HEADER TRANSFERASE 10-JUN-15 5BY6
TITLE CRYSTAL STRUCTURE OF TRICHINELLA SPIRALIS THYMIDYLATE SYNTHASE
TITLE 2 COMPLEXED WITH DUMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.1.1.45;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRICHINELLA SPIRALIS;
SOURCE 3 ORGANISM_COMMON: TRICHINA WORM;
SOURCE 4 ORGANISM_TAXID: 6334;
SOURCE 5 GENE: TS, TSP_03568;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TX61-;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A(+)::ST
KEYWDS TRICHINELLA SPIRALIS, PARASITIC NEMATODE, PROTEIN-LIGAND COMPLEX,
KEYWDS 2 METHYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DOWIERCIAL,A.JARMULA,W.RYPNIEWSKI,T.FRACZYK,P.WILK,W.RODE
REVDAT 3 10-JAN-24 5BY6 1 REMARK
REVDAT 2 06-DEC-17 5BY6 1 JRNL
REVDAT 1 17-JUN-15 5BY6 0
SPRSDE 17-JUN-15 5BY6 4G9U
JRNL AUTH A.JARMULA,P.WILK,P.MAJ,J.LUDWICZAK,A.DOWIERCIAL,K.BANASZAK,
JRNL AUTH 2 W.RYPNIEWSKI,J.CIESLA,M.DABROWSKA,T.FRACZYK,A.K.BRONOWSKA,
JRNL AUTH 3 J.JAKOWIECKI,S.FILIPEK,W.RODE
JRNL TITL CRYSTAL STRUCTURES OF NEMATODE (PARASITIC T. SPIRALIS AND
JRNL TITL 2 FREE LIVING C. ELEGANS), COMPARED TO MAMMALIAN, THYMIDYLATE
JRNL TITL 3 SYNTHASES (TS). MOLECULAR DOCKING AND MOLECULAR DYNAMICS
JRNL TITL 4 SIMULATIONS IN SEARCH FOR NEMATODE-SPECIFIC INHIBITORS OF
JRNL TITL 5 TS.
JRNL REF J. MOL. GRAPH. MODEL. V. 77 33 2017
JRNL REFN ISSN 1873-4243
JRNL PMID 28826032
JRNL DOI 10.1016/J.JMGM.2017.08.008
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 84834
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4466
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5667
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 285
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9318
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 136
REMARK 3 SOLVENT ATOMS : 862
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.30000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : -0.07000
REMARK 3 B13 (A**2) : -0.55000
REMARK 3 B23 (A**2) : 0.65000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.160
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.908
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9988 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9347 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13569 ; 1.815 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21558 ; 0.891 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1218 ; 6.745 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 516 ;35.537 ;23.547
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1733 ;16.268 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 80 ;20.773 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1422 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11317 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2471 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4640 ; 1.609 ; 1.765
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4639 ; 1.607 ; 1.765
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5814 ; 2.453 ; 2.634
