HEADER TRANSFERASE 15-FEB-17 5X5D
TITLE HUMAN THYMIDYLATE SYNTHASE BOUND WITH DUMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 26-313;
COMPND 5 SYNONYM: TSASE;
COMPND 6 EC: 2.1.1.45;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TYMS, TS, OK/SW-CL.29;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS METHYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.CHEN,A.JANSSON,A.LARSSON,P.NORDLUND
REVDAT 3 22-NOV-23 5X5D 1 REMARK
REVDAT 2 30-AUG-17 5X5D 1 JRNL
REVDAT 1 28-JUN-17 5X5D 0
JRNL AUTH D.CHEN,A.JANSSON,D.SIM,A.LARSSON,P.NORDLUND
JRNL TITL STRUCTURAL ANALYSES OF HUMAN THYMIDYLATE SYNTHASE REVEAL A
JRNL TITL 2 SITE THAT MAY CONTROL CONFORMATIONAL SWITCHING BETWEEN
JRNL TITL 3 ACTIVE AND INACTIVE STATES
JRNL REF J. BIOL. CHEM. V. 292 13449 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28634233
JRNL DOI 10.1074/JBC.M117.787267
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.1
REMARK 3 NUMBER OF REFLECTIONS : 110666
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5830
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8599
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 423
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13758
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 1624
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : -0.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.189
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.177
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.978
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14268 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19328 ; 1.885 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1710 ; 6.452 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 688 ;35.883 ;23.358
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2412 ;14.205 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 112 ;16.903 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2037 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10944 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 15
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 26 313 B 26 313 19278 0.060 0.050
REMARK 3 2 A 26 310 C 26 310 19022 0.060 0.050
REMARK 3 3 A 26 309 D 26 309 18770 0.060 0.050
REMARK 3 4 A 26 305 E 26 305 18452 0.070 0.050
REMARK 3 5 A 26 308 F 26 308 18464 0.080 0.050
REMARK 3 6 B 26 310 C 26 310 18908 0.060 0.050
REMARK 3 7 B 26 309 D 26 309 18770 0.060 0.050
REMARK 3 8 B 26 305 E 26 305 18310 0.070 0.050
REMARK 3 9 B 26 308 F 26 308 18508 0.070 0.050
REMARK 3 10 C 26 309 D 26 309 18726 0.060 0.050
REMARK 3 11 C 26 305 E 26 305 18386 0.070 0.050
REMARK 3 12 C 26 308 F 26 308 18466 0.070 0.050
REMARK 3 13 D 26 305 E 26 305 18534 0.060 0.050
REMARK 3 14 D 26 308 F 26 308 18706 0.060 0.050
REMARK 3 15 E 26 305 F 26 305 18360 0.060 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5X5D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300002956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116562
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.40300
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
REMARK 200 STARTING MODEL: 1I00
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CALCODYLATE, PH 6.5, 25%
