HEADER ISOMERASE 18-FEB-12 4DSH
TITLE CRYSTAL STRUCTURE OF REDUCED UDP-GALACTOPYRANOSE MUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-GALACTOPYRANOSE MUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.4.99.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 GENE: TC00.1047053507993.160;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROSSMANN FOLD, FLAVIN ADENINE DINUCLEOTIDE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.DHATWALIA,H.SINGH,J.J.TANNER
REVDAT 3 13-SEP-23 4DSH 1 REMARK SEQADV
REVDAT 2 05-SEP-12 4DSH 1 JRNL
REVDAT 1 13-JUN-12 4DSH 0
JRNL AUTH R.DHATWALIA,H.SINGH,M.OPPENHEIMER,P.SOBRADO,J.J.TANNER
JRNL TITL CRYSTAL STRUCTURES OF TRYPANOSOMA CRUZI UDP-GALACTOPYRANOSE
JRNL TITL 2 MUTASE IMPLICATE FLEXIBILITY OF THE HISTIDINE LOOP IN ENZYME
JRNL TITL 3 ACTIVATION.
JRNL REF BIOCHEMISTRY V. 51 4968 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22646091
JRNL DOI 10.1021/BI300498C
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.2_432
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 102877
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 5134
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.9117 - 4.8459 0.99 10348 557 0.1707 0.1876
REMARK 3 2 4.8459 - 3.8469 1.00 9907 531 0.1304 0.1518
REMARK 3 3 3.8469 - 3.3608 1.00 9809 516 0.1801 0.2059
REMARK 3 4 3.3608 - 3.0536 1.00 9776 504 0.1994 0.2278
REMARK 3 5 3.0536 - 2.8347 1.00 9694 515 0.1876 0.2247
REMARK 3 6 2.8347 - 2.6676 1.00 9694 498 0.1936 0.2427
REMARK 3 7 2.6676 - 2.5340 1.00 9663 543 0.2030 0.2386
REMARK 3 8 2.5340 - 2.4237 1.00 9665 480 0.2125 0.2674
REMARK 3 9 2.4237 - 2.3304 1.00 9603 496 0.2252 0.2782
REMARK 3 10 2.3304 - 2.2500 1.00 9584 494 0.2381 0.2853
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 20.23
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.31090
REMARK 3 B22 (A**2) : 3.31090
REMARK 3 B33 (A**2) : -6.62170
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 7914
REMARK 3 ANGLE : 1.106 10820
REMARK 3 CHIRALITY : 0.073 1138
REMARK 3 PLANARITY : 0.005 1374
REMARK 3 DIHEDRAL : 15.538 2929
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 65.6826 -12.4597 -35.3515
REMARK 3 T TENSOR
REMARK 3 T11: 0.1531 T22: 0.0444
REMARK 3 T33: 0.0655 T12: -0.0313
REMARK 3 T13: 0.0031 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.1462 L22: 0.7861
REMARK 3 L33: 0.2070 L12: 0.0230
REMARK 3 L13: 0.0229 L23: -0.4412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0302 S12: -0.0175 S13: -0.0030
REMARK 3 S21: 0.1534 S22: 0.0018 S23: 0.0561
REMARK 3 S31: -0.0977 S32: -0.0087 S33: 0.0229
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 69.9004 -41.9500 -67.6645
REMARK 3 T TENSOR