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 18 A 299 4
REMARK 3 1 B 18 B 299 4
REMARK 3 1 C 18 C 299 4
REMARK 3 1 D 18 D 299 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 4104 ; 0.500 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 4104 ; 0.470 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 4104 ; 0.470 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 4104 ; 0.450 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4104 ; 2.430 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 4104 ; 3.330 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 4104 ; 2.080 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 4104 ; 2.900 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 308 A 308 4
REMARK 3 1 B 308 B 308 4
REMARK 3 1 C 308 C 308 4
REMARK 3 1 D 308 D 308 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 30 ; 0.520 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 B (A): 30 ; 0.540 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 C (A): 30 ; 0.360 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 D (A): 30 ; 0.360 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 30 ; 1.580 ; 2.000
REMARK 3 MEDIUM THERMAL 2 B (A**2): 30 ; 3.070 ; 2.000
REMARK 3 MEDIUM THERMAL 2 C (A**2): 30 ; 1.240 ; 2.000
REMARK 3 MEDIUM THERMAL 2 D (A**2): 30 ; 2.430 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 17 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5167 -12.9164 -11.9030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1288 T22: 0.0680
REMARK 3 T33: 0.0327 T12: 0.0828
REMARK 3 T13: 0.0137 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 1.0949 L22: 0.9369
REMARK 3 L33: 0.9942 L12: -0.0875
REMARK 3 L13: -0.3088 L23: 0.4807
REMARK 3 S TENSOR
REMARK 3 S11: -0.1295 S12: -0.1941 S13: -0.0921
REMARK 3 S21: 0.1763 S22: 0.1252 S23: 0.0211
REMARK 3 S31: 0.2470 S32: 0.1510 S33: 0.0043
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 17 B 304
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5604 15.0256 -11.9493
REMARK 3 T TENSOR
REMARK 3 T11: 0.0563 T22: 0.0453
REMARK 3 T33: 0.1389 T12: 0.0221
REMARK 3 T13: -0.0052 T23: -0.0645
REMARK 3 L TENSOR
REMARK 3 L11: 0.9836 L22: 1.2466
REMARK 3 L33: 1.0084 L12: -0.3826
REMARK 3 L13: -0.2821 L23: 0.3920
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: -0.1583 S13: 0.3315
REMARK 3 S21: -0.0692 S22: 0.0591 S23: -0.0714
REMARK 3 S31: -0.1432 S32: 0.0434 S33: -0.0613
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 18 C 303
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9967 -30.0826 -58.7476
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.0279
REMARK 3 T33: 0.0721 T12: -0.0218
REMARK 3 T13: 0.0323 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 1.0126 L22: 1.7934
REMARK 3 L33: 1.1358 L12: 0.4679
REMARK 3 L13: 0.2688 L23: 0.7128
REMARK 3 S TENSOR
REMARK 3 S11: -0.0122 S12: 0.1108 S13: -0.2140
REMARK 3 S21: 0.1392 S22: 0.0584 S23: -0.0448
REMARK 3 S31: 0.1826 S32: 0.0310 S33: -0.0463
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 18 D 299