REMARK 280 PEG 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 158.84500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.87100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.87100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 238.26750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.87100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.87100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.42250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.87100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.87100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 238.26750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.87100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.87100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 79.42250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 158.84500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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 SER A 24
REMARK 465 MET A 25
REMARK 465 SER B 24
REMARK 465 MET B 25
REMARK 465 SER C 24
REMARK 465 MET C 25
REMARK 465 ALA C 312
REMARK 465 VAL C 313
REMARK 465 SER D 24
REMARK 465 MET D 25
REMARK 465 MET D 311
REMARK 465 ALA D 312
REMARK 465 VAL D 313
REMARK 465 SER E 24
REMARK 465 MET E 25
REMARK 465 ILE E 307
REMARK 465 LYS E 308
REMARK 465 MET E 309
REMARK 465 GLU E 310
REMARK 465 MET E 311
REMARK 465 ALA E 312
REMARK 465 VAL E 313
REMARK 465 SER F 24
REMARK 465 MET F 25
REMARK 465 GLU F 310
REMARK 465 MET F 311
REMARK 465 ALA F 312
REMARK 465 VAL F 313
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 308 CG CD CE NZ
REMARK 470 GLU A 310 CG CD OE1 OE2
REMARK 470 MET A 311 CG SD CE
REMARK 470 GLU C 145 CG CD OE1 OE2
REMARK 470 LYS C 244 CG CD CE NZ
REMARK 470 LYS C 308 CG CD CE NZ
REMARK 470 GLU C 310 CG CD OE1 OE2
REMARK 470 MET C 311 CG SD CE
REMARK 470 ARG D 147 NE CZ NH1 NH2
REMARK 470 GLN D 270 CG CD OE1 NE2
REMARK 470 LYS D 287 CE NZ
REMARK 470 ARG E 46 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 48 CG OD1 OD2
REMARK 470 ARG E 50 CG CD NE CZ NH1 NH2
REMARK 470 THR E 53 OG1 CG2
REMARK 470 LYS E 292 CE NZ
REMARK 470 HIS F 28 CG ND1 CD2 CE1 NE2
REMARK 470 ILE F 307 CG1 CG2 CD1
REMARK 470 LYS F 308 CG CD CE NZ
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 E 502 O HOH E 705 1.97
REMARK 500 O HOH D 693 O HOH D 716 2.04
REMARK 500 NH2 ARG D 46 O HOH D 501 2.08
REMARK 500 O HOH A 801 O HOH A 808 2.09
REMARK 500 OD1 ASP F 166 O HOH F 501 2.13
REMARK 500 O HOH E 668 O HOH E 756 2.14
REMARK 500 O HOH A 663 O HOH A 776 2.15
REMARK 500 NH1 ARG A 147 O HOH A 501 2.16
REMARK 500 OD1 ASP A 166 O HOH A 502 2.16
REMARK 500 OD1 ASP D 48 O HOH D 502 2.17
REMARK 500 O HOH B 752 O HOH B 783 2.17
REMARK 500 O HOH D 501 O HOH D 502 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH D 733 O HOH E 752 8454 2.03
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 C 294 CD GLU C 294 OE1 -0.077
REMARK 500 GLU D 70 CD GLU D 70 OE1 -0.071
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 GLN A 38 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG A 126 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 126 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 140 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LYS B 266 CD - CE - NZ ANGL. DEV. = -15.6 DEGREES
REMARK 500 ASP C 48 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG C 140 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 147 CB - CG - CD ANGL. DEV. = 15.8 DEGREES
REMARK 500 GLU C 294 CA - CB - CG ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG D 140 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 GLU E 70 CA - CB - CG ANGL. DEV. = 20.1 DEGREES
REMARK 500 GLU E 70 OE1 - CD - OE2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ARG E 140 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG E 185 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 GLU F 70 CA - CB - CG ANGL. DEV. = 21.6 DEGREES
REMARK 500 ASP F 116 CB - CG - OD1 ANGL. DEV. = 6.7 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 PHE A 123 58.65 -92.64
REMARK 500 HIS A 141 34.88 -142.54
