 LEU TYR ILE GLU VAL ASP GLN ILE TYR HIS LEU ALA SER
SEQRES 7 A 337 PRO ALA SER PRO PRO ASN TYR MET TYR ASN PRO ILE LYS
SEQRES 8 A 337 THR LEU LYS THR ASN THR ILE GLY THR LEU ASN MET LEU
SEQRES 9 A 337 GLY LEU ALA LYS ARG VAL GLY ALA ARG LEU LEU LEU ALA
SEQRES 10 A 337 SER THR SER GLU VAL TYR GLY ASP PRO GLU VAL HIS PRO
SEQRES 11 A 337 GLN SER GLU ASP TYR TRP GLY HIS VAL ASN PRO ILE GLY
SEQRES 12 A 337 PRO ARG ALA CYS TYR ASP GLU GLY LYS ARG VAL ALA GLU
SEQRES 13 A 337 THR MET CYS TYR ALA TYR MET LYS GLN GLU GLY VAL GLU
SEQRES 14 A 337 VAL ARG VAL ALA ARG ILE PHE ASN THR PHE GLY PRO ARG
SEQRES 15 A 337 MET HIS MET ASN ASP GLY ARG VAL VAL SER ASN PHE ILE
SEQRES 16 A 337 LEU GLN ALA LEU GLN GLY GLU PRO LEU THR VAL TYR GLY
SEQRES 17 A 337 SER GLY SER GLN THR ARG ALA PHE GLN TYR VAL SER ASP
SEQRES 18 A 337 LEU VAL ASN GLY LEU VAL ALA LEU MET ASN SER ASN VAL
SEQRES 19 A 337 SER SER PRO VAL ASN LEU GLY ASN PRO GLU GLU HIS THR
SEQRES 20 A 337 ILE LEU GLU PHE ALA GLN LEU ILE LYS ASN LEU VAL GLY
SEQRES 21 A 337 SER GLY SER GLU ILE GLN PHE LEU SER GLU ALA GLN ASP
SEQRES 22 A 337 ASP PRO GLN LYS ARG LYS PRO ASP ILE LYS LYS ALA LYS
SEQRES 23 A 337 LEU MET LEU GLY TRP GLU PRO VAL VAL PRO LEU GLU GLU
SEQRES 24 A 337 GLY LEU ASN LYS ALA ILE HIS TYR PHE ARG LYS GLU LEU
SEQRES 25 A 337 GLU TYR GLN ALA ASN ASN GLN TYR ILE PRO LYS PRO LYS
SEQRES 26 A 337 PRO ALA ARG ILE LYS LYS GLY ARG THR ARG HIS SER
SEQRES 1 B 337 MET GLU LYS ASP ARG LYS ARG ILE LEU ILE THR GLY GLY
SEQRES 2 B 337 ALA GLY PHE VAL GLY SER HIS LEU THR ASP LYS LEU MET
SEQRES 3 B 337 MET ASP GLY HIS GLU VAL THR VAL VAL ASP ASN PHE PHE
SEQRES 4 B 337 THR GLY ARG LYS ARG ASN VAL GLU HIS TRP ILE GLY HIS
SEQRES 5 B 337 GLU ASN PHE GLU LEU ILE ASN HIS ASP VAL VAL GLU PRO
SEQRES 6 B 337 LEU TYR ILE GLU VAL ASP GLN ILE TYR HIS LEU ALA SER
SEQRES 7 B 337 PRO ALA SER PRO PRO ASN TYR MET TYR ASN PRO ILE LYS
SEQRES 8 B 337 THR LEU LYS THR ASN THR ILE GLY THR LEU ASN MET LEU
SEQRES 9 B 337 GLY LEU ALA LYS ARG VAL GLY ALA ARG LEU LEU LEU ALA
SEQRES 10 B 337 SER THR SER GLU VAL TYR GLY ASP PRO GLU VAL HIS PRO
SEQRES 11 B 337 GLN SER GLU ASP TYR TRP GLY HIS VAL ASN PRO ILE GLY
SEQRES 12 B 337 PRO ARG ALA CYS TYR ASP GLU GLY LYS ARG VAL ALA GLU
SEQRES 13 B 337 THR MET CYS TYR ALA TYR MET LYS GLN GLU GLY VAL GLU
SEQRES 14 B 337 VAL ARG VAL ALA ARG ILE PHE ASN THR PHE GLY PRO ARG