REMARK 3 T11: 0.0395 T22: 0.0581
REMARK 3 T33: 0.0402 T12: -0.0201
REMARK 3 T13: -0.0293 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.4699 L22: 0.4046
REMARK 3 L33: 0.2583 L12: -0.0299
REMARK 3 L13: 0.0635 L23: 0.0898
REMARK 3 S TENSOR
REMARK 3 S11: 0.0161 S12: -0.0035 S13: 0.0524
REMARK 3 S21: -0.0606 S22: 0.0181 S23: 0.0173
REMARK 3 S31: 0.0092 S32: 0.0604 S33: -0.0320
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4DSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000070725.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102978
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 47.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.52600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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 3UTE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM SULFATE, 0.5% PEG8000,
REMARK 280 0.1 M HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 236.25933
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 118.12967
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 177.19450
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 59.06483
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 295.32417
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 236.25933
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 118.12967
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 59.06483
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 177.19450
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 295.32417
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA A -2
REMARK 465 ILE A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 GLN A 477
REMARK 465 LYS A 478
REMARK 465 ASP A 479
REMARK 465 MET A 480
REMARK 465 VAL A 481
REMARK 465 ALA B -2
REMARK 465 ILE B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 LEU B 4
REMARK 465 LEU B 5
REMARK 465 GLY B 466
REMARK 465 THR B 467
REMARK 465 ARG B 468
REMARK 465 ALA B 469
REMARK 465 THR B 470
REMARK 465 LEU B 476
REMARK 465 GLN B 477
REMARK 465 LYS B 478
REMARK 465 ASP B 479
REMARK 465 MET B 480
REMARK 465 VAL B 481
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 LYS A 31 CG CD CE NZ
REMARK 470 LYS A 115 CE NZ
REMARK 470 GLU A 131 OE1 OE2
REMARK 470 GLU A 146 CG CD OE1 OE2
REMARK 470 ASP A 150 OD1 OD2
REMARK 470 GLU A 171 CD OE1 OE2
REMARK 470 GLU A 174 OE1 OE2
REMARK 470 GLU A 183 CG CD OE1 OE2
REMARK 470 LYS A 278 CD CE NZ
REMARK 470 LYS A 336 NZ
REMARK 470 GLU A 341 CG CD OE1 OE2
REMARK 470 LYS A 354 CD CE NZ
REMARK 470 GLU A 407 CG CD OE1 OE2
REMARK 470 ARG A 428 CZ NH1 NH2
REMARK 470 GLU A 454 OE1 OE2
REMARK 470 ASN A 460 CG OD1 ND2
REMARK 470 ARG A 463 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 31 CE NZ
