HEADER TRANSFERASE 28-AUG-14 4R7P
TITLE HUMAN UDP-GLUCOSE PYROPHOSPHORYLASE ISOFORM 1 IN COMPLEX WITH UDP-
TITLE 2 GLUCOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UDP-GLUCOSE PYROPHOSPHORYLASE;
COMPND 5 SYNONYM: UDP-GLUCOSE PYROPHOSPHORYLASE, UDPGP, UGPASE;
COMPND 6 EC: 2.7.7.9;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: UGP2, UGP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROSSMANN-LIKE ALPHA/BETA/ALPHA SANDWICH FOLD, PYROPHOSPHORYLASE, UTP,
KEYWDS 2 GLC-1-P, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.FUEHRING,J.T.CRAMER,J.SCHNEIDER,P.BARUCH,R.GERARDY-SCHAHN,R.FEDOROV
REVDAT 2 28-FEB-24 4R7P 1 REMARK SEQADV LINK
REVDAT 1 22-APR-15 4R7P 0
JRNL AUTH J.I.FUHRING,J.T.CRAMER,J.SCHNEIDER,P.BARUCH,
JRNL AUTH 2 R.GERARDY-SCHAHN,R.FEDOROV
JRNL TITL A QUATERNARY MECHANISM ENABLES THE COMPLEX BIOLOGICAL
JRNL TITL 2 FUNCTIONS OF OCTAMERIC HUMAN UDP-GLUCOSE PYROPHOSPHORYLASE,
JRNL TITL 3 A KEY ENZYME IN CELL METABOLISM.
JRNL REF SCI REP V. 5 9618
JRNL REFN ESSN 2045-2322
JRNL PMID 25860585
JRNL DOI 10.1038/SREP09618
REMARK 2
REMARK 2 RESOLUTION. 3.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 3.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 50946
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2580
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 47.6279 - 8.7622 0.99 2887 133 0.2295 0.2330
REMARK 3 2 8.7622 - 6.9618 1.00 2740 167 0.2304 0.2490
REMARK 3 3 6.9618 - 6.0838 1.00 2751 136 0.2430 0.3648
REMARK 3 4 6.0838 - 5.5285 1.00 2726 125 0.1903 0.2253
REMARK 3 5 5.5285 - 5.1327 1.00 2687 148 0.1706 0.2320
REMARK 3 6 5.1327 - 4.8304 1.00 2699 145 0.1542 0.2069
REMARK 3 7 4.8304 - 4.5887 1.00 2676 138 0.1524 0.2056
REMARK 3 8 4.5887 - 4.3891 1.00 2689 140 0.1500 0.2181
REMARK 3 9 4.3891 - 4.2202 1.00 2630 161 0.1486 0.2260
REMARK 3 10 4.2202 - 4.0747 1.00 2652 163 0.1706 0.2067
REMARK 3 11 4.0747 - 3.9474 1.00 2660 136 0.1706 0.2799
REMARK 3 12 3.9474 - 3.8346 1.00 2683 130 0.1848 0.2541
REMARK 3 13 3.8346 - 3.7337 1.00 2672 124 0.2076 0.2284
REMARK 3 14 3.7337 - 3.6426 1.00 2612 159 0.2135 0.2656
REMARK 3 15 3.6426 - 3.5598 1.00 2656 141 0.2179 0.2906
REMARK 3 16 3.5598 - 3.4841 1.00 2643 159 0.2299 0.2991
REMARK 3 17 3.4841 - 3.4144 1.00 2666 135 0.2671 0.3087
REMARK 3 18 3.4144 - 3.3500 1.00 2637 140 0.2804 0.3415
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 96.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.008 15718
REMARK 3 ANGLE : 1.101 21248
REMARK 3 CHIRALITY : 0.042 2428
REMARK 3 PLANARITY : 0.006 2714
REMARK 3 DIHEDRAL : 16.348 5912
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 24 THROUGH 508)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9816 -23.0143 31.0992
REMARK 3 T TENSOR
REMARK 3 T11: 1.3017 T22: 1.0095
REMARK 3 T33: 0.4089 T12: 0.6193
REMARK 3 T13: 0.1773 T23: 0.1505
REMARK 3 L TENSOR
REMARK 3 L11: 1.4336 L22: 2.4501
REMARK 3 L33: 2.2142 L12: 0.6327
REMARK 3 L13: -0.5328 L23: -0.2041
REMARK 3 S TENSOR
REMARK 3 S11: 0.2606 S12: 0.1859 S13: 0.2441
REMARK 3 S21: -0.1454 S22: -0.1926 S23: -0.3170
REMARK 3 S31: -0.2938 S32: 0.4286 S33: 0.0385
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 24 THROUGH 508)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.2993 -93.9480 27.7658
REMARK 3 T TENSOR
REMARK 3 T11: 1.5382 T22: 1.0113
REMARK 3 T33: 0.6275 T12: 0.6163
REMARK 3 T13: 0.2380 T23: 0.1903
REMARK 3 L TENSOR
REMARK 3 L11: 1.1396 L22: 1.7929
REMARK 3 L33: 1.7256 L12: -0.3653
REMARK 3 L13: -0.2837 L23: 0.5103
REMARK 3 S TENSOR
REMARK 3 S11: 0.1361 S12: 0.4033 S13: 0.0333
REMARK 3 S21: -0.6717 S22: -0.2727 S23: -0.1070
REMARK 3 S31: -0.0632 S32: -0.1429 S33: 0.1979
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 24 THROUGH 508)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6736 -76.7400 11.3180
REMARK 3 T TENSOR
REMARK 3 T11: 1.1944 T22: 1.1929
REMARK 3 T33: 0.6850 T12: 0.4488
REMARK 3 T13: -0.0140 T23: -0.1277
REMARK 3 L TENSOR
REMARK 3 L11: 2.3030 L22: 1.6239
REMARK 3 L33: 4.1815 L12: -0.5124
REMARK 3 L13: 0.0229 L23: -0.0827
REMARK 3 S TENSOR
REMARK 3 S11: 0.1014 S12: 0.7922 S13: -0.0165
REMARK 3 S21: -0.3951 S22: -0.1194 S23: 0.3102
REMARK 3 S31: -0.3792 S32: -1.0061 S33: 0.0942
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 24 THROUGH 508)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.5088 -40.1776 47.6058
REMARK 3 T TENSOR
REMARK 3 T11: 1.3752 T22: 1.1418
REMARK 3 T33: 1.1083 T12: 0.1934
REMARK 3 T13: 0.2515 T23: 0.3120
REMARK 3 L TENSOR
REMARK 3 L11: 4.2572 L22: 1.8734
REMARK 3 L33: 2.9119 L12: -0.4473
REMARK 3 L13: -1.0949 L23: -0.3627
REMARK 3 S TENSOR
REMARK 3 S11: 0.0437 S12: 0.3199 S13: 0.5942
REMARK 3 S21: -0.4008 S22: -0.2299 S23: -0.9655
REMARK 3 S31: -0.1878 S32: 1.1757 S33: 0.1845
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 AUTHOR STATED THE FOLLOWING: IN THE CRYSTALS OF HUGP1-UDP-GLC
REMARK 3 COMPLEX THE ELECTRON DENSITY FOR THE SUBSTRATE (UPG) AS WELL AS
REMARK 3 FOR SOME OTHER PARTS OF THE STRUCTURE WAS OBSERVED TO BE RATHER
REMARK 3 WEAK. IT MAY IN PART BE EXPLAINED BY A CERTAIN DEGREE OF DISORDER
REMARK 3 WITHIN THE UNIT CELL, WHICH IS REFLECTED IN A HIGH VALUE OF THE
REMARK 3 WILSON B-FACTOR (108.6 A**2) AND A WEAKER ELECTRON DENSITY FOR THE
REMARK 3 PROTEIN CHAIN D. HOWEVER, THE PARTIAL ELECTRON DENSITY OBSERVED
REMARK 3 FOR THE UPG RIBOSE AND THE GLUCOSE MOIETIES INDICATED THAT THE
REMARK 3 SUBSTRATE IS PRESENT IN THE ACTIVE SITE OF PROTEIN CHAIN A. TO
REMARK 3 IMPROVE THE QUALITY OF THE ELECTRON DENSITY, ESPECIALLY IN ITS
REMARK 3 WEAK REGIONS, WE PERFORMED A PHASE IMPROVEMENT PROCEDURE USING THE
REMARK 3 DENSITY MODIFICATION (DM) METHODS IN THE FOLLOWING WAY. THE DM WAS
REMARK 3 PERFORMED IN A SOLVENT FLATTENING MODE USING HENDRICKSON-LATTMAN
REMARK 3 COEFFICIENTS FROM THE REFINED PROTEIN MODEL WITH OMITTED SUBSTRATE
REMARK 3 AND LIGANDS AS AN INITIAL APPROXIMATION. AFTER SEVERAL CYCLES OF
REMARK 3 THE DM, WE OBSERVED A NOTICEABLE INCREASE OF THE FIGURE-OF-MERIT
REMARK 3 (15% IN A HIGH-RESOLUTION SHELL). THE RESULTING WEIGHTED STRUCTURE
REMARK 3 FACTOR AND MODIFIED PHASES FROM DM PROCEDURE WERE USED TO
REMARK 3 CALCULATE THE COMPOSITE 2FO-FC ELECTRON DENSITY WHICH YOU CAN SEE
REMARK 3 ON THE FIGURE ATTACHED TO THIS MESSAGE. THE DM-IMPROVED LIGAND-
REMARK 3 OMIT MAP ALLOWED TO DETERMINE THE BINDING MODE OF UPG
REMARK 3 UNAMBIGUOUSLY. IN ADDITION TO THE UPG, THE DM MAP ALLOWED TO
REMARK 3 RESOLVE SEVERAL OTHER WEAK DENSITY REGIONS WHICH WERE NOT CLEARLY
REMARK 3 INTERPRETABLE BEFORE. THE DESCRIBED METHOD OF IMPROVEMENT OF THE
REMARK 3 WEAK ELECTRON DENSITY REGIONS HAS BEEN SUCCESSFULLY APPLIED TO
REMARK 3 RESOLVE THE DISORDERED PROTEIN REGIONS IN A PUBLICATION:
REMARK 3
REMARK 3 FEDOROV R, WITTE G, URBANKE C, MANSTEIN DJ, CURTH U. 3D STRUCTURE
REMARK 3 OF THERMUS AQUATICUS SINGLE-STRANDED DNA-BINDING PROTEIN GIVES
REMARK 3 INSIGHT INTO THE FUNCTIONING OF SSB PROTEINS. (2006) NUCLEIC ACIDS
REMARK 3 RES 34, 6708-6717.