SEQRES 15 B 337 MET HIS MET ASN ASP GLY ARG VAL VAL SER ASN PHE ILE
SEQRES 16 B 337 LEU GLN ALA LEU GLN GLY GLU PRO LEU THR VAL TYR GLY
SEQRES 17 B 337 SER GLY SER GLN THR ARG ALA PHE GLN TYR VAL SER ASP
SEQRES 18 B 337 LEU VAL ASN GLY LEU VAL ALA LEU MET ASN SER ASN VAL
SEQRES 19 B 337 SER SER PRO VAL ASN LEU GLY ASN PRO GLU GLU HIS THR
SEQRES 20 B 337 ILE LEU GLU PHE ALA GLN LEU ILE LYS ASN LEU VAL GLY
SEQRES 21 B 337 SER GLY SER GLU ILE GLN PHE LEU SER GLU ALA GLN ASP
SEQRES 22 B 337 ASP PRO GLN LYS ARG LYS PRO ASP ILE LYS LYS ALA LYS
SEQRES 23 B 337 LEU MET LEU GLY TRP GLU PRO VAL VAL PRO LEU GLU GLU
SEQRES 24 B 337 GLY LEU ASN LYS ALA ILE HIS TYR PHE ARG LYS GLU LEU
SEQRES 25 B 337 GLU TYR GLN ALA ASN ASN GLN TYR ILE PRO LYS PRO LYS
SEQRES 26 B 337 PRO ALA ARG ILE LYS LYS GLY ARG THR ARG HIS SER
HET NAD A 800 44
HET GAI A 801 4
HET SO4 A 802 5
HET NAD B 501 44
HET GAI B 502 4
HET SO4 B 503 5
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM GAI GUANIDINE
HETNAM SO4 SULFATE ION
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 4 GAI 2(C H5 N3)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 9 HOH *136(H2 O)
HELIX 1 1 GLY A 98 ASP A 111 1 14
HELIX 2 2 ARG A 125 ILE A 133 5 9
HELIX 3 3 SER A 164 ASN A 171 1 8
HELIX 4 4 ASN A 171 GLY A 194 1 24
HELIX 5 5 GLU A 204 GLY A 207 5 4
HELIX 6 6 ARG A 228 GLY A 250 1 23
HELIX 7 7 ARG A 272 GLN A 283 1 12
HELIX 8 8 VAL A 302 ASN A 314 1 13
HELIX 9 9 ILE A 331 GLY A 343 1 13
HELIX 10 10 ILE A 365 GLY A 373 1 9
HELIX 11 11 PRO A 379 LYS A 393 1 15
HELIX 12 12 GLY B 98 ASP B 111 1 14
HELIX 13 13 ARG B 125 ILE B 133 5 9
HELIX 14 14 PRO B 172 THR B 180 1 9
HELIX 15 15 THR B 180 GLY B 194 1 15
HELIX 16 16 GLU B 204 GLY B 207 5 4
HELIX 17 17 ARG B 228 GLY B 250 1 23
HELIX 18 18 ARG B 272 GLN B 283 1 12
HELIX 19 19 VAL B 302 ASN B 314 1 13
HELIX 20 20 ILE B 331 GLY B 343 1 13
HELIX 21 21 ILE B 365 GLY B 373 1 9
HELIX 22 22 PRO B 379 GLU B 396 1 18
SHEET 1 A 7 PHE A 138 ASN A 142 0
SHEET 2 A 7 GLU A 114 ASP A 119 1 N VAL A 117 O ILE A 141
SHEET 3 A 7 ARG A 90 THR A 94 1 N ILE A 91 O THR A 116
SHEET 4 A 7 GLN A 155 HIS A 158 1 O TYR A 157 N LEU A 92
SHEET 5 A 7 ARG A 196 THR A 202 1 O ARG A 196 N ILE A 156
SHEET 6 A 7 GLU A 252 ILE A 258 1 O ARG A 254 N LEU A 199
SHEET 7 A 7 VAL A 321 LEU A 323 1 O LEU A 323 N ARG A 257
SHEET 1 B 2 THR A 261 PHE A 262 0