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1159 -2.3022 -58.8267
REMARK 3 T TENSOR
REMARK 3 T11: 0.1291 T22: 0.0555
REMARK 3 T33: 0.0261 T12: -0.0775
REMARK 3 T13: 0.0165 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.8238 L22: 1.2882
REMARK 3 L33: 1.1042 L12: 0.1241
REMARK 3 L13: -0.0057 L23: 0.6764
REMARK 3 S TENSOR
REMARK 3 S11: -0.0857 S12: 0.1278 S13: 0.0499
REMARK 3 S21: -0.2101 S22: 0.1146 S23: 0.0410
REMARK 3 S31: -0.2563 S32: 0.1451 S33: -0.0290
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5BY6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210450.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89350
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.64400
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: PHASER 2.1.4, PHASER
REMARK 200 STARTING MODEL: 4EZ8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, PEG 4K, MAGNESIUM CHLORIDE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
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: DIMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 VAL A 5
REMARK 465 HIS A 6
REMARK 465 LYS A 7
REMARK 465 LEU A 8
REMARK 465 ASP A 9
REMARK 465 THR A 10
REMARK 465 ASN A 11
REMARK 465 SER A 12
REMARK 465 THR A 13
REMARK 465 SER A 14
REMARK 465 GLN A 15
REMARK 465 ASP A 16
REMARK 465 ILE A 301
REMARK 465 SER A 302
REMARK 465 MET A 303
REMARK 465 PRO A 304
REMARK 465 MET A 305
REMARK 465 ALA A 306
REMARK 465 VAL A 307
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 GLU B 3
REMARK 465 THR B 4
REMARK 465 VAL B 5
REMARK 465 HIS B 6
REMARK 465 LYS B 7
REMARK 465 LEU B 8
REMARK 465 ASP B 9
REMARK 465 THR B 10
REMARK 465 ASN B 11
REMARK 465 SER B 12
REMARK 465 THR B 13
REMARK 465 SER B 14
REMARK 465 GLN B 15
REMARK 465 ASP B 16
REMARK 465 MET B 305
REMARK 465 ALA B 306
REMARK 465 VAL B 307
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 GLU C 3
REMARK 465 THR C 4
REMARK 465 VAL C 5
REMARK 465 HIS C 6
REMARK 465 LYS C 7
REMARK 465 LEU C 8
REMARK 465 ASP C 9
REMARK 465 THR C 10
REMARK 465 ASN C 11
REMARK 465 SER C 12
REMARK 465 THR C 13
REMARK 465 SER C 14
REMARK 465 GLN C 15
REMARK 465 ASP C 16
REMARK 465 ASP C 17
REMARK 465 PRO C 304
REMARK 465 MET C 305
REMARK 465 ALA C 306
REMARK 465 VAL C 307
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 GLU D 3
REMARK 465 THR D 4
REMARK 465 VAL D 5
REMARK 465 HIS D 6
REMARK 465 LYS D 7
REMARK 465 LEU D 8
REMARK 465 ASP D 9
REMARK 465 THR D 10
REMARK 465 ASN D 11
REMARK 465 SER D 12
REMARK 465 THR D 13
REMARK 465 SER D 14
REMARK 465 GLN D 15
REMARK 465 ASP D 16
REMARK 465 ASP D 17
REMARK 465 LYS D 300
REMARK 465 ILE D 301
REMARK 465 SER D 302
REMARK 465 MET D 303
REMARK 465 PRO D 304
REMARK 465 MET D 305
REMARK 465 ALA D 306
REMARK 465 VAL D 307
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 O HOH D 691 O HOH D 700 1.92
REMARK 500 O HOH A 586 O HOH A 708 1.98
REMARK 500 O HOH A 581 O HOH A 628 1.98
REMARK 500 OD1 ASP A 63 O HOH A 501 2.02
REMARK 500 O HOH D 647 O HOH D 687 2.05
REMARK 500 O HOH C 610 O HOH C 633 2.10
REMARK 500 OG1 THR A 144 O HOH A 502 2.10