REMARK 3
REMARK 3 AND IN A NUMBER OF APPLICATION NOTES OF OUR GROUP TOGETHER WITH
REMARK 3 BRUKER COMPANY. THE CONSIDERABLE INCREASE OF THE ELECTRON DENSITY
REMARK 3 QUALITY AND THE VALUE OF FIGURE-OF-MERIT IN THE PARTICULAR CASE OF
REMARK 3 HUGP1.UDP-GLC COMPLEX STRUCTURE CAN BE EXPLAINED BY A HIGH SOLVENT
REMARK 3 CONTENT IN THE HUGP1.UDP-GLC COMPLEX CRYSTALS (VS = 67.7%), WHICH
REMARK 3 MAKES THE PHASE IMPROVEMENT BY SOLVENT FLATTENING PROCEDURE VERY
REMARK 3 EFFICIENT.
REMARK 4
REMARK 4 4R7P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000087003.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-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 : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
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 : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58213
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.623
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 12.30
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN SAMPLE CONTAINED 10.3
REMARK 280 MG/ML OF HUGP, 50 MM HEPES PH 7.5, 5 MM MGCL2, 1 MM EDTA, 20% (W/
REMARK 280 V) SUCROSE AND 4 MM UDP-GLC. 1 L OF THE HUGP UDP-GLC COMPLEX WAS
REMARK 280 MIXED 1:1 WITH THE RESERVOIR SOLUTION CONTAINING 100 MM SODIUM
REMARK 280 ACETATE BUFFER PH 4.8, 520 MM ZINC ACETATE, 6% (W/V)
REMARK 280 AMINOCAPROIC ACID AND 75 MM AMMONIUM SULFATE. , VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 281.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 103.87333
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 207.74667
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 207.74667
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 103.87333
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 300 REMARK: TWO CYCLIC C4 TETRAMERS ARE STACKED ONTO EACH OTHER AND ARE
REMARK 300 RELATED BY TWOFOLD SYMMETRY AXES CREATING THE OCTAMERIC STRUCTURE
REMARK 300 WITH DIHEDRAL SYMMETRY D4
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 177790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -913.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 103.87333
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 ZN ZN B 610 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 MET A -17
REMARK 465 ALA A -16
REMARK 465 SER A -15
REMARK 465 TRP A -14
REMARK 465 SER A -13
REMARK 465 HIS A -12
REMARK 465 PRO A -11
REMARK 465 GLN A -10
REMARK 465 PHE A -9
REMARK 465 GLU A -8
REMARK 465 LYS A -7
REMARK 465 GLY A -6
REMARK 465 ALA A -5
REMARK 465 LEU A -4
REMARK 465 VAL A -3
REMARK 465 PRO A -2
REMARK 465 ARG A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 PHE A 4
REMARK 465 VAL A 5
REMARK 465 GLN A 6
REMARK 465 ASP A 7
REMARK 465 LEU A 8
REMARK 465 SER A 9
REMARK 465 LYS A 10
REMARK 465 ALA A 11
REMARK 465 MET A 12
REMARK 465 SER A 13
REMARK 465 GLN A 14
REMARK 465 ASP A 15
REMARK 465 GLY A 16
REMARK 465 ALA A 17
REMARK 465 SER A 18
REMARK 465 GLN A 19
REMARK 465 PHE A 20
REMARK 465 GLN A 21
REMARK 465 GLU A 22
REMARK 465 VAL A 23
REMARK 465 MET B -17
REMARK 465 ALA B -16
REMARK 465 SER B -15
REMARK 465 TRP B -14
REMARK 465 SER B -13
REMARK 465 HIS B -12
REMARK 465 PRO B -11
REMARK 465 GLN B -10
REMARK 465 PHE B -9
REMARK 465 GLU B -8
REMARK 465 LYS B -7
REMARK 465 GLY B -6
REMARK 465 ALA B -5
REMARK 465 LEU B -4
REMARK 465 VAL B -3
REMARK 465 PRO B -2
REMARK 465 ARG B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 PHE B 4
REMARK 465 VAL B 5
REMARK 465 GLN B 6
REMARK 465 ASP B 7
REMARK 465 LEU B 8
REMARK 465 SER B 9
REMARK 465 LYS B 10
REMARK 465 ALA B 11
REMARK 465 MET B 12
REMARK 465 SER B 13
REMARK 465 GLN B 14
REMARK 465 ASP B 15
REMARK 465 GLY B 16
REMARK 465 ALA B 17
REMARK 465 SER B 18
REMARK 465 GLN B 19
REMARK 465 PHE B 20
REMARK 465 GLN B 21
REMARK 465 GLU B 22
REMARK 465 VAL B 23
REMARK 465 MET C -17
REMARK 465 ALA C -16
REMARK 465 SER C -15
REMARK 465 TRP C -14
REMARK 465 SER C -13
REMARK 465 HIS C -12
REMARK 465 PRO C -11
REMARK 465 GLN C -10
REMARK 465 PHE C -9
REMARK 465 GLU C -8
REMARK 465 LYS C -7
REMARK 465 GLY C -6
REMARK 465 ALA C -5
REMARK 465 LEU C -4
REMARK 465 VAL C -3
REMARK 465 PRO C -2
REMARK 465 ARG C -1
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 SER C 2
REMARK 465 ARG C 3
REMARK 465 PHE C 4
REMARK 465 VAL C 5
REMARK 465 GLN C 6
REMARK 465 ASP C 7
REMARK 465 LEU C 8
REMARK 465 SER C 9
REMARK 465 LYS C 10
REMARK 465 ALA C 11
REMARK 465 MET C 12
REMARK 465 SER C 13
REMARK 465 GLN C 14
REMARK 465 ASP C 15
REMARK 465 GLY C 16
REMARK 465 ALA C 17
REMARK 465 SER C 18
REMARK 465 GLN C 19
REMARK 465 PHE C 20
REMARK 465 GLN C 21
REMARK 465 GLU C 22
REMARK 465 VAL C 23
REMARK 465 MET D -17
REMARK 465 ALA D -16
REMARK 465 SER D -15
REMARK 465 TRP D -14
REMARK 465 SER D -13
REMARK 465 HIS D -12
REMARK 465 PRO D -11
REMARK 465 GLN D -10
REMARK 465 PHE D -9
REMARK 465 GLU D -8
REMARK 465 LYS D -7
REMARK 465 GLY D -6
REMARK 465 ALA D -5
REMARK 465 LEU D -4
REMARK 465 VAL D -3
REMARK 465 PRO D -2
REMARK 465 ARG D -1
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 SER D 2
REMARK 465 ARG D 3
REMARK 465 PHE D 4
REMARK 465 VAL D 5
REMARK 465 GLN D 6
REMARK 465 ASP D 7
REMARK 465 LEU D 8
REMARK 465 SER D 9
REMARK 465 LYS D 10
REMARK 465 ALA D 11
REMARK 465 MET D 12
REMARK 465 SER D 13
REMARK 465 GLN D 14
REMARK 465 ASP D 15
REMARK 465 GLY D 16
REMARK 465 ALA D 17
REMARK 465 SER D 18
REMARK 465 GLN D 19
REMARK 465 PHE D 20
REMARK 465 GLN D 21
REMARK 465 GLU D 22
REMARK 465 VAL D 23
REMARK 465 LEU D 359
REMARK 465 ASP D 360
REMARK 465 GLY D 361
REMARK 465 GLY D 362