SHEET 2 B 2 GLN A 300 TYR A 301 1 O GLN A 300 N PHE A 262
SHEET 1 C 2 LEU A 287 TYR A 290 0
SHEET 2 C 2 ILE A 348 LEU A 351 1 O GLN A 349 N VAL A 289
SHEET 1 D 2 THR A 296 ARG A 297 0
SHEET 2 D 2 HIS A 329 THR A 330 -1 O HIS A 329 N ARG A 297
SHEET 1 E 7 PHE B 138 ASN B 142 0
SHEET 2 E 7 GLU B 114 ASP B 119 1 N VAL B 117 O ILE B 141
SHEET 3 E 7 ARG B 90 THR B 94 1 N ILE B 91 O GLU B 114
SHEET 4 E 7 GLN B 155 HIS B 158 1 O GLN B 155 N LEU B 92
SHEET 5 E 7 ARG B 196 THR B 202 1 O LEU B 198 N HIS B 158
SHEET 6 E 7 VAL B 253 ILE B 258 1 O ARG B 254 N LEU B 199
SHEET 7 E 7 VAL B 321 LEU B 323 1 O VAL B 321 N ARG B 257
SHEET 1 F 2 THR B 261 PHE B 262 0
SHEET 2 F 2 GLN B 300 TYR B 301 1 O GLN B 300 N PHE B 262
SHEET 1 G 2 LEU B 287 TYR B 290 0
SHEET 2 G 2 ILE B 348 LEU B 351 1 O GLN B 349 N VAL B 289
SHEET 1 H 2 THR B 296 ARG B 297 0
SHEET 2 H 2 HIS B 329 THR B 330 -1 O HIS B 329 N ARG B 297
CISPEP 1 HIS A 212 PRO A 213 0 -5.98
CISPEP 2 SER B 164 PRO B 165 0 -1.38
CISPEP 3 HIS B 212 PRO B 213 0 -10.61
SITE 1 AC1 26 GLY A 95 ALA A 97 GLY A 98 PHE A 99
SITE 2 AC1 26 VAL A 100 ASP A 119 ASN A 120 PHE A 121
SITE 3 AC1 26 PHE A 122 THR A 123 GLY A 124 HIS A 143
SITE 4 AC1 26 ASP A 144 VAL A 145 LEU A 159 ALA A 160
SITE 5 AC1 26 SER A 161 ALA A 163 THR A 178 SER A 201
SITE 6 AC1 26 TYR A 231 LYS A 235 ILE A 258 THR A 261
SITE 7 AC1 26 HIS A 267 HOH A 940
SITE 1 AC2 4 THR A 288 TYR A 290 ILE A 331 ASP A 356
SITE 1 AC3 5 SER A 203 PHE A 259 ASN A 260 GLN A 359
SITE 2 AC3 5 ARG A 361
SITE 1 AC4 31 GLY B 95 GLY B 98 PHE B 99 VAL B 100
SITE 2 AC4 31 ASP B 119 ASN B 120 PHE B 121 PHE B 122
SITE 3 AC4 31 THR B 123 GLY B 124 HIS B 143 ASP B 144
SITE 4 AC4 31 VAL B 145 LEU B 159 ALA B 160 SER B 161
SITE 5 AC4 31 PRO B 162 ALA B 163 LYS B 174 THR B 178
SITE 6 AC4 31 ALA B 200 THR B 202 TYR B 231 LYS B 235
SITE 7 AC4 31 ILE B 258 PHE B 259 ASN B 260 THR B 261
SITE 8 AC4 31 HIS B 267 ARG B 272 HOH B 608
SITE 1 AC5 3 THR B 288 TYR B 290 ASP B 356
SITE 1 AC6 7 TYR B 150 ARG B 192 TYR B 290 SER B 292
SITE 2 AC6 7 GLY B 293 SER B 294 GLN B 295
CRYST1 125.610 125.610 98.920 90.00 90.00 120.00 P 32 2 1 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 0.007961 0.004596 0.000000 0.00000
SCALE2 0.000000 0.009193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010109 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