REMARK 500 O HOH B 555 O HOH B 635 2.12
REMARK 500 OH TYR A 129 O HOH A 503 2.13
REMARK 500 O HOH A 557 O HOH A 560 2.13
REMARK 500 OD1 ASP B 42 O ILE B 46 2.14
REMARK 500 O HOH B 688 O HOH B 694 2.14
REMARK 500 O HOH C 626 O HOH D 553 2.15
REMARK 500 O HOH A 625 O HOH A 681 2.17
REMARK 500 OD1 ASP B 63 O HOH B 501 2.17
REMARK 500 OD2 ASP B 63 NZ LYS B 274 2.17
REMARK 500 NE2 GLN C 29 O HOH C 501 2.18
REMARK 500 O HOH A 535 O HOH A 640 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU D 182 CD GLU D 182 OE1 0.079
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 ARG A 169 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 169 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 212 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 229 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 57 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 229 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG C 286 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG D 229 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 277 NE - CZ - NH1 ANGL. DEV. = 3.4 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 HIS A 135 31.64 -142.10
REMARK 500 SER A 141 -67.77 -107.38
REMARK 500 TYR A 298 -179.02 -67.08
REMARK 500 PRO A 299 -176.99 -62.90
REMARK 500 LEU B 117 67.05 -109.38
REMARK 500 HIS B 135 30.28 -143.37
REMARK 500 SER B 141 -71.51 -108.88
REMARK 500 GLU B 165 58.11 -140.33
REMARK 500 HIS C 135 30.80 -141.83
REMARK 500 LYS D 71 116.67 -166.94
REMARK 500 HIS D 135 28.24 -144.99
REMARK 500 SER D 141 -74.36 -102.79
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 UMP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404
DBREF 5BY6 A 1 307 UNP Q9NDD3 Q9NDD3_TRISP 1 307
DBREF 5BY6 B 1 307 UNP Q9NDD3 Q9NDD3_TRISP 1 307
DBREF 5BY6 C 1 307 UNP Q9NDD3 Q9NDD3_TRISP 1 307
DBREF 5BY6 D 1 307 UNP Q9NDD3 Q9NDD3_TRISP 1 307
SEQRES 1 A 307 MET THR GLU THR VAL HIS LYS LEU ASP THR ASN SER THR
SEQRES 2 A 307 SER GLN ASP ASP TYR VAL ASN GLN GLU GLU LEU ASN TYR
SEQRES 3 A 307 LEU ASN GLN LEU LYS ASP ILE ILE ASP HIS GLY VAL ARG
SEQRES 4 A 307 LYS ASN ASP ARG THR GLY ILE GLY THR LEU SER THR PHE
SEQRES 5 A 307 GLY THR GLN SER ARG TYR CYS LEU ARG ASP ASP ILE PHE
SEQRES 6 A 307 PRO LEU LEU THR THR LYS ARG VAL PHE TRP ARG GLY VAL
SEQRES 7 A 307 VAL GLU GLU LEU LEU TRP PHE ILE SER GLY SER THR ASN
SEQRES 8 A 307 ALA LYS GLN LEU SER GLU LYS ASN VAL ASN ILE TRP ASP
SEQRES 9 A 307 GLY ASN SER SER ARG GLU PHE LEU ASP SER ARG GLY LEU
SEQRES 10 A 307 TYR ASN TYR GLU GLU GLY ASP LEU GLY PRO VAL TYR GLY
SEQRES 11 A 307 PHE GLN TRP ARG HIS PHE GLY CYS PRO TYR SER SER MET
SEQRES 12 A 307 THR ALA ASP TYR LYS GLY LYS GLY TYR ASP GLN LEU GLN
SEQRES 13 A 307 GLN CYS ILE LYS MET ILE ARG GLU GLU PRO GLU SER ARG
SEQRES 14 A 307 ARG ILE ILE MET THR ALA TRP ASN PRO CYS ASP LEU GLU
SEQRES 15 A 307 LYS VAL ALA LEU PRO PRO CYS HIS CYS PHE VAL GLN PHE
SEQRES 16 A 307 TYR VAL ALA ASP GLY GLU LEU SER CYS GLN MET TYR GLN
SEQRES 17 A 307 ARG SER ALA ASP MET GLY LEU GLY VAL PRO PHE ASN ILE