REMARK 470 GLU B 52 OE1 OE2
REMARK 470 LYS B 115 CE NZ
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 GLU B 171 CG CD OE1 OE2
REMARK 470 GLU B 174 OE1 OE2
REMARK 470 ARG B 184 NH1 NH2
REMARK 470 ARG B 187 NH1 NH2
REMARK 470 GLU B 226 CG CD OE1 OE2
REMARK 470 LYS B 273 CE NZ
REMARK 470 LYS B 278 CG CD CE NZ
REMARK 470 GLU B 282 OE1 OE2
REMARK 470 LYS B 336 NZ
REMARK 470 GLU B 341 CG CD OE1 OE2
REMARK 470 LYS B 354 CD CE NZ
REMARK 470 GLU B 407 CG CD OE1 OE2
REMARK 470 GLU B 412 OE1 OE2
REMARK 470 ARG B 428 CZ NH1 NH2
REMARK 470 GLU B 454 CD OE1 OE2
REMARK 470 ARG B 463 CG CD NE CZ NH1 NH2
REMARK 470 THR B 471 OG1 CG2
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 152 -59.90 -123.30
REMARK 500 ASN A 192 55.73 39.57
REMARK 500 PHE A 234 40.08 -100.82
REMARK 500 CYS A 314 -78.79 -105.30
REMARK 500 THR A 467 -168.42 -124.60
REMARK 500 PHE B 152 -55.72 -125.84
REMARK 500 PHE B 234 42.78 -103.88
REMARK 500 CYS B 314 -83.05 -100.24
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 UDP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FDA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FDA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
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: 4DSG RELATED DB: PDB
DBREF 4DSH A 1 480 UNP Q4E1W2 Q4E1W2_TRYCC 1 480
DBREF 4DSH B 1 480 UNP Q4E1W2 Q4E1W2_TRYCC 1 480
SEQADV 4DSH ALA A -2 UNP Q4E1W2 EXPRESSION TAG
SEQADV 4DSH ILE A -1 UNP Q4E1W2 EXPRESSION TAG
SEQADV 4DSH ALA A 0 UNP Q4E1W2 EXPRESSION TAG
SEQADV 4DSH VAL A 481 UNP Q4E1W2 CLONING ARTIFACT
SEQADV 4DSH ALA B -2 UNP Q4E1W2 EXPRESSION TAG
SEQADV 4DSH ILE B -1 UNP Q4E1W2 EXPRESSION TAG
SEQADV 4DSH ALA B 0 UNP Q4E1W2 EXPRESSION TAG
SEQADV 4DSH VAL B 481 UNP Q4E1W2 CLONING ARTIFACT
SEQRES 1 A 484 ALA ILE ALA MET ALA GLU LEU LEU THR PRO LYS ILE VAL
SEQRES 2 A 484 ILE ILE GLY ALA GLY PRO THR GLY LEU GLY ALA ALA VAL
SEQRES 3 A 484 ARG LEU THR GLU LEU GLY TYR LYS ASN TRP HIS LEU TYR
SEQRES 4 A 484 GLU CYS ASN ASP THR PRO GLY GLY LEU SER ARG SER PHE
SEQRES 5 A 484 LEU ASP GLU ASN GLY PHE THR TRP ASP LEU GLY GLY HIS
SEQRES 6 A 484 VAL ILE PHE SER HIS TYR GLN TYR PHE ASP ASP VAL MET
SEQRES 7 A 484 ASP TRP ALA VAL GLN GLY TRP ASN VAL LEU GLN ARG GLU
SEQRES 8 A 484 SER TRP VAL TRP VAL ARG GLY ARG TRP VAL PRO TYR PRO
SEQRES 9 A 484 PHE GLN ASN ASN ILE HIS ARG LEU PRO GLU GLN ASP ARG
SEQRES 10 A 484 LYS ARG CYS LEU ASP GLU LEU VAL ARG SER HIS ALA ARG
SEQRES 11 A 484 THR TYR THR GLU PRO PRO ASN ASN PHE GLU GLU SER PHE
SEQRES 12 A 484 THR ARG GLN PHE GLY GLU GLY ILE ALA ASP ILE PHE MET
SEQRES 13 A 484 ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO PRO CYS