REMARK 465 LEU D 363
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 OE1 GLU C 216 OD2 ASP C 360 0.87
REMARK 500 OXT HIS C 508 O2 EDO C 605 1.25
REMARK 500 OD2 ASP A 170 O1 EDO A 611 1.27
REMARK 500 OD2 ASP B 99 O1 EDO B 605 1.43
REMARK 500 OE2 GLU B 47 ND1 HIS B 50 1.50
REMARK 500 CE LYS B 77 CZ PHE B 324 1.54
REMARK 500 OD1 ASP B 74 CD1 ILE B 78 1.61
REMARK 500 OE1 GLU C 216 CG ASP C 360 1.76
REMARK 500 CE LYS B 77 CE1 PHE B 324 1.84
REMARK 500 O VAL C 208 N GLY C 212 1.87
REMARK 500 O PHE C 48 OG1 THR C 51 1.95
REMARK 500 NZ LYS B 77 CZ PHE B 324 1.98
REMARK 500 CD GLU C 216 OD2 ASP C 360 2.00
REMARK 500 O SER D 128 OG1 THR D 137 2.00
REMARK 500 OD1 ASP A 56 NH1 ARG A 59 2.02
REMARK 500 OE2 GLU B 47 CG HIS B 50 2.03
REMARK 500 OE2 GLU D 147 SG CYS D 181 2.04
REMARK 500 OD2 ASP B 74 CD1 ILE B 78 2.06
REMARK 500 O PHE D 48 OG1 THR D 51 2.07
REMARK 500 CG ASP B 74 CD1 ILE B 78 2.07
REMARK 500 OG1 THR B 358 OD1 ASN B 364 2.08
REMARK 500 O THR A 167 OG1 THR A 171 2.10
REMARK 500 O ASN C 214 N TRP C 218 2.13
REMARK 500 O ALA D 205 ND2 ASN D 214 2.13
REMARK 500 NH2 ARG B 445 OD1 ASP B 463 2.15
REMARK 500 CE1 HIS C 314 OE1 GLU C 317 2.15
REMARK 500 NZ LYS D 151 O HOH D 705 2.15
REMARK 500 O GLY A 293 N ASN A 328 2.16
REMARK 500 OD2 ASP A 289 NH2 ARG A 389 2.16
REMARK 500 O GLY D 234 OG1 THR D 238 2.16
REMARK 500 NH1 ARG C 195 O THR C 215 2.17
REMARK 500 OG SER B 191 OD2 ASP B 225 2.17
REMARK 500 O GLY A 70 OG SER A 72 2.18
REMARK 500 O SER A 128 OG1 THR A 137 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS C 181 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 LEU D 267 CB - CG - CD2 ANGL. DEV. = -14.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 209 -165.37 -76.46
REMARK 500 PRO A 221 -72.69 -57.82
REMARK 500 ILE A 226 -33.94 -39.99
REMARK 500 ASN A 254 98.46 -68.22
REMARK 500 ASP A 456 -52.80 -131.58
REMARK 500 SER B 45 -11.45 86.70
REMARK 500 ASN B 100 76.06 52.75
REMARK 500 HIS B 223 -15.84 -143.63
REMARK 500 ILE B 226 -39.84 -35.38
REMARK 500 ASP B 289 45.69 -100.74
REMARK 500 LEU B 359 -155.51 -159.63
REMARK 500 SER B 461 -73.32 -105.10
REMARK 500 ASP C 84 4.63 83.65
REMARK 500 GLU C 135 -3.32 70.01
REMARK 500 HIS C 223 -17.03 -141.09
REMARK 500 ILE C 226 -37.60 -39.20
REMARK 500 ASP C 289 35.62 -94.31
REMARK 500 LYS C 312 -131.46 58.29
REMARK 500 HIS C 314 4.77 83.57
REMARK 500 LYS C 357 167.97 179.96
REMARK 500 LEU C 359 -65.80 -138.76
REMARK 500 SER D 45 -11.25 84.60
REMARK 500 SER D 72 -55.69 -128.89
REMARK 500 PRO D 82 -170.64 -69.99
REMARK 500 ASN D 100 -131.38 53.89
REMARK 500 THR D 155 -160.23 -129.40
REMARK 500 HIS D 180 -5.28 75.58
REMARK 500 ASP D 207 41.57 -149.67
REMARK 500 GLU D 213 -53.15 -123.24
REMARK 500 PRO D 425 -7.09 -59.08
REMARK 500 ASP D 456 -58.52 -121.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS B 77 ILE B 78 -53.87
REMARK 500 VAL C 208 SER C 209 -46.20
REMARK 500 SER C 209 TYR C 210 149.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 UPG A 601
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 ZN A 614 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 47 OE2
REMARK 620 2 HOH A 730 O 60.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 615 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 123 SG
REMARK 620 2 GLN A 440 NE2 129.6
REMARK 620 3 HOH A 727 O 57.3 84.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 608 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 170 OD2
REMARK 620 2 ASP B 170 OD1 60.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 609 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 179 OD1
REMARK 620 2 HIS B 180 NE2 114.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 609 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 87 NE2
REMARK 620 2 GLN C 87 OE1 60.1
REMARK 620 3 HIS C 266 NE2 140.5 104.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 607 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 147 OE1
REMARK 620 2 GLU C 147 OE2 64.0
REMARK 620 3 CYS C 181 SG 128.8 150.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 608 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 441 OD2
REMARK 620 2 ASP C 441 OD1 69.9
REMARK 620 3 HOH C 722 O 138.9 151.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 608 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 147 OE1
REMARK 620 2 GLU D 147 OE2 70.9
REMARK 620 3 CYS D 181 SG 104.3 56.0
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 UPG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 608
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R2W RELATED DB: PDB
REMARK 900 HUMAN UDP-GLUCOSE PYROPHOSPHORYLASE ISOFORM 2 IN APO-FORM
REMARK 900 RELATED ID: 3R3I RELATED DB: PDB
REMARK 900 C-TERMINAL TRUNCATION OF HUMAN UDP-GLUCOSE PYROPHOSPHORYLASE
REMARK 900 ISOFORM 2 IN APO-FORM
DBREF 4R7P A 2 508 UNP Q16851 UGPA_HUMAN 2 508
DBREF 4R7P B 2 508 UNP Q16851 UGPA_HUMAN 2 508
DBREF 4R7P C 2 508 UNP Q16851 UGPA_HUMAN 2 508
DBREF 4R7P D 2 508 UNP Q16851 UGPA_HUMAN 2 508