SEQRES 18 A 307 ALA SER TYR SER LEU LEU THR ARG MET ILE ALA HIS ILE
SEQRES 19 A 307 THR SER LEU LYS PRO GLY PHE PHE ILE HIS THR ILE GLY
SEQRES 20 A 307 ASP ALA HIS VAL TYR LEU THR HIS VAL ASP ALA LEU LYS
SEQRES 21 A 307 VAL GLN MET GLU ARG LYS PRO ARG PRO PHE PRO LYS LEU
SEQRES 22 A 307 LYS ILE LEU ARG ASN VAL GLU ASN ILE ASP ASP PHE ARG
SEQRES 23 A 307 ALA GLU ASP PHE GLU LEU ILE ASN TYR LYS PRO TYR PRO
SEQRES 24 A 307 LYS ILE SER MET PRO MET ALA VAL
SEQRES 1 B 307 MET THR GLU THR VAL HIS LYS LEU ASP THR ASN SER THR
SEQRES 2 B 307 SER GLN ASP ASP TYR VAL ASN GLN GLU GLU LEU ASN TYR
SEQRES 3 B 307 LEU ASN GLN LEU LYS ASP ILE ILE ASP HIS GLY VAL ARG
SEQRES 4 B 307 LYS ASN ASP ARG THR GLY ILE GLY THR LEU SER THR PHE
SEQRES 5 B 307 GLY THR GLN SER ARG TYR CYS LEU ARG ASP ASP ILE PHE
SEQRES 6 B 307 PRO LEU LEU THR THR LYS ARG VAL PHE TRP ARG GLY VAL
SEQRES 7 B 307 VAL GLU GLU LEU LEU TRP PHE ILE SER GLY SER THR ASN
SEQRES 8 B 307 ALA LYS GLN LEU SER GLU LYS ASN VAL ASN ILE TRP ASP
SEQRES 9 B 307 GLY ASN SER SER ARG GLU PHE LEU ASP SER ARG GLY LEU
SEQRES 10 B 307 TYR ASN TYR GLU GLU GLY ASP LEU GLY PRO VAL TYR GLY
SEQRES 11 B 307 PHE GLN TRP ARG HIS PHE GLY CYS PRO TYR SER SER MET
SEQRES 12 B 307 THR ALA ASP TYR LYS GLY LYS GLY TYR ASP GLN LEU GLN
SEQRES 13 B 307 GLN CYS ILE LYS MET ILE ARG GLU GLU PRO GLU SER ARG
SEQRES 14 B 307 ARG ILE ILE MET THR ALA TRP ASN PRO CYS ASP LEU GLU
SEQRES 15 B 307 LYS VAL ALA LEU PRO PRO CYS HIS CYS PHE VAL GLN PHE
SEQRES 16 B 307 TYR VAL ALA ASP GLY GLU LEU SER CYS GLN MET TYR GLN
SEQRES 17 B 307 ARG SER ALA ASP MET GLY LEU GLY VAL PRO PHE ASN ILE
SEQRES 18 B 307 ALA SER TYR SER LEU LEU THR ARG MET ILE ALA HIS ILE
SEQRES 19 B 307 THR SER LEU LYS PRO GLY PHE PHE ILE HIS THR ILE GLY
SEQRES 20 B 307 ASP ALA HIS VAL TYR LEU THR HIS VAL ASP ALA LEU LYS
SEQRES 21 B 307 VAL GLN MET GLU ARG LYS PRO ARG PRO PHE PRO LYS LEU
SEQRES 22 B 307 LYS ILE LEU ARG ASN VAL GLU ASN ILE ASP ASP PHE ARG
SEQRES 23 B 307 ALA GLU ASP PHE GLU LEU ILE ASN TYR LYS PRO TYR PRO
SEQRES 24 B 307 LYS ILE SER MET PRO MET ALA VAL
SEQRES 1 C 307 MET THR GLU THR VAL HIS LYS LEU ASP THR ASN SER THR
SEQRES 2 C 307 SER GLN ASP ASP TYR VAL ASN GLN GLU GLU LEU ASN TYR
SEQRES 3 C 307 LEU ASN GLN LEU LYS ASP ILE ILE ASP HIS GLY VAL ARG
SEQRES 4 C 307 LYS ASN ASP ARG THR GLY ILE GLY THR LEU SER THR PHE
SEQRES 5 C 307 GLY THR GLN SER ARG TYR CYS LEU ARG ASP ASP ILE PHE
SEQRES 6 C 307 PRO LEU LEU THR THR LYS ARG VAL PHE TRP ARG GLY VAL
SEQRES 7 C 307 VAL GLU GLU LEU LEU TRP PHE ILE SER GLY SER THR ASN
SEQRES 8 C 307 ALA LYS GLN LEU SER GLU LYS ASN VAL ASN ILE TRP ASP
SEQRES 9 C 307 GLY ASN SER SER ARG GLU PHE LEU ASP SER ARG GLY LEU
SEQRES 10 C 307 TYR ASN TYR GLU GLU GLY ASP LEU GLY PRO VAL TYR GLY
SEQRES 11 C 307 PHE GLN TRP ARG HIS PHE GLY CYS PRO TYR SER SER MET
SEQRES 12 C 307 THR ALA ASP TYR LYS GLY LYS GLY TYR ASP GLN LEU GLN
SEQRES 13 C 307 GLN CYS ILE LYS MET ILE ARG GLU GLU PRO GLU SER ARG
SEQRES 14 C 307 ARG ILE ILE MET THR ALA TRP ASN PRO CYS ASP LEU GLU