REMARK 500 ARG A 147 -80.28 -109.53
REMARK 500 THR A 306 140.43 -38.13
REMARK 500 ALA A 312 -70.06 -48.49
REMARK 500 PHE B 123 57.95 -93.19
REMARK 500 HIS B 141 35.07 -142.81
REMARK 500 ARG B 147 -79.42 -111.70
REMARK 500 PHE C 123 57.98 -91.95
REMARK 500 HIS C 141 34.89 -143.01
REMARK 500 ARG C 147 -80.13 -111.75
REMARK 500 THR C 306 140.30 -38.24
REMARK 500 PHE D 123 52.31 -91.70
REMARK 500 HIS D 141 34.46 -143.77
REMARK 500 ARG D 147 -79.74 -111.08
REMARK 500 THR D 306 139.29 -35.64
REMARK 500 PHE E 123 49.30 -88.29
REMARK 500 HIS E 141 34.88 -142.64
REMARK 500 ARG E 147 -78.63 -110.79
REMARK 500 PHE F 123 57.24 -93.20
REMARK 500 HIS F 141 34.88 -142.67
REMARK 500 ARG F 147 -80.85 -114.23
REMARK 500 THR F 306 139.61 -38.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 808 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A 809 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B 788 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH C 742 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH D 793 DISTANCE = 8.04 ANGSTROMS
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 UMP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP F 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5X4W RELATED DB: PDB
REMARK 900 RELATED ID: 5X4X RELATED DB: PDB
REMARK 900 RELATED ID: 5X4Y RELATED DB: PDB
REMARK 900 RELATED ID: 5X5A RELATED DB: PDB
REMARK 900 RELATED ID: 5X5Q RELATED DB: PDB
REMARK 900 RELATED ID: 5X66 RELATED DB: PDB
REMARK 900 RELATED ID: 5X67 RELATED DB: PDB
REMARK 900 RELATED ID: 5X69 RELATED DB: PDB
DBREF 5X5D A 26 313 UNP P04818 TYSY_HUMAN 26 313
DBREF 5X5D B 26 313 UNP P04818 TYSY_HUMAN 26 313
DBREF 5X5D C 26 313 UNP P04818 TYSY_HUMAN 26 313
DBREF 5X5D D 26 313 UNP P04818 TYSY_HUMAN 26 313
DBREF 5X5D E 26 313 UNP P04818 TYSY_HUMAN 26 313
DBREF 5X5D F 26 313 UNP P04818 TYSY_HUMAN 26 313
SEQADV 5X5D SER A 24 UNP P04818 EXPRESSION TAG
SEQADV 5X5D MET A 25 UNP P04818 EXPRESSION TAG
SEQADV 5X5D SER B 24 UNP P04818 EXPRESSION TAG
SEQADV 5X5D MET B 25 UNP P04818 EXPRESSION TAG
SEQADV 5X5D SER C 24 UNP P04818 EXPRESSION TAG
SEQADV 5X5D MET C 25 UNP P04818 EXPRESSION TAG
SEQADV 5X5D SER D 24 UNP P04818 EXPRESSION TAG
SEQADV 5X5D MET D 25 UNP P04818 EXPRESSION TAG
SEQADV 5X5D SER E 24 UNP P04818 EXPRESSION TAG
SEQADV 5X5D MET E 25 UNP P04818 EXPRESSION TAG
SEQADV 5X5D SER F 24 UNP P04818 EXPRESSION TAG
SEQADV 5X5D MET F 25 UNP P04818 EXPRESSION TAG
SEQRES 1 A 290 SER MET PRO PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN
SEQRES 2 A 290 ILE GLN HIS ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP
SEQRES 3 A 290 ARG THR GLY THR GLY THR LEU SER VAL PHE GLY MET GLN
SEQRES 4 A 290 ALA ARG TYR SER LEU ARG ASP GLU PHE PRO LEU LEU THR
SEQRES 5 A 290 THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU
SEQRES 6 A 290 LEU TRP PHE ILE LYS GLY SER THR ASN ALA LYS GLU LEU
SEQRES 7 A 290 SER SER LYS GLY VAL LYS ILE TRP ASP ALA ASN GLY SER
SEQRES 8 A 290 ARG ASP PHE LEU ASP SER LEU GLY PHE SER THR ARG GLU
SEQRES 9 A 290 GLU GLY ASP LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG
SEQRES 10 A 290 HIS PHE GLY ALA GLU TYR ARG ASP MET GLU SER ASP TYR
SEQRES 11 A 290 SER GLY GLN GLY VAL ASP GLN LEU GLN ARG VAL ILE ASP
SEQRES 12 A 290 THR ILE LYS THR ASN PRO ASP ASP ARG ARG ILE ILE MET
SEQRES 13 A 290 CYS ALA TRP ASN PRO ARG ASP LEU PRO LEU MET ALA LEU
SEQRES 14 A 290 PRO PRO CYS HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN
SEQRES 15 A 290 SER GLU LEU SER CYS GLN LEU TYR GLN ARG SER GLY ASP
SEQRES 16 A 290 MET GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 17 A 290 LEU LEU THR TYR MET ILE ALA HIS ILE THR GLY LEU LYS