SEQADV 4R7P MET A -17 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ALA A -16 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER A -15 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P TRP A -14 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER A -13 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P HIS A -12 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PRO A -11 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLN A -10 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PHE A -9 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLU A -8 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P LYS A -7 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLY A -6 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ALA A -5 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P LEU A -4 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P VAL A -3 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PRO A -2 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ARG A -1 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLY A 0 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER A 1 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P MET B -17 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ALA B -16 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER B -15 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P TRP B -14 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER B -13 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P HIS B -12 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PRO B -11 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLN B -10 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PHE B -9 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLU B -8 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P LYS B -7 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLY B -6 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ALA B -5 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P LEU B -4 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P VAL B -3 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PRO B -2 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ARG B -1 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLY B 0 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER B 1 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P MET C -17 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ALA C -16 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER C -15 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P TRP C -14 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER C -13 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P HIS C -12 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PRO C -11 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLN C -10 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PHE C -9 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLU C -8 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P LYS C -7 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLY C -6 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ALA C -5 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P LEU C -4 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P VAL C -3 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PRO C -2 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ARG C -1 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLY C 0 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER C 1 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P MET D -17 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ALA D -16 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER D -15 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P TRP D -14 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER D -13 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P HIS D -12 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PRO D -11 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLN D -10 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PHE D -9 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLU D -8 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P LYS D -7 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLY D -6 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ALA D -5 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P LEU D -4 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P VAL D -3 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P PRO D -2 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P ARG D -1 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P GLY D 0 UNP Q16851 EXPRESSION TAG
SEQADV 4R7P SER D 1 UNP Q16851 EXPRESSION TAG
SEQRES 1 A 526 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 526 LEU VAL PRO ARG GLY SER SER ARG PHE VAL GLN ASP LEU
SEQRES 3 A 526 SER LYS ALA MET SER GLN ASP GLY ALA SER GLN PHE GLN
SEQRES 4 A 526 GLU VAL ILE ARG GLN GLU LEU GLU LEU SER VAL LYS LYS
SEQRES 5 A 526 GLU LEU GLU LYS ILE LEU THR THR ALA SER SER HIS GLU
SEQRES 6 A 526 PHE GLU HIS THR LYS LYS ASP LEU ASP GLY PHE ARG LYS
SEQRES 7 A 526 LEU PHE HIS ARG PHE LEU GLN GLU LYS GLY PRO SER VAL
SEQRES 8 A 526 ASP TRP GLY LYS ILE GLN ARG PRO PRO GLU ASP SER ILE
SEQRES 9 A 526 GLN PRO TYR GLU LYS ILE LYS ALA ARG GLY LEU PRO ASP
SEQRES 10 A 526 ASN ILE SER SER VAL LEU ASN LYS LEU VAL VAL VAL LYS
SEQRES 11 A 526 LEU ASN GLY GLY LEU GLY THR SER MET GLY CYS LYS GLY
SEQRES 12 A 526 PRO LYS SER LEU ILE GLY VAL ARG ASN GLU ASN THR PHE
SEQRES 13 A 526 LEU ASP LEU THR VAL GLN GLN ILE GLU HIS LEU ASN LYS
SEQRES 14 A 526 THR TYR ASN THR ASP VAL PRO LEU VAL LEU MET ASN SER
SEQRES 15 A 526 PHE ASN THR ASP GLU ASP THR LYS LYS ILE LEU GLN LYS
SEQRES 16 A 526 TYR ASN HIS CYS ARG VAL LYS ILE TYR THR PHE ASN GLN
SEQRES 17 A 526 SER ARG TYR PRO ARG ILE ASN LYS GLU SER LEU LEU PRO
SEQRES 18 A 526 VAL ALA LYS ASP VAL SER TYR SER GLY GLU ASN THR GLU
SEQRES 19 A 526 ALA TRP TYR PRO PRO GLY HIS GLY ASP ILE TYR ALA SER
SEQRES 20 A 526 PHE TYR ASN SER GLY LEU LEU ASP THR PHE ILE GLY GLU