SEQRES 14 A 484 LEU MET SER THR GLU TRP VAL GLU GLU ARG VAL ALA PRO
SEQRES 15 A 484 VAL ASP LEU GLU ARG ILE ARG ARG ASN ILE GLN GLU ASN
SEQRES 16 A 484 ARG ASP ASP LEU GLY TRP GLY PRO ASN ALA THR PHE ARG
SEQRES 17 A 484 PHE PRO GLN ARG GLY GLY THR GLY ILE ILE TYR GLN ALA
SEQRES 18 A 484 ILE LYS GLU LYS LEU PRO SER GLU LYS LEU THR PHE ASN
SEQRES 19 A 484 SER GLY PHE GLN ALA ILE ALA ILE ASP ALA ASP ALA LYS
SEQRES 20 A 484 THR ILE THR PHE SER ASN GLY GLU VAL VAL SER TYR ASP
SEQRES 21 A 484 TYR LEU ILE SER THR VAL PRO PHE ASP ASN LEU LEU ARG
SEQRES 22 A 484 MET THR LYS GLY THR GLY PHE LYS GLY TYR ASP GLU TRP
SEQRES 23 A 484 PRO ALA ILE ALA ASP LYS MET VAL TYR SER SER THR ASN
SEQRES 24 A 484 VAL ILE GLY ILE GLY VAL LYS GLY THR PRO PRO PRO HIS
SEQRES 25 A 484 LEU LYS THR ALA CYS TRP LEU TYR PHE PRO GLU ASP THR
SEQRES 26 A 484 SER PRO PHE TYR ARG ALA THR VAL PHE SER ASN TYR SER
SEQRES 27 A 484 LYS TYR ASN VAL PRO GLU GLY HIS TRP SER LEU MET LEU
SEQRES 28 A 484 GLU VAL SER GLU SER LYS TYR LYS PRO VAL ASN HIS SER
SEQRES 29 A 484 THR LEU ILE GLU ASP CYS ILE VAL GLY CYS LEU ALA SER
SEQRES 30 A 484 ASN LEU LEU LEU PRO GLU ASP LEU LEU VAL SER LYS TRP
SEQRES 31 A 484 HIS TYR ARG ILE GLU LYS GLY TYR PRO THR PRO PHE ILE
SEQRES 32 A 484 GLY ARG ASN ASN LEU LEU GLU LYS ALA GLN PRO GLU LEU
SEQRES 33 A 484 MET SER ARG CYS ILE TYR SER ARG GLY ARG PHE GLY ALA
SEQRES 34 A 484 TRP ARG TYR GLU VAL GLY ASN GLN ASP HIS SER PHE MET
SEQRES 35 A 484 GLN GLY VAL GLU ALA ILE ASP HIS VAL LEU GLY LEU ALA
SEQRES 36 A 484 THR GLU GLU THR THR VAL ALA ASN PRO GLY ARG VAL ASN
SEQRES 37 A 484 GLY THR ARG ALA THR THR HIS PHE GLY LEU LEU GLN LYS
SEQRES 38 A 484 ASP MET VAL
SEQRES 1 B 484 ALA ILE ALA MET ALA GLU LEU LEU THR PRO LYS ILE VAL
SEQRES 2 B 484 ILE ILE GLY ALA GLY PRO THR GLY LEU GLY ALA ALA VAL
SEQRES 3 B 484 ARG LEU THR GLU LEU GLY TYR LYS ASN TRP HIS LEU TYR
SEQRES 4 B 484 GLU CYS ASN ASP THR PRO GLY GLY LEU SER ARG SER PHE
SEQRES 5 B 484 LEU ASP GLU ASN GLY PHE THR TRP ASP LEU GLY GLY HIS
SEQRES 6 B 484 VAL ILE PHE SER HIS TYR GLN TYR PHE ASP ASP VAL MET
SEQRES 7 B 484 ASP TRP ALA VAL GLN GLY TRP ASN VAL LEU GLN ARG GLU
SEQRES 8 B 484 SER TRP VAL TRP VAL ARG GLY ARG TRP VAL PRO TYR PRO
SEQRES 9 B 484 PHE GLN ASN ASN ILE HIS ARG LEU PRO GLU GLN ASP ARG
SEQRES 10 B 484 LYS ARG CYS LEU ASP GLU LEU VAL ARG SER HIS ALA ARG
SEQRES 11 B 484 THR TYR THR GLU PRO PRO ASN ASN PHE GLU GLU SER PHE
SEQRES 12 B 484 THR ARG GLN PHE GLY GLU GLY ILE ALA ASP ILE PHE MET
SEQRES 13 B 484 ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO PRO CYS
SEQRES 14 B 484 LEU MET SER THR GLU TRP VAL GLU GLU ARG VAL ALA PRO
SEQRES 15 B 484 VAL ASP LEU GLU ARG ILE ARG ARG ASN ILE GLN GLU ASN