SEQRES 15 C 307 LYS VAL ALA LEU PRO PRO CYS HIS CYS PHE VAL GLN PHE
SEQRES 16 C 307 TYR VAL ALA ASP GLY GLU LEU SER CYS GLN MET TYR GLN
SEQRES 17 C 307 ARG SER ALA ASP MET GLY LEU GLY VAL PRO PHE ASN ILE
SEQRES 18 C 307 ALA SER TYR SER LEU LEU THR ARG MET ILE ALA HIS ILE
SEQRES 19 C 307 THR SER LEU LYS PRO GLY PHE PHE ILE HIS THR ILE GLY
SEQRES 20 C 307 ASP ALA HIS VAL TYR LEU THR HIS VAL ASP ALA LEU LYS
SEQRES 21 C 307 VAL GLN MET GLU ARG LYS PRO ARG PRO PHE PRO LYS LEU
SEQRES 22 C 307 LYS ILE LEU ARG ASN VAL GLU ASN ILE ASP ASP PHE ARG
SEQRES 23 C 307 ALA GLU ASP PHE GLU LEU ILE ASN TYR LYS PRO TYR PRO
SEQRES 24 C 307 LYS ILE SER MET PRO MET ALA VAL
SEQRES 1 D 307 MET THR GLU THR VAL HIS LYS LEU ASP THR ASN SER THR
SEQRES 2 D 307 SER GLN ASP ASP TYR VAL ASN GLN GLU GLU LEU ASN TYR
SEQRES 3 D 307 LEU ASN GLN LEU LYS ASP ILE ILE ASP HIS GLY VAL ARG
SEQRES 4 D 307 LYS ASN ASP ARG THR GLY ILE GLY THR LEU SER THR PHE
SEQRES 5 D 307 GLY THR GLN SER ARG TYR CYS LEU ARG ASP ASP ILE PHE
SEQRES 6 D 307 PRO LEU LEU THR THR LYS ARG VAL PHE TRP ARG GLY VAL
SEQRES 7 D 307 VAL GLU GLU LEU LEU TRP PHE ILE SER GLY SER THR ASN
SEQRES 8 D 307 ALA LYS GLN LEU SER GLU LYS ASN VAL ASN ILE TRP ASP
SEQRES 9 D 307 GLY ASN SER SER ARG GLU PHE LEU ASP SER ARG GLY LEU
SEQRES 10 D 307 TYR ASN TYR GLU GLU GLY ASP LEU GLY PRO VAL TYR GLY
SEQRES 11 D 307 PHE GLN TRP ARG HIS PHE GLY CYS PRO TYR SER SER MET
SEQRES 12 D 307 THR ALA ASP TYR LYS GLY LYS GLY TYR ASP GLN LEU GLN
SEQRES 13 D 307 GLN CYS ILE LYS MET ILE ARG GLU GLU PRO GLU SER ARG
SEQRES 14 D 307 ARG ILE ILE MET THR ALA TRP ASN PRO CYS ASP LEU GLU
SEQRES 15 D 307 LYS VAL ALA LEU PRO PRO CYS HIS CYS PHE VAL GLN PHE
SEQRES 16 D 307 TYR VAL ALA ASP GLY GLU LEU SER CYS GLN MET TYR GLN
SEQRES 17 D 307 ARG SER ALA ASP MET GLY LEU GLY VAL PRO PHE ASN ILE
SEQRES 18 D 307 ALA SER TYR SER LEU LEU THR ARG MET ILE ALA HIS ILE
SEQRES 19 D 307 THR SER LEU LYS PRO GLY PHE PHE ILE HIS THR ILE GLY
SEQRES 20 D 307 ASP ALA HIS VAL TYR LEU THR HIS VAL ASP ALA LEU LYS
SEQRES 21 D 307 VAL GLN MET GLU ARG LYS PRO ARG PRO PHE PRO LYS LEU
SEQRES 22 D 307 LYS ILE LEU ARG ASN VAL GLU ASN ILE ASP ASP PHE ARG
SEQRES 23 D 307 ALA GLU ASP PHE GLU LEU ILE ASN TYR LYS PRO TYR PRO
SEQRES 24 D 307 LYS ILE SER MET PRO MET ALA VAL
HET UMP A 401 20
HET DTT A 402 8
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HET UMP B 401 20
HET UMP C 401 20
HET GOL C 402 6
HET UMP D 401 20
HET GOL D 402 6
HET GOL D 403 6
HET GOL D 404 6
HETNAM UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETNAM GOL GLYCEROL
HETSYN UMP DUMP
HETSYN DTT 1,4-DITHIOTHREITOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 UMP 4(C9 H13 N2 O8 P)
FORMUL 6 DTT C4 H10 O2 S2
FORMUL 7 GOL 8(C3 H8 O3)
FORMUL 18 HOH *862(H2 O)
HELIX 1 AA1 ASN A 20 GLY A 37 1 18
HELIX 2 AA2 ARG A 61 ILE A 64 5 4
HELIX 3 AA3 PHE A 74 SER A 87 1 14
HELIX 4 AA4 ALA A 92 GLU A 97 1 6
HELIX 5 AA5 ASP A 104 SER A 107 5 4
HELIX 6 AA6 SER A 108 ARG A 115 1 8
HELIX 7 AA7 VAL A 128 PHE A 136 1 9
HELIX 8 AA8 ASP A 153 GLU A 165 1 13
HELIX 9 AA9 ASN A 177 VAL A 184 5 8