SEQRES 21 A 526 GLY LYS GLU TYR ILE PHE VAL SER ASN ILE ASP ASN LEU
SEQRES 22 A 526 GLY ALA THR VAL ASP LEU TYR ILE LEU ASN HIS LEU MET
SEQRES 23 A 526 ASN PRO PRO ASN GLY LYS ARG CYS GLU PHE VAL MET GLU
SEQRES 24 A 526 VAL THR ASN LYS THR ARG ALA ASP VAL LYS GLY GLY THR
SEQRES 25 A 526 LEU THR GLN TYR GLU GLY LYS LEU ARG LEU VAL GLU ILE
SEQRES 26 A 526 ALA GLN VAL PRO LYS ALA HIS VAL ASP GLU PHE LYS SER
SEQRES 27 A 526 VAL SER LYS PHE LYS ILE PHE ASN THR ASN ASN LEU TRP
SEQRES 28 A 526 ILE SER LEU ALA ALA VAL LYS ARG LEU GLN GLU GLN ASN
SEQRES 29 A 526 ALA ILE ASP MET GLU ILE ILE VAL ASN ALA LYS THR LEU
SEQRES 30 A 526 ASP GLY GLY LEU ASN VAL ILE GLN LEU GLU THR ALA VAL
SEQRES 31 A 526 GLY ALA ALA ILE LYS SER PHE GLU ASN SER LEU GLY ILE
SEQRES 32 A 526 ASN VAL PRO ARG SER ARG PHE LEU PRO VAL LYS THR THR
SEQRES 33 A 526 SER ASP LEU LEU LEU VAL MET SER ASN LEU TYR SER LEU
SEQRES 34 A 526 ASN ALA GLY SER LEU THR MET SER GLU LYS ARG GLU PHE
SEQRES 35 A 526 PRO THR VAL PRO LEU VAL LYS LEU GLY SER SER PHE THR
SEQRES 36 A 526 LYS VAL GLN ASP TYR LEU ARG ARG PHE GLU SER ILE PRO
SEQRES 37 A 526 ASP MET LEU GLU LEU ASP HIS LEU THR VAL SER GLY ASP
SEQRES 38 A 526 VAL THR PHE GLY LYS ASN VAL SER LEU LYS GLY THR VAL
SEQRES 39 A 526 ILE ILE ILE ALA ASN HIS GLY ASP ARG ILE ASP ILE PRO
SEQRES 40 A 526 PRO GLY ALA VAL LEU GLU ASN LYS ILE VAL SER GLY ASN
SEQRES 41 A 526 LEU ARG ILE LEU ASP HIS
SEQRES 1 B 526 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 526 LEU VAL PRO ARG GLY SER SER ARG PHE VAL GLN ASP LEU
SEQRES 3 B 526 SER LYS ALA MET SER GLN ASP GLY ALA SER GLN PHE GLN
SEQRES 4 B 526 GLU VAL ILE ARG GLN GLU LEU GLU LEU SER VAL LYS LYS
SEQRES 5 B 526 GLU LEU GLU LYS ILE LEU THR THR ALA SER SER HIS GLU
SEQRES 6 B 526 PHE GLU HIS THR LYS LYS ASP LEU ASP GLY PHE ARG LYS
SEQRES 7 B 526 LEU PHE HIS ARG PHE LEU GLN GLU LYS GLY PRO SER VAL
SEQRES 8 B 526 ASP TRP GLY LYS ILE GLN ARG PRO PRO GLU ASP SER ILE
SEQRES 9 B 526 GLN PRO TYR GLU LYS ILE LYS ALA ARG GLY LEU PRO ASP
SEQRES 10 B 526 ASN ILE SER SER VAL LEU ASN LYS LEU VAL VAL VAL LYS
SEQRES 11 B 526 LEU ASN GLY GLY LEU GLY THR SER MET GLY CYS LYS GLY
SEQRES 12 B 526 PRO LYS SER LEU ILE GLY VAL ARG ASN GLU ASN THR PHE
SEQRES 13 B 526 LEU ASP LEU THR VAL GLN GLN ILE GLU HIS LEU ASN LYS
SEQRES 14 B 526 THR TYR ASN THR ASP VAL PRO LEU VAL LEU MET ASN SER
SEQRES 15 B 526 PHE ASN THR ASP GLU ASP THR LYS LYS ILE LEU GLN LYS
SEQRES 16 B 526 TYR ASN HIS CYS ARG VAL LYS ILE TYR THR PHE ASN GLN
SEQRES 17 B 526 SER ARG TYR PRO ARG ILE ASN LYS GLU SER LEU LEU PRO
SEQRES 18 B 526 VAL ALA LYS ASP VAL SER TYR SER GLY GLU ASN THR GLU
SEQRES 19 B 526 ALA TRP TYR PRO PRO GLY HIS GLY ASP ILE TYR ALA SER
SEQRES 20 B 526 PHE TYR ASN SER GLY LEU LEU ASP THR PHE ILE GLY GLU
SEQRES 21 B 526 GLY LYS GLU TYR ILE PHE VAL SER ASN ILE ASP ASN LEU
SEQRES 22 B 526 GLY ALA THR VAL ASP LEU TYR ILE LEU ASN HIS LEU MET
SEQRES 23 B 526 ASN PRO PRO ASN GLY LYS ARG CYS GLU PHE VAL MET GLU
SEQRES 24 B 526 VAL THR ASN LYS THR ARG ALA ASP VAL LYS GLY GLY THR
SEQRES 25 B 526 LEU THR GLN TYR GLU GLY LYS LEU ARG LEU VAL GLU ILE
SEQRES 26 B 526 ALA GLN VAL PRO LYS ALA HIS VAL ASP GLU PHE LYS SER
SEQRES 27 B 526 VAL SER LYS PHE LYS ILE PHE ASN THR ASN ASN LEU TRP
SEQRES 28 B 526 ILE SER LEU ALA ALA VAL LYS ARG LEU GLN GLU GLN ASN
SEQRES 29 B 526 ALA ILE ASP MET GLU ILE ILE VAL ASN ALA LYS THR LEU
SEQRES 30 B 526 ASP GLY GLY LEU ASN VAL ILE GLN LEU GLU THR ALA VAL
SEQRES 31 B 526 GLY ALA ALA ILE LYS SER PHE GLU ASN SER LEU GLY ILE
SEQRES 32 B 526 ASN VAL PRO ARG SER ARG PHE LEU PRO VAL LYS THR THR
SEQRES 33 B 526 SER ASP LEU LEU LEU VAL MET SER ASN LEU TYR SER LEU
SEQRES 34 B 526 ASN ALA GLY SER LEU THR MET SER GLU LYS ARG GLU PHE
SEQRES 35 B 526 PRO THR VAL PRO LEU VAL LYS LEU GLY SER SER PHE THR
SEQRES 36 B 526 LYS VAL GLN ASP TYR LEU ARG ARG PHE GLU SER ILE PRO
SEQRES 37 B 526 ASP MET LEU GLU LEU ASP HIS LEU THR VAL SER GLY ASP
SEQRES 38 B 526 VAL THR PHE GLY LYS ASN VAL SER LEU LYS GLY THR VAL
SEQRES 39 B 526 ILE ILE ILE ALA ASN HIS GLY ASP ARG ILE ASP ILE PRO
SEQRES 40 B 526 PRO GLY ALA VAL LEU GLU ASN LYS ILE VAL SER GLY ASN
SEQRES 41 B 526 LEU ARG ILE LEU ASP HIS
SEQRES 1 C 526 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 C 526 LEU VAL PRO ARG GLY SER SER ARG PHE VAL GLN ASP LEU
SEQRES 3 C 526 SER LYS ALA MET SER GLN ASP GLY ALA SER GLN PHE GLN
SEQRES 4 C 526 GLU VAL ILE ARG GLN GLU LEU GLU LEU SER VAL LYS LYS
SEQRES 5 C 526 GLU LEU GLU LYS ILE LEU THR THR ALA SER SER HIS GLU
SEQRES 6 C 526 PHE GLU HIS THR LYS LYS ASP LEU ASP GLY PHE ARG LYS
SEQRES 7 C 526 LEU PHE HIS ARG PHE LEU GLN GLU LYS GLY PRO SER VAL
SEQRES 8 C 526 ASP TRP GLY LYS ILE GLN ARG PRO PRO GLU ASP SER ILE
SEQRES 9 C 526 GLN PRO TYR GLU LYS ILE LYS ALA ARG GLY LEU PRO ASP
SEQRES 10 C 526 ASN ILE SER SER VAL LEU ASN LYS LEU VAL VAL VAL LYS
SEQRES 11 C 526 LEU ASN GLY GLY LEU GLY THR SER MET GLY CYS LYS GLY
SEQRES 12 C 526 PRO LYS SER LEU ILE GLY VAL ARG ASN GLU ASN THR PHE
SEQRES 13 C 526 LEU ASP LEU THR VAL GLN GLN ILE GLU HIS LEU ASN LYS
SEQRES 14 C 526 THR TYR ASN THR ASP VAL PRO LEU VAL LEU MET ASN SER
SEQRES 15 C 526 PHE ASN THR ASP GLU ASP THR LYS LYS ILE LEU GLN LYS
SEQRES 16 C 526 TYR ASN HIS CYS ARG VAL LYS ILE TYR THR PHE ASN GLN
SEQRES 17 C 526 SER ARG TYR PRO ARG ILE ASN LYS GLU SER LEU LEU PRO
SEQRES 18 C 526 VAL ALA LYS ASP VAL SER TYR SER GLY GLU ASN THR GLU
SEQRES 19 C 526 ALA TRP TYR PRO PRO GLY HIS GLY ASP ILE TYR ALA SER
SEQRES 20 C 526 PHE TYR ASN SER GLY LEU LEU ASP THR PHE ILE GLY GLU
SEQRES 21 C 526 GLY LYS GLU TYR ILE PHE VAL SER ASN ILE ASP ASN LEU