SEQRES 16 B 484 ARG ASP ASP LEU GLY TRP GLY PRO ASN ALA THR PHE ARG
SEQRES 17 B 484 PHE PRO GLN ARG GLY GLY THR GLY ILE ILE TYR GLN ALA
SEQRES 18 B 484 ILE LYS GLU LYS LEU PRO SER GLU LYS LEU THR PHE ASN
SEQRES 19 B 484 SER GLY PHE GLN ALA ILE ALA ILE ASP ALA ASP ALA LYS
SEQRES 20 B 484 THR ILE THR PHE SER ASN GLY GLU VAL VAL SER TYR ASP
SEQRES 21 B 484 TYR LEU ILE SER THR VAL PRO PHE ASP ASN LEU LEU ARG
SEQRES 22 B 484 MET THR LYS GLY THR GLY PHE LYS GLY TYR ASP GLU TRP
SEQRES 23 B 484 PRO ALA ILE ALA ASP LYS MET VAL TYR SER SER THR ASN
SEQRES 24 B 484 VAL ILE GLY ILE GLY VAL LYS GLY THR PRO PRO PRO HIS
SEQRES 25 B 484 LEU LYS THR ALA CYS TRP LEU TYR PHE PRO GLU ASP THR
SEQRES 26 B 484 SER PRO PHE TYR ARG ALA THR VAL PHE SER ASN TYR SER
SEQRES 27 B 484 LYS TYR ASN VAL PRO GLU GLY HIS TRP SER LEU MET LEU
SEQRES 28 B 484 GLU VAL SER GLU SER LYS TYR LYS PRO VAL ASN HIS SER
SEQRES 29 B 484 THR LEU ILE GLU ASP CYS ILE VAL GLY CYS LEU ALA SER
SEQRES 30 B 484 ASN LEU LEU LEU PRO GLU ASP LEU LEU VAL SER LYS TRP
SEQRES 31 B 484 HIS TYR ARG ILE GLU LYS GLY TYR PRO THR PRO PHE ILE
SEQRES 32 B 484 GLY ARG ASN ASN LEU LEU GLU LYS ALA GLN PRO GLU LEU
SEQRES 33 B 484 MET SER ARG CYS ILE TYR SER ARG GLY ARG PHE GLY ALA
SEQRES 34 B 484 TRP ARG TYR GLU VAL GLY ASN GLN ASP HIS SER PHE MET
SEQRES 35 B 484 GLN GLY VAL GLU ALA ILE ASP HIS VAL LEU GLY LEU ALA
SEQRES 36 B 484 THR GLU GLU THR THR VAL ALA ASN PRO GLY ARG VAL ASN
SEQRES 37 B 484 GLY THR ARG ALA THR THR HIS PHE GLY LEU LEU GLN LYS
SEQRES 38 B 484 ASP MET VAL
HET UDP A 501 25
HET FDA A 502 53
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET EPE A 506 15
HET FDA B 501 53
HET UDP B 502 25
HET SO4 B 503 5
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETNAM FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE
HETNAM SO4 SULFATE ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 3 UDP 2(C9 H14 N2 O12 P2)
FORMUL 4 FDA 2(C27 H35 N9 O15 P2)
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 8 EPE C8 H18 N2 O4 S
FORMUL 12 HOH *246(H2 O)
HELIX 1 1 GLY A 15 GLY A 29 1 15
HELIX 2 2 GLY A 43 SER A 46 5 4
HELIX 3 3 TYR A 68 VAL A 79 1 12
HELIX 4 4 PRO A 101 LEU A 109 5 9
HELIX 5 5 PRO A 110 ALA A 126 1 17
HELIX 6 6 ASN A 135 PHE A 152 1 18
HELIX 7 7 PHE A 152 ALA A 162 1 11
HELIX 8 8 PRO A 164 MET A 168 5 5
HELIX 9 9 THR A 170 GLU A 174 5 5
HELIX 10 10 ASP A 181 ASN A 192 1 12
HELIX 11 11 THR A 212 LEU A 223 1 12
HELIX 12 12 PRO A 224 GLU A 226 5 3
HELIX 13 13 SER A 232 PHE A 234 5 3
HELIX 14 14 PRO A 264 MET A 271 1 8
HELIX 15 15 GLY A 279 ASP A 281 5 3
HELIX 16 16 GLU A 282 MET A 290 1 9
HELIX 17 17 PRO A 307 LYS A 311 5 5
HELIX 18 18 PHE A 331 TYR A 334 5 4
HELIX 19 19 SER A 335 VAL A 339 5 5