HELIX 10 AB1 GLY A 216 THR A 235 1 20
HELIX 11 AB2 HIS A 255 ARG A 265 1 11
HELIX 12 AB3 ASN A 281 PHE A 285 5 5
HELIX 13 AB4 ARG A 286 GLU A 288 5 3
HELIX 14 AB5 ASN B 20 GLY B 37 1 18
HELIX 15 AB6 ARG B 61 ILE B 64 5 4
HELIX 16 AB7 PHE B 74 GLY B 88 1 15
HELIX 17 AB8 ASN B 91 GLU B 97 1 7
HELIX 18 AB9 ASP B 104 SER B 107 5 4
HELIX 19 AC1 SER B 108 ARG B 115 1 8
HELIX 20 AC2 VAL B 128 PHE B 136 1 9
HELIX 21 AC3 ASP B 153 GLU B 165 1 13
HELIX 22 AC4 ASN B 177 VAL B 184 5 8
HELIX 23 AC5 GLY B 216 THR B 235 1 20
HELIX 24 AC6 HIS B 255 GLU B 264 1 10
HELIX 25 AC7 ASN B 281 PHE B 285 5 5
HELIX 26 AC8 ARG B 286 GLU B 288 5 3
HELIX 27 AC9 ASN C 20 GLY C 37 1 18
HELIX 28 AD1 ARG C 61 ILE C 64 5 4
HELIX 29 AD2 PHE C 74 SER C 87 1 14
HELIX 30 AD3 ALA C 92 GLU C 97 1 6
HELIX 31 AD4 ASP C 104 SER C 107 5 4
HELIX 32 AD5 SER C 108 ARG C 115 1 8
HELIX 33 AD6 VAL C 128 PHE C 136 1 9
HELIX 34 AD7 ASP C 153 GLU C 165 1 13
HELIX 35 AD8 ASN C 177 VAL C 184 5 8
HELIX 36 AD9 GLY C 216 THR C 235 1 20
HELIX 37 AE1 HIS C 255 MET C 263 1 9
HELIX 38 AE2 ASN C 281 PHE C 285 5 5
HELIX 39 AE3 ARG C 286 GLU C 288 5 3
HELIX 40 AE4 ASN D 20 GLY D 37 1 18
HELIX 41 AE5 ARG D 61 ILE D 64 5 4
HELIX 42 AE6 PHE D 74 GLY D 88 1 15
HELIX 43 AE7 ALA D 92 GLU D 97 1 6
HELIX 44 AE8 SER D 108 ARG D 115 1 8
HELIX 45 AE9 VAL D 128 PHE D 136 1 9
HELIX 46 AF1 ASP D 153 GLU D 165 1 13
HELIX 47 AF2 ASN D 177 LEU D 181 5 5
HELIX 48 AF3 GLY D 216 SER D 236 1 21
HELIX 49 AF4 HIS D 255 MET D 263 1 9
HELIX 50 AF5 ASN D 281 PHE D 285 5 5
HELIX 51 AF6 ARG D 286 GLU D 288 5 3
SHEET 1 AA1 6 VAL A 38 ASN A 41 0
SHEET 2 AA1 6 GLY A 47 CYS A 59 -1 O THR A 48 N LYS A 40
SHEET 3 AA1 6 LYS A 238 TYR A 252 -1 O HIS A 244 N SER A 56
SHEET 4 AA1 6 GLU A 201 ASP A 212 1 N GLN A 208 O THR A 245
SHEET 5 AA1 6 HIS A 190 ALA A 198 -1 N GLN A 194 O GLN A 205
SHEET 6 AA1 6 ILE A 172 THR A 174 -1 N MET A 173 O VAL A 193
SHEET 1 AA2 2 LYS A 272 ILE A 275 0
SHEET 2 AA2 2 PHE A 290 ILE A 293 -1 O ILE A 293 N LYS A 272
SHEET 1 AA3 6 VAL B 38 ASN B 41 0
SHEET 2 AA3 6 GLY B 47 CYS B 59 -1 O THR B 48 N LYS B 40
SHEET 3 AA3 6 LYS B 238 TYR B 252 -1 O HIS B 244 N SER B 56
SHEET 4 AA3 6 GLU B 201 ASP B 212 1 N GLN B 208 O THR B 245
SHEET 5 AA3 6 HIS B 190 ALA B 198 -1 N PHE B 192 O TYR B 207
SHEET 6 AA3 6 ILE B 172 THR B 174 -1 N MET B 173 O VAL B 193
SHEET 1 AA4 2 LYS B 272 ILE B 275 0
SHEET 2 AA4 2 PHE B 290 ILE B 293 -1 O ILE B 293 N LYS B 272
SHEET 1 AA5 6 VAL C 38 ASN C 41 0
SHEET 2 AA5 6 GLY C 47 CYS C 59 -1 O SER C 50 N VAL C 38
SHEET 3 AA5 6 LYS C 238 TYR C 252 -1 O PHE C 242 N TYR C 58
SHEET 4 AA5 6 GLU C 201 ASP C 212 1 N GLN C 208 O THR C 245
SHEET 5 AA5 6 HIS C 190 ALA C 198 -1 N TYR C 196 O SER C 203
SHEET 6 AA5 6 ILE C 172 THR C 174 -1 N MET C 173 O VAL C 193
SHEET 1 AA6 2 LYS C 272 ILE C 275 0
SHEET 2 AA6 2 PHE C 290 ILE C 293 -1 O ILE C 293 N LYS C 272
SHEET 1 AA7 6 VAL D 38 ASN D 41 0
SHEET 2 AA7 6 GLY D 47 CYS D 59 -1 O THR D 48 N LYS D 40
SHEET 3 AA7 6 LYS D 238 TYR D 252 -1 O HIS D 244 N SER D 56