SEQRES 22 C 526 GLY ALA THR VAL ASP LEU TYR ILE LEU ASN HIS LEU MET
SEQRES 23 C 526 ASN PRO PRO ASN GLY LYS ARG CYS GLU PHE VAL MET GLU
SEQRES 24 C 526 VAL THR ASN LYS THR ARG ALA ASP VAL LYS GLY GLY THR
SEQRES 25 C 526 LEU THR GLN TYR GLU GLY LYS LEU ARG LEU VAL GLU ILE
SEQRES 26 C 526 ALA GLN VAL PRO LYS ALA HIS VAL ASP GLU PHE LYS SER
SEQRES 27 C 526 VAL SER LYS PHE LYS ILE PHE ASN THR ASN ASN LEU TRP
SEQRES 28 C 526 ILE SER LEU ALA ALA VAL LYS ARG LEU GLN GLU GLN ASN
SEQRES 29 C 526 ALA ILE ASP MET GLU ILE ILE VAL ASN ALA LYS THR LEU
SEQRES 30 C 526 ASP GLY GLY LEU ASN VAL ILE GLN LEU GLU THR ALA VAL
SEQRES 31 C 526 GLY ALA ALA ILE LYS SER PHE GLU ASN SER LEU GLY ILE
SEQRES 32 C 526 ASN VAL PRO ARG SER ARG PHE LEU PRO VAL LYS THR THR
SEQRES 33 C 526 SER ASP LEU LEU LEU VAL MET SER ASN LEU TYR SER LEU
SEQRES 34 C 526 ASN ALA GLY SER LEU THR MET SER GLU LYS ARG GLU PHE
SEQRES 35 C 526 PRO THR VAL PRO LEU VAL LYS LEU GLY SER SER PHE THR
SEQRES 36 C 526 LYS VAL GLN ASP TYR LEU ARG ARG PHE GLU SER ILE PRO
SEQRES 37 C 526 ASP MET LEU GLU LEU ASP HIS LEU THR VAL SER GLY ASP
SEQRES 38 C 526 VAL THR PHE GLY LYS ASN VAL SER LEU LYS GLY THR VAL
SEQRES 39 C 526 ILE ILE ILE ALA ASN HIS GLY ASP ARG ILE ASP ILE PRO
SEQRES 40 C 526 PRO GLY ALA VAL LEU GLU ASN LYS ILE VAL SER GLY ASN
SEQRES 41 C 526 LEU ARG ILE LEU ASP HIS
SEQRES 1 D 526 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 D 526 LEU VAL PRO ARG GLY SER SER ARG PHE VAL GLN ASP LEU
SEQRES 3 D 526 SER LYS ALA MET SER GLN ASP GLY ALA SER GLN PHE GLN
SEQRES 4 D 526 GLU VAL ILE ARG GLN GLU LEU GLU LEU SER VAL LYS LYS
SEQRES 5 D 526 GLU LEU GLU LYS ILE LEU THR THR ALA SER SER HIS GLU
SEQRES 6 D 526 PHE GLU HIS THR LYS LYS ASP LEU ASP GLY PHE ARG LYS
SEQRES 7 D 526 LEU PHE HIS ARG PHE LEU GLN GLU LYS GLY PRO SER VAL
SEQRES 8 D 526 ASP TRP GLY LYS ILE GLN ARG PRO PRO GLU ASP SER ILE
SEQRES 9 D 526 GLN PRO TYR GLU LYS ILE LYS ALA ARG GLY LEU PRO ASP
SEQRES 10 D 526 ASN ILE SER SER VAL LEU ASN LYS LEU VAL VAL VAL LYS
SEQRES 11 D 526 LEU ASN GLY GLY LEU GLY THR SER MET GLY CYS LYS GLY
SEQRES 12 D 526 PRO LYS SER LEU ILE GLY VAL ARG ASN GLU ASN THR PHE
SEQRES 13 D 526 LEU ASP LEU THR VAL GLN GLN ILE GLU HIS LEU ASN LYS
SEQRES 14 D 526 THR TYR ASN THR ASP VAL PRO LEU VAL LEU MET ASN SER
SEQRES 15 D 526 PHE ASN THR ASP GLU ASP THR LYS LYS ILE LEU GLN LYS
SEQRES 16 D 526 TYR ASN HIS CYS ARG VAL LYS ILE TYR THR PHE ASN GLN
SEQRES 17 D 526 SER ARG TYR PRO ARG ILE ASN LYS GLU SER LEU LEU PRO
SEQRES 18 D 526 VAL ALA LYS ASP VAL SER TYR SER GLY GLU ASN THR GLU
SEQRES 19 D 526 ALA TRP TYR PRO PRO GLY HIS GLY ASP ILE TYR ALA SER
SEQRES 20 D 526 PHE TYR ASN SER GLY LEU LEU ASP THR PHE ILE GLY GLU
SEQRES 21 D 526 GLY LYS GLU TYR ILE PHE VAL SER ASN ILE ASP ASN LEU
SEQRES 22 D 526 GLY ALA THR VAL ASP LEU TYR ILE LEU ASN HIS LEU MET
SEQRES 23 D 526 ASN PRO PRO ASN GLY LYS ARG CYS GLU PHE VAL MET GLU
SEQRES 24 D 526 VAL THR ASN LYS THR ARG ALA ASP VAL LYS GLY GLY THR
SEQRES 25 D 526 LEU THR GLN TYR GLU GLY LYS LEU ARG LEU VAL GLU ILE
SEQRES 26 D 526 ALA GLN VAL PRO LYS ALA HIS VAL ASP GLU PHE LYS SER
SEQRES 27 D 526 VAL SER LYS PHE LYS ILE PHE ASN THR ASN ASN LEU TRP
SEQRES 28 D 526 ILE SER LEU ALA ALA VAL LYS ARG LEU GLN GLU GLN ASN
SEQRES 29 D 526 ALA ILE ASP MET GLU ILE ILE VAL ASN ALA LYS THR LEU
SEQRES 30 D 526 ASP GLY GLY LEU ASN VAL ILE GLN LEU GLU THR ALA VAL
SEQRES 31 D 526 GLY ALA ALA ILE LYS SER PHE GLU ASN SER LEU GLY ILE
SEQRES 32 D 526 ASN VAL PRO ARG SER ARG PHE LEU PRO VAL LYS THR THR
SEQRES 33 D 526 SER ASP LEU LEU LEU VAL MET SER ASN LEU TYR SER LEU
SEQRES 34 D 526 ASN ALA GLY SER LEU THR MET SER GLU LYS ARG GLU PHE
SEQRES 35 D 526 PRO THR VAL PRO LEU VAL LYS LEU GLY SER SER PHE THR
SEQRES 36 D 526 LYS VAL GLN ASP TYR LEU ARG ARG PHE GLU SER ILE PRO
SEQRES 37 D 526 ASP MET LEU GLU LEU ASP HIS LEU THR VAL SER GLY ASP
SEQRES 38 D 526 VAL THR PHE GLY LYS ASN VAL SER LEU LYS GLY THR VAL
SEQRES 39 D 526 ILE ILE ILE ALA ASN HIS GLY ASP ARG ILE ASP ILE PRO
SEQRES 40 D 526 PRO GLY ALA VAL LEU GLU ASN LYS ILE VAL SER GLY ASN
SEQRES 41 D 526 LEU ARG ILE LEU ASP HIS
HET UPG A 601 36
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 605 5
HET SO4 A 606 5
HET SO4 A 607 5
HET SO4 A 608 5
HET ACT A 609 4
HET EDO A 610 4
HET EDO A 611 4
HET EDO A 612 4
HET EDO A 613 4
HET ZN A 614 1
HET ZN A 615 1
HET SO4 B 601 5
HET SO4 B 602 5
HET EDO B 603 4
HET EDO B 604 4
HET EDO B 605 4
HET EDO B 606 4
HET EDO B 607 4
HET ZN B 608 1
HET ZN B 609 1
HET ZN B 610 1
HET SO4 C 601 5
HET SO4 C 602 5
HET SO4 C 603 5
HET ACT C 604 4
HET EDO C 605 4
HET ZN C 606 1
HET ZN C 607 1
HET ZN C 608 1
HET ZN C 609 1
HET SO4 D 601 5
HET SO4 D 602 5
HET SO4 D 603 5
HET ACT D 604 4
HET ACT D 605 4
HET EDO D 606 4
HET ZN D 607 1
HET ZN D 608 1
HETNAM UPG URIDINE-5'-DIPHOSPHATE-GLUCOSE
HETNAM SO4 SULFATE ION
HETNAM ACT ACETATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ZN ZINC ION
HETSYN UPG URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE
HETSYN 2 UPG ESTER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 UPG C15 H24 N2 O17 P2
FORMUL 6 SO4 15(O4 S 2-)
FORMUL 13 ACT 4(C2 H3 O2 1-)
FORMUL 14 EDO 11(C2 H6 O2)
FORMUL 18 ZN 11(ZN 2+)
FORMUL 47 HOH *117(H2 O)
HELIX 1 1 ILE A 24 THR A 42 1 19
HELIX 2 2 SER A 44 GLU A 47 5 4
HELIX 3 3 PHE A 48 LEU A 66 1 19
HELIX 4 4 ASP A 74 GLY A 76 5 3
HELIX 5 5 TYR A 89 GLY A 96 1 8
HELIX 6 6 ASN A 100 ASN A 106 1 7
HELIX 7 7 PRO A 126 LEU A 129 5 4
HELIX 8 8 PHE A 138 ASN A 154 1 17
HELIX 9 9 THR A 167 LYS A 173 1 7
HELIX 10 10 ILE A 174 ASN A 179 5 6