HELIX 20 20 THR A 362 SER A 374 1 13
HELIX 21 21 GLY A 401 SER A 415 1 15
HELIX 22 22 ARG A 428 GLY A 432 5 5
HELIX 23 23 ASN A 433 LEU A 449 1 17
HELIX 24 24 GLU A 455 ASN A 460 1 6
HELIX 25 25 ASN A 460 THR A 467 1 8
HELIX 26 26 GLY B 15 LEU B 28 1 14
HELIX 27 27 GLY B 43 SER B 46 5 4
HELIX 28 28 TYR B 68 VAL B 79 1 12
HELIX 29 29 PRO B 101 LEU B 109 5 9
HELIX 30 30 PRO B 110 ARG B 127 1 18
HELIX 31 31 ASN B 135 PHE B 152 1 18
HELIX 32 32 PHE B 152 ALA B 162 1 11
HELIX 33 33 PRO B 164 MET B 168 5 5
HELIX 34 34 THR B 170 GLU B 174 5 5
HELIX 35 35 ASP B 181 ASN B 192 1 12
HELIX 36 36 THR B 212 LEU B 223 1 12
HELIX 37 37 PRO B 224 GLU B 226 5 3
HELIX 38 38 SER B 232 PHE B 234 5 3
HELIX 39 39 PRO B 264 MET B 271 1 8
HELIX 40 40 GLY B 279 ASP B 281 5 3
HELIX 41 41 GLU B 282 MET B 290 1 9
HELIX 42 42 PRO B 307 LYS B 311 5 5
HELIX 43 43 PHE B 331 TYR B 334 5 4
HELIX 44 44 SER B 335 VAL B 339 5 5
HELIX 45 45 THR B 362 SER B 374 1 13
HELIX 46 46 GLY B 401 ARG B 416 1 16
HELIX 47 47 ARG B 428 GLY B 432 5 5
HELIX 48 48 ASN B 433 LEU B 449 1 17
HELIX 49 49 GLU B 455 ASN B 460 1 6
HELIX 50 50 ASN B 460 ASN B 465 1 6
SHEET 1 A 5 LEU A 228 PHE A 230 0
SHEET 2 A 5 TRP A 33 GLU A 37 1 N GLU A 37 O THR A 229
SHEET 3 A 5 ILE A 9 ILE A 12 1 N ILE A 11 O TYR A 36
SHEET 4 A 5 TYR A 258 SER A 261 1 O ILE A 260 N VAL A 10
SHEET 5 A 5 ILE A 418 SER A 420 1 O TYR A 419 N LEU A 259
SHEET 1 B 2 SER A 48 LEU A 50 0
SHEET 2 B 2 THR A 56 ASP A 58 -1 O TRP A 57 N PHE A 49
SHEET 1 C 2 TRP A 82 GLN A 86 0
SHEET 2 C 2 THR A 203 PRO A 207 -1 O PHE A 206 N ASN A 83
SHEET 1 D 7 ARG A 96 PRO A 99 0
SHEET 2 D 7 TRP A 90 VAL A 93 -1 N VAL A 91 O VAL A 98
SHEET 3 D 7 TRP A 315 TYR A 317 1 O TYR A 317 N TRP A 92
SHEET 4 D 7 ARG A 327 THR A 329 -1 O ALA A 328 N LEU A 316
SHEET 5 D 7 HIS A 343 GLU A 352 -1 O MET A 347 N THR A 329
SHEET 6 D 7 TYR A 292 LYS A 303 -1 N ILE A 298 O LEU A 348
SHEET 7 D 7 LEU A 383 PRO A 396 -1 O ILE A 391 N THR A 295
SHEET 1 E 4 VAL A 253 SER A 255 0
SHEET 2 E 4 THR A 245 PHE A 248 -1 N ILE A 246 O VAL A 254
SHEET 3 E 4 ALA A 236 ASP A 240 -1 N ALA A 238 O THR A 247
SHEET 4 E 4 THR A 272 LYS A 273 1 O LYS A 273 N ILE A 239
SHEET 1 F 5 LEU B 228 PHE B 230 0
SHEET 2 F 5 TRP B 33 GLU B 37 1 N GLU B 37 O THR B 229
SHEET 3 F 5 ILE B 9 ILE B 12 1 N ILE B 11 O HIS B 34
SHEET 4 F 5 TYR B 258 SER B 261 1 O ILE B 260 N VAL B 10
SHEET 5 F 5 ILE B 418 SER B 420 1 O TYR B 419 N LEU B 259
SHEET 1 G 2 SER B 48 LEU B 50 0
SHEET 2 G 2 THR B 56 ASP B 58 -1 O TRP B 57 N PHE B 49
SHEET 1 H 2 TRP B 82 GLN B 86 0
SHEET 2 H 2 THR B 203 PRO B 207 -1 O PHE B 204 N LEU B 85
SHEET 1 I 7 ARG B 96 PRO B 99 0
SHEET 2 I 7 TRP B 90 VAL B 93 -1 N VAL B 91 O VAL B 98