SHEET 4 AA7 6 GLU D 201 ASP D 212 1 N GLN D 208 O THR D 245
SHEET 5 AA7 6 HIS D 190 ALA D 198 -1 N GLN D 194 O GLN D 205
SHEET 6 AA7 6 ILE D 172 THR D 174 -1 N MET D 173 O VAL D 193
SHEET 1 AA8 2 LYS D 272 ILE D 275 0
SHEET 2 AA8 2 PHE D 290 ILE D 293 -1 O ILE D 293 N LYS D 272
SITE 1 AC1 17 ARG A 43 CYS A 189 HIS A 190 GLN A 208
SITE 2 AC1 17 ARG A 209 SER A 210 ALA A 211 ASP A 212
SITE 3 AC1 17 GLY A 216 ASN A 220 HIS A 250 TYR A 252
SITE 4 AC1 17 HOH A 559 HOH A 616 HOH A 640 ARG B 169
SITE 5 AC1 17 ARG B 170
SITE 1 AC2 2 GLU A 81 HOH A 616
SITE 1 AC3 4 GLY A 137 ASN A 177 HOH A 524 ASN B 177
SITE 1 AC4 3 CYS A 179 GLY B 137 GLY B 151
SITE 1 AC5 5 ASP A 257 ILE A 275 LEU A 276 ARG A 277
SITE 2 AC5 5 ASN A 278
SITE 1 AC6 5 TYR A 152 ASP A 153 GLN A 157 HOH A 531
SITE 2 AC6 5 ASN D 119
SITE 1 AC7 15 ARG A 169 ARG A 170 ARG B 43 CYS B 189
SITE 2 AC7 15 HIS B 190 GLN B 208 ARG B 209 SER B 210
SITE 3 AC7 15 ALA B 211 ASP B 212 ASN B 220 HIS B 250
SITE 4 AC7 15 TYR B 252 HOH B 531 HOH B 552
SITE 1 AC8 18 ARG C 43 CYS C 189 HIS C 190 GLN C 208
SITE 2 AC8 18 ARG C 209 SER C 210 ALA C 211 ASP C 212
SITE 3 AC8 18 GLY C 216 ASN C 220 HIS C 250 TYR C 252
SITE 4 AC8 18 HOH C 591 HOH C 607 HOH C 648 HOH C 667
SITE 5 AC8 18 ARG D 169 ARG D 170
SITE 1 AC9 3 CYS C 179 GLY D 137 GLY D 151
SITE 1 AD1 16 ARG C 169 ARG C 170 ARG D 43 CYS D 189
SITE 2 AD1 16 HIS D 190 GLN D 208 ARG D 209 SER D 210
SITE 3 AD1 16 ALA D 211 ASP D 212 GLY D 216 ASN D 220
SITE 4 AD1 16 HIS D 250 TYR D 252 HOH D 591 HOH D 599
SITE 1 AD2 5 GLY D 151 TYR D 152 ASP D 153 GLN D 157
SITE 2 AD2 5 HOH D 524
SITE 1 AD3 5 PHE C 136 GLY C 151 TYR C 152 CYS D 179
SITE 2 AD3 5 HOH D 553
SITE 1 AD4 4 ILE D 102 ASN D 106 HOH D 505 HOH D 572
CRYST1 51.695 65.914 96.511 85.31 85.33 67.12 P 1 4
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 0.019344 -0.008165 -0.001137 0.00000
SCALE2 0.000000 0.016467 -0.000901 0.00000
SCALE3 0.000000 0.000000 0.010412 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.793465 0.037198 -0.607477 0.75335 1
MTRIX2 2 0.037924 -0.993169 -0.110350 0.46334 1
MTRIX3 2 -0.607433 -0.110597 0.786635 0.17040 1
MTRIX1 3 -0.801590 -0.033228 0.596951 59.91692 1
MTRIX2 3 0.038297 0.993550 0.106729 22.23715 1
MTRIX3 3 -0.596647 0.108414 -0.795147 -41.65974 1
MTRIX1 4 0.999968 -0.006767 0.004258 -21.31737 1
MTRIX2 4 -0.006761 -0.999976 -0.001391 -15.04196 1
MTRIX3 4 0.004268 0.001362 -0.999990 -70.96286 1
MTRIX1 5 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 5 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 5 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 6 -0.812380 0.003429 -0.583118 1.39857 1
MTRIX2 6 0.059042 -0.994360 -0.088103 0.42013 1
MTRIX3 6 -0.580132 -0.106001 0.807596 0.15892 1
MTRIX1 7 -0.801053 -0.031813 0.597748 59.77079 1
MTRIX2 7 0.051230 0.991279 0.121411 22.69170 1
MTRIX3 7 -0.596397 0.127879 -0.792438 -40.84011 1
MTRIX1 8 0.999704 0.009892 0.022224 -20.31622 1
MTRIX2 8 0.009686 -0.999910 0.009334 -14.70920 1
MTRIX3 8 0.022314 -0.009116 -0.999709 -71.39606 1
(ATOM LINES ARE NOT SHOWN.)
END