HELIX 11 11 SER A 209 GLU A 213 5 5
HELIX 12 12 ASN A 214 GLU A 216 5 3
HELIX 13 13 ASP A 225 SER A 233 1 9
HELIX 14 14 GLY A 234 GLU A 242 1 9
HELIX 15 15 ASP A 260 ASN A 269 1 10
HELIX 16 16 PRO A 270 LYS A 274 5 5
HELIX 17 17 GLU A 306 VAL A 310 5 5
HELIX 18 18 HIS A 314 SER A 320 1 7
HELIX 19 19 LEU A 336 GLN A 345 1 10
HELIX 20 20 ALA A 371 PHE A 379 5 9
HELIX 21 21 PRO A 388 PHE A 392 5 5
HELIX 22 22 THR A 397 SER A 406 1 10
HELIX 23 23 SER A 434 THR A 437 5 4
HELIX 24 24 LYS A 438 PHE A 446 1 9
HELIX 25 25 GLN B 26 THR B 41 1 16
HELIX 26 26 GLU B 47 GLU B 68 1 22
HELIX 27 27 TYR B 89 ARG B 95 1 7
HELIX 28 28 ASN B 100 ASN B 106 1 7
HELIX 29 29 PRO B 126 LEU B 129 5 4
HELIX 30 30 PHE B 138 ASN B 154 1 17
HELIX 31 31 THR B 167 LEU B 175 1 9
HELIX 32 32 GLN B 176 HIS B 180 5 5
HELIX 33 33 ASN B 214 GLU B 216 5 3
HELIX 34 34 GLY B 224 SER B 233 1 10
HELIX 35 35 GLY B 234 GLY B 243 1 10
HELIX 36 36 ASP B 260 ASN B 269 1 10
HELIX 37 37 PRO B 270 LYS B 274 5 5
HELIX 38 38 GLU B 306 VAL B 310 5 5
HELIX 39 39 HIS B 314 SER B 320 1 7
HELIX 40 40 LEU B 336 ASN B 346 1 11
HELIX 41 41 VAL B 372 PHE B 379 5 8
HELIX 42 42 PRO B 388 PHE B 392 5 5
HELIX 43 43 THR B 397 SER B 406 1 10
HELIX 44 44 SER B 434 THR B 437 5 4
HELIX 45 45 LYS B 438 PHE B 446 1 9
HELIX 46 46 ARG C 25 THR C 41 1 17
HELIX 47 47 GLU C 47 GLU C 68 1 22
HELIX 48 48 TYR C 89 ALA C 94 1 6
HELIX 49 49 ASN C 100 LYS C 107 1 8
HELIX 50 50 PRO C 126 LEU C 129 5 4
HELIX 51 51 PHE C 138 ASN C 154 1 17
HELIX 52 52 THR C 167 LEU C 175 1 9
HELIX 53 53 GLN C 176 HIS C 180 5 5
HELIX 54 54 GLU C 213 ALA C 217 1 5
HELIX 55 55 ASP C 225 SER C 233 1 9
HELIX 56 56 GLY C 234 GLY C 243 1 10
HELIX 57 57 ASP C 260 ASN C 269 1 10
HELIX 58 58 PRO C 270 LYS C 274 5 5
HELIX 59 59 ARG C 287 LYS C 291 5 5
HELIX 60 60 GLU C 306 VAL C 310 5 5
HELIX 61 61 HIS C 314 SER C 320 1 7
HELIX 62 62 LEU C 336 GLU C 344 1 9
HELIX 63 63 ALA C 371 PHE C 379 5 9
HELIX 64 64 PRO C 388 PHE C 392 5 5
HELIX 65 65 THR C 397 SER C 406 1 10
HELIX 66 66 SER C 434 THR C 437 5 4
HELIX 67 67 LYS C 438 ARG C 445 1 8
HELIX 68 68 ARG D 25 THR D 41 1 17
HELIX 69 69 PHE D 48 LEU D 66 1 19
HELIX 70 70 TYR D 89 ARG D 95 1 7
HELIX 71 71 ILE D 101 ASN D 106 5 6
HELIX 72 72 PHE D 138 ASN D 154 1 17
HELIX 73 73 THR D 167 LYS D 173 1 7
HELIX 74 74 ILE D 174 ASN D 179 5 6
HELIX 75 75 GLU D 213 GLU D 216 5 4
HELIX 76 76 ASP D 225 ASN D 232 1 8
HELIX 77 77 GLY D 234 GLU D 242 1 9
HELIX 78 78 ASP D 260 HIS D 266 1 7
HELIX 79 79 PRO D 270 LYS D 274 5 5
HELIX 80 80 THR D 286 VAL D 290 5 5
HELIX 81 81 HIS D 314 SER D 320 1 7
HELIX 82 82 LEU D 336 ASN D 346 1 11
HELIX 83 83 VAL D 372 PHE D 379 5 8
HELIX 84 84 PRO D 388 PHE D 392 5 5
HELIX 85 85 THR D 397 SER D 406 1 10
HELIX 86 86 SER D 434 THR D 437 5 4
HELIX 87 87 LYS D 438 PHE D 446 1 9
SHEET 1 A 3 ILE A 78 GLN A 79 0
SHEET 2 A 3 THR A 294 TYR A 298 -1 O GLN A 297 N GLN A 79
SHEET 3 A 3 LYS A 301 VAL A 305 -1 O LYS A 301 N TYR A 298
SHEET 1 B 8 ILE A 86 PRO A 88 0
SHEET 2 B 8 LEU A 383 ASN A 386 1 O ASN A 386 N GLN A 87
SHEET 3 B 8 PHE A 278 ASN A 284 1 N PHE A 278 O LEU A 383
SHEET 4 B 8 ILE A 326 SER A 335 -1 O TRP A 333 N VAL A 279
SHEET 5 B 8 TYR A 246 ASN A 251 -1 N ILE A 247 O ILE A 334
SHEET 6 B 8 LEU A 108 ASN A 114 1 N VAL A 111 O PHE A 248
SHEET 7 B 8 PRO A 158 ASN A 163 1 O VAL A 160 N LYS A 112
SHEET 8 B 8 LYS A 184 ASN A 189 1 O TYR A 186 N LEU A 159
SHEET 1 C 2 GLY A 131 ARG A 133 0
SHEET 2 C 2 ASN A 136 THR A 137 -1 O ASN A 136 N VAL A 132
SHEET 1 D 2 TYR A 193 PRO A 194 0
SHEET 2 D 2 TRP A 218 TYR A 219 -1 O TYR A 219 N TYR A 193
SHEET 1 E 3 ILE A 196 ASN A 197 0
SHEET 2 E 3 LEU A 363 GLU A 369 -1 O ILE A 366 N ILE A 196
SHEET 3 E 3 ILE A 353 LEU A 359 -1 N ILE A 353 O GLU A 369
SHEET 1 F 2 TYR A 409 ASN A 412 0
SHEET 2 F 2 SER A 415 MET A 418 -1 O THR A 417 N SER A 410
SHEET 1 G 4 LEU A 429 LEU A 432 0
SHEET 2 G 4 LEU A 455 VAL A 460 1 O VAL A 460 N LYS A 431
SHEET 3 G 4 SER A 471 ALA A 480 1 O GLY A 474 N HIS A 457
SHEET 4 G 4 VAL A 493 GLU A 495 1 O LEU A 494 N LYS A 473
SHEET 1 H 4 LEU A 429 LEU A 432 0
SHEET 2 H 4 LEU A 455 VAL A 460 1 O VAL A 460 N LYS A 431
SHEET 3 H 4 SER A 471 ALA A 480 1 O GLY A 474 N HIS A 457
SHEET 4 H 4 ILE A 498 GLY A 501 1 O VAL A 499 N ILE A 479
SHEET 1 I 2 ASP A 463 PHE A 466 0
SHEET 2 I 2 ARG A 485 ILE A 488 1 O ILE A 486 N ASP A 463
SHEET 1 J 8 ILE B 86 PRO B 88 0
SHEET 2 J 8 LEU B 383 ASN B 386 1 O ASN B 386 N GLN B 87
SHEET 3 J 8 PHE B 278 ASN B 284 1 N PHE B 278 O LEU B 383
SHEET 4 J 8 ILE B 326 SER B 335 -1 O PHE B 327 N THR B 283
SHEET 5 J 8 TYR B 246 ASN B 251 -1 N ILE B 247 O ILE B 334
SHEET 6 J 8 LEU B 108 ASN B 114 1 N LEU B 113 O SER B 250
SHEET 7 J 8 LEU B 159 ASN B 163 1 O VAL B 160 N VAL B 110
SHEET 8 J 8 ILE B 185 ASN B 189 1 O TYR B 186 N LEU B 159
SHEET 1 K 2 GLY B 131 ARG B 133 0
SHEET 2 K 2 ASN B 136 THR B 137 -1 O ASN B 136 N VAL B 132
SHEET 1 L 2 TYR B 193 PRO B 194 0
SHEET 2 L 2 TRP B 218 TYR B 219 -1 O TYR B 219 N TYR B 193
SHEET 1 M 3 ILE B 196 ASN B 197 0
SHEET 2 M 3 LEU B 363 GLU B 369 -1 O ILE B 366 N ILE B 196
SHEET 3 M 3 ILE B 353 LEU B 359 -1 N LYS B 357 O VAL B 365
SHEET 1 N 2 THR B 294 TYR B 298 0
SHEET 2 N 2 LYS B 301 VAL B 305 -1 O ARG B 303 N THR B 296
SHEET 1 O 2 TYR B 409 ASN B 412 0
SHEET 2 O 2 SER B 415 MET B 418 -1 O THR B 417 N SER B 410
SHEET 1 P 4 LEU B 429 LEU B 432 0
SHEET 2 P 4 ASP B 451 VAL B 460 1 O ASP B 456 N LEU B 429
SHEET 3 P 4 SER B 471 ALA B 480 1 O GLY B 474 N HIS B 457
SHEET 4 P 4 VAL B 493 GLY B 501 1 O LEU B 494 N LYS B 473
SHEET 1 Q 2 ASP B 463 PHE B 466 0