SHEET 3 I 7 TRP B 315 TYR B 317 1 O TYR B 317 N TRP B 90
SHEET 4 I 7 ARG B 327 THR B 329 -1 O ALA B 328 N LEU B 316
SHEET 5 I 7 HIS B 343 GLU B 352 -1 O MET B 347 N THR B 329
SHEET 6 I 7 TYR B 292 LYS B 303 -1 N SER B 294 O GLU B 352
SHEET 7 I 7 LEU B 383 PRO B 396 -1 O TRP B 387 N GLY B 299
SHEET 1 J 4 VAL B 253 SER B 255 0
SHEET 2 J 4 THR B 245 PHE B 248 -1 N ILE B 246 O VAL B 254
SHEET 3 J 4 ALA B 236 ASP B 240 -1 N ALA B 238 O THR B 247
SHEET 4 J 4 THR B 272 LYS B 273 1 O LYS B 273 N ILE B 239
SSBOND 1 CYS A 166 CYS B 166 1555 1555 2.11
CISPEP 1 TYR A 100 PRO A 101 0 -4.88
CISPEP 2 TYR B 100 PRO B 101 0 -1.24
SITE 1 AC1 20 TYR A 100 PRO A 101 PHE A 102 GLN A 103
SITE 2 AC1 20 PHE A 152 MET A 153 ASN A 157 TRP A 161
SITE 3 AC1 20 ARG A 176 VAL A 177 TYR A 317 ARG A 327
SITE 4 AC1 20 TYR A 395 TYR A 429 HOH A 616 HOH A 630
SITE 5 AC1 20 HOH A 632 HOH A 633 HOH A 634 HOH A 671
SITE 1 AC2 35 ILE A 12 GLY A 13 GLY A 15 PRO A 16
SITE 2 AC2 35 THR A 17 GLU A 37 CYS A 38 ASN A 39
SITE 3 AC2 35 GLY A 44 LEU A 45 SER A 46 LEU A 59
SITE 4 AC2 35 GLY A 61 HIS A 62 VAL A 63 PHE A 65
SITE 5 AC2 35 PHE A 234 GLN A 235 ALA A 236 VAL A 263
SITE 6 AC2 35 GLU A 349 GLY A 394 GLY A 422 ARG A 423
SITE 7 AC2 35 GLY A 432 ASN A 433 GLN A 434 SER A 437
SITE 8 AC2 35 HOH A 601 HOH A 605 HOH A 617 HOH A 619
SITE 9 AC2 35 HOH A 660 HOH A 664 HOH A 715
SITE 1 AC3 4 ARG A 270 TYR A 292 HOH A 644 HOH A 665
SITE 1 AC4 4 HIS A 388 TYR A 389 ARG A 390 EPE A 506
SITE 1 AC5 4 VAL A 358 ASN A 359 HIS A 360 SER A 361
SITE 1 AC6 7 HIS A 388 TYR A 389 ARG A 390 GLU A 392
SITE 2 AC6 7 SO4 A 504 HOH A 668 HOH A 709
SITE 1 AC7 35 ILE B 12 GLY B 13 GLY B 15 PRO B 16
SITE 2 AC7 35 THR B 17 GLU B 37 CYS B 38 ASN B 39
SITE 3 AC7 35 GLY B 43 GLY B 44 LEU B 45 SER B 46
SITE 4 AC7 35 LEU B 59 GLY B 61 HIS B 62 VAL B 63
SITE 5 AC7 35 PHE B 234 GLN B 235 ALA B 236 THR B 262
SITE 6 AC7 35 VAL B 263 GLU B 349 GLY B 394 GLY B 422
SITE 7 AC7 35 ARG B 423 GLY B 432 ASN B 433 GLN B 434
SITE 8 AC7 35 SER B 437 HOH B 602 HOH B 605 HOH B 628
SITE 9 AC7 35 HOH B 629 HOH B 632 HOH B 671
SITE 1 AC8 20 TYR B 100 PRO B 101 PHE B 102 GLN B 103
SITE 2 AC8 20 PHE B 152 MET B 153 ASN B 157 TRP B 161
SITE 3 AC8 20 ARG B 176 VAL B 177 TYR B 317 ARG B 327
SITE 4 AC8 20 TYR B 395 TYR B 429 HOH B 603 HOH B 604
SITE 5 AC8 20 HOH B 641 HOH B 642 HOH B 644 HOH B 668
SITE 1 AC9 5 ASP B 266 ARG B 270 TYR B 292 HOH B 664
SITE 2 AC9 5 HOH B 703
CRYST1 143.840 143.840 354.389 90.00 90.00 120.00 P 65 2 2 24
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 0.006952 0.004014 0.000000 0.00000
SCALE2 0.000000 0.008028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002822 0.00000
(ATOM LINES ARE NOT SHOWN.)
END