SHEET 2 Q 2 ARG B 485 ILE B 488 1 O ILE B 488 N THR B 465
SHEET 1 R 3 ILE C 78 GLN C 79 0
SHEET 2 R 3 THR C 294 TYR C 298 -1 O GLN C 297 N GLN C 79
SHEET 3 R 3 LYS C 301 VAL C 305 -1 O VAL C 305 N THR C 294
SHEET 1 S 8 ILE C 86 PRO C 88 0
SHEET 2 S 8 GLY C 384 ASN C 386 1 O ASN C 386 N GLN C 87
SHEET 3 S 8 PHE C 278 ASN C 284 1 N VAL C 282 O ILE C 385
SHEET 4 S 8 ILE C 326 SER C 335 -1 O PHE C 327 N THR C 283
SHEET 5 S 8 TYR C 246 ASN C 251 -1 N ILE C 247 O ILE C 334
SHEET 6 S 8 LEU C 108 LEU C 113 1 N VAL C 111 O PHE C 248
SHEET 7 S 8 PRO C 158 ASN C 163 1 O VAL C 160 N VAL C 110
SHEET 8 S 8 LYS C 184 ASN C 189 1 O TYR C 186 N LEU C 159
SHEET 1 T 2 GLY C 131 ARG C 133 0
SHEET 2 T 2 ASN C 136 THR C 137 -1 O ASN C 136 N VAL C 132
SHEET 1 U 2 TYR C 193 PRO C 194 0
SHEET 2 U 2 TRP C 218 TYR C 219 -1 O TYR C 219 N TYR C 193
SHEET 1 V 3 ILE C 196 ASN C 197 0
SHEET 2 V 3 VAL C 365 GLU C 369 -1 O ILE C 366 N ILE C 196
SHEET 3 V 3 ILE C 353 LYS C 357 -1 N ILE C 353 O GLU C 369
SHEET 1 W 2 TYR C 409 ASN C 412 0
SHEET 2 W 2 SER C 415 MET C 418 -1 O THR C 417 N SER C 410
SHEET 1 X 4 LEU C 429 LEU C 432 0
SHEET 2 X 4 LEU C 455 SER C 461 1 O ASP C 456 N LEU C 429
SHEET 3 X 4 SER C 471 ILE C 479 1 O VAL C 476 N THR C 459
SHEET 4 X 4 VAL C 493 SER C 500 1 O LEU C 494 N SER C 471
SHEET 1 Y 2 ASP C 463 PHE C 466 0
SHEET 2 Y 2 ARG C 485 ILE C 488 1 O ILE C 488 N THR C 465
SHEET 1 Z 8 ILE D 86 PRO D 88 0
SHEET 2 Z 8 LEU D 383 ASN D 386 1 O ASN D 386 N GLN D 87
SHEET 3 Z 8 PHE D 278 ASN D 284 1 N VAL D 282 O ILE D 385
SHEET 4 Z 8 ILE D 326 SER D 335 -1 O TRP D 333 N VAL D 279
SHEET 5 Z 8 TYR D 246 ASN D 251 -1 N ILE D 247 O ILE D 334
SHEET 6 Z 8 LEU D 108 ASN D 114 1 N VAL D 111 O PHE D 248
SHEET 7 Z 8 PRO D 158 ASN D 163 1 O VAL D 160 N LYS D 112
SHEET 8 Z 8 LYS D 184 ASN D 189 1 O TYR D 186 N LEU D 161
SHEET 1 AA 2 GLY D 131 ARG D 133 0
SHEET 2 AA 2 ASN D 136 THR D 137 -1 O ASN D 136 N ARG D 133
SHEET 1 AB 2 TYR D 193 PRO D 194 0
SHEET 2 AB 2 TRP D 218 TYR D 219 -1 O TYR D 219 N TYR D 193
SHEET 1 AC 3 ILE D 196 ASN D 197 0
SHEET 2 AC 3 VAL D 365 THR D 370 -1 O ILE D 366 N ILE D 196
SHEET 3 AC 3 ILE D 352 ALA D 356 -1 N ASN D 355 O GLN D 367
SHEET 1 AD 2 THR D 294 TYR D 298 0
SHEET 2 AD 2 LYS D 301 VAL D 305 -1 O VAL D 305 N THR D 294
SHEET 1 AE 2 TYR D 409 ASN D 412 0
SHEET 2 AE 2 SER D 415 MET D 418 -1 O THR D 417 N SER D 410
SHEET 1 AF 4 LEU D 429 LEU D 432 0
SHEET 2 AF 4 ASP D 451 SER D 461 1 O ASP D 456 N LEU D 429
SHEET 3 AF 4 SER D 471 ILE D 479 1 O GLY D 474 N GLU D 454
SHEET 4 AF 4 VAL D 493 SER D 500 1 O VAL D 499 N ILE D 477
SHEET 1 AG 2 ASP D 463 PHE D 466 0
SHEET 2 AG 2 ARG D 485 ILE D 488 1 O ILE D 488 N THR D 465
LINK OE2 GLU A 47 ZN ZN A 614 1555 1555 2.24
LINK SG CYS A 123 ZN ZN A 615 1555 1555 2.77
LINK NE2 GLN A 440 ZN ZN A 615 1555 1555 2.08
LINK ZN ZN A 614 O HOH A 730 1555 1555 2.17
LINK ZN ZN A 615 O HOH A 727 1555 1555 2.21
LINK OD2 ASP B 170 ZN ZN B 608 1555 1555 1.99
LINK OD1 ASP B 170 ZN ZN B 608 1555 1555 2.32
LINK OD1 ASN B 179 ZN ZN B 609 1555 1555 2.00
LINK NE2 HIS B 180 ZN ZN B 609 1555 1555 1.98
LINK ND1 HIS B 457 ZN ZN B 610 1555 1555 2.01
LINK NE2 GLN C 87 ZN ZN C 609 1555 1555 1.73
LINK OE1 GLN C 87 ZN ZN C 609 1555 1555 2.53
LINK OE1 GLU C 147 ZN ZN C 607 1555 1555 1.94
LINK OE2 GLU C 147 ZN ZN C 607 1555 1555 2.12
LINK SG CYS C 181 ZN ZN C 607 1555 1555 2.03
LINK NE2 HIS C 266 ZN ZN C 609 1555 1555 1.77
LINK OD2 ASP C 441 ZN ZN C 608 1555 1555 2.00
LINK OD1 ASP C 441 ZN ZN C 608 1555 1555 2.01
LINK ZN ZN C 608 O HOH C 722 1555 1555 2.13
LINK OE1 GLU D 147 ZN ZN D 608 1555 1555 1.92
LINK OE2 GLU D 147 ZN ZN D 608 1555 1555 1.94
LINK SG CYS D 181 ZN ZN D 608 1555 1555 2.34
LINK ZN ZN D 607 O HOH D 721 1555 1555 2.36
SITE 1 AC1 11 LEU A 113 ASN A 114 GLY A 115 GLY A 116
SITE 2 AC1 11 GLN A 190 HIS A 223 ASN A 251 ASP A 253
SITE 3 AC1 11 LYS A 291 ASN A 328 ASN A 330
SITE 1 AC2 3 GLU A 27 ASN D 179 HIS D 180
SITE 1 AC3 1 HIS A 482
SITE 1 AC4 1 HIS A 148
SITE 1 AC5 1 HIS A 180
SITE 1 AC6 2 TRP A 75 HIS A 314
SITE 1 AC7 2 GLU A 245 MET A 268
SITE 1 AC8 2 LYS A 438 ASP A 441
SITE 1 AC9 3 GLY A 433 SER A 434 SER A 461
SITE 1 BC1 3 LYS A 319 LYS A 473 GLU A 495
SITE 1 BC2 3 ASN A 166 ASP A 170 HOH A 717
SITE 1 BC3 2 GLN A 87 HIS A 266
SITE 1 BC4 1 LYS D 77
SITE 1 BC5 2 GLU A 47 HOH A 730
SITE 1 BC6 3 CYS A 123 GLN A 440 HOH A 727
SITE 1 BC7 2 HIS B 148 THR B 152
SITE 1 BC8 2 GLU B 29 HIS B 63
SITE 1 BC9 4 LYS B 319 GLU B 454 LYS B 473 GLU B 495
SITE 1 CC1 3 CYS B 123 LYS B 124 GLN B 440
SITE 1 CC2 3 LYS A 274 ASN A 381 ASP B 99
SITE 1 CC3 2 ASP B 507 LYS C 497
SITE 1 CC4 3 ARG B 444 ARG B 445 THR B 465
SITE 1 CC5 1 ASP B 170
SITE 1 CC6 2 ASN B 179 HIS B 180
SITE 1 CC7 1 HIS B 457
SITE 1 CC8 2 HIS C 148 THR C 152
SITE 1 CC9 3 GLU B 27 LEU B 28 HIS C 180
SITE 1 DC1 2 GLU C 447 ASP C 507
SITE 1 DC2 1 HIS C 482
SITE 1 DC3 2 LYS B 431 HIS C 508
SITE 1 DC4 2 GLY C 222 HIS C 223
SITE 1 DC5 2 GLU C 147 CYS C 181
SITE 1 DC6 2 ASP C 441 HOH C 722
SITE 1 DC7 2 GLN C 87 HIS C 266
SITE 1 DC8 3 HIS D 148 THR D 152 HOH D 706
SITE 1 DC9 3 ASN A 502 ASP D 484 ASN D 502
SITE 1 EC1 3 LEU D 443 ARG D 444 PHE D 446
SITE 1 EC2 2 GLY B 483 HIS D 482
SITE 1 EC3 2 GLU D 454 GLU D 495
SITE 1 EC4 3 LYS D 438 ASP D 441 HOH D 730
SITE 1 EC5 1 HOH D 721
SITE 1 EC6 2 GLU D 147 CYS D 181
CRYST1 138.970 138.970 311.620 90.00 90.00 120.00 P 31 2 1 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 0.007196 0.004154 0.000000 0.00000
SCALE2 0.000000 0.008309 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003209 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