SEQRES 18 A 290 PRO GLY ASP PHE ILE HIS THR LEU GLY ASP ALA HIS ILE
SEQRES 19 A 290 TYR LEU ASN HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN
SEQRES 20 A 290 ARG GLU PRO ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG
SEQRES 21 A 290 LYS VAL GLU LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE
SEQRES 22 A 290 GLN ILE GLU GLY TYR ASN PRO HIS PRO THR ILE LYS MET
SEQRES 23 A 290 GLU MET ALA VAL
SEQRES 1 B 290 SER MET PRO PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN
SEQRES 2 B 290 ILE GLN HIS ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP
SEQRES 3 B 290 ARG THR GLY THR GLY THR LEU SER VAL PHE GLY MET GLN
SEQRES 4 B 290 ALA ARG TYR SER LEU ARG ASP GLU PHE PRO LEU LEU THR
SEQRES 5 B 290 THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU
SEQRES 6 B 290 LEU TRP PHE ILE LYS GLY SER THR ASN ALA LYS GLU LEU
SEQRES 7 B 290 SER SER LYS GLY VAL LYS ILE TRP ASP ALA ASN GLY SER
SEQRES 8 B 290 ARG ASP PHE LEU ASP SER LEU GLY PHE SER THR ARG GLU
SEQRES 9 B 290 GLU GLY ASP LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG
SEQRES 10 B 290 HIS PHE GLY ALA GLU TYR ARG ASP MET GLU SER ASP TYR
SEQRES 11 B 290 SER GLY GLN GLY VAL ASP GLN LEU GLN ARG VAL ILE ASP
SEQRES 12 B 290 THR ILE LYS THR ASN PRO ASP ASP ARG ARG ILE ILE MET
SEQRES 13 B 290 CYS ALA TRP ASN PRO ARG ASP LEU PRO LEU MET ALA LEU
SEQRES 14 B 290 PRO PRO CYS HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN
SEQRES 15 B 290 SER GLU LEU SER CYS GLN LEU TYR GLN ARG SER GLY ASP
SEQRES 16 B 290 MET GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 17 B 290 LEU LEU THR TYR MET ILE ALA HIS ILE THR GLY LEU LYS
SEQRES 18 B 290 PRO GLY ASP PHE ILE HIS THR LEU GLY ASP ALA HIS ILE
SEQRES 19 B 290 TYR LEU ASN HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN
SEQRES 20 B 290 ARG GLU PRO ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG
SEQRES 21 B 290 LYS VAL GLU LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE
SEQRES 22 B 290 GLN ILE GLU GLY TYR ASN PRO HIS PRO THR ILE LYS MET
SEQRES 23 B 290 GLU MET ALA VAL
SEQRES 1 C 290 SER MET PRO PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN
SEQRES 2 C 290 ILE GLN HIS ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP
SEQRES 3 C 290 ARG THR GLY THR GLY THR LEU SER VAL PHE GLY MET GLN
SEQRES 4 C 290 ALA ARG TYR SER LEU ARG ASP GLU PHE PRO LEU LEU THR
SEQRES 5 C 290 THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU
SEQRES 6 C 290 LEU TRP PHE ILE LYS GLY SER THR ASN ALA LYS GLU LEU
SEQRES 7 C 290 SER SER LYS GLY VAL LYS ILE TRP ASP ALA ASN GLY SER
SEQRES 8 C 290 ARG ASP PHE LEU ASP SER LEU GLY PHE SER THR ARG GLU
SEQRES 9 C 290 GLU GLY ASP LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG
SEQRES 10 C 290 HIS PHE GLY ALA GLU TYR ARG ASP MET GLU SER ASP TYR
SEQRES 11 C 290 SER GLY GLN GLY VAL ASP GLN LEU GLN ARG VAL ILE ASP
SEQRES 12 C 290 THR ILE LYS THR ASN PRO ASP ASP ARG ARG ILE ILE MET
SEQRES 13 C 290 CYS ALA TRP ASN PRO ARG ASP LEU PRO LEU MET ALA LEU
SEQRES 14 C 290 PRO PRO CYS HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN
SEQRES 15 C 290 SER GLU LEU SER CYS GLN LEU TYR GLN ARG SER GLY ASP
SEQRES 16 C 290 MET GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 17 C 290 LEU LEU THR TYR MET ILE ALA HIS ILE THR GLY LEU LYS
SEQRES 18 C 290 PRO GLY ASP PHE ILE HIS THR LEU GLY ASP ALA HIS ILE
SEQRES 19 C 290 TYR LEU ASN HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN
SEQRES 20 C 290 ARG GLU PRO ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG
SEQRES 21 C 290 LYS VAL GLU LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE
SEQRES 22 C 290 GLN ILE GLU GLY TYR ASN PRO HIS PRO THR ILE LYS MET
SEQRES 23 C 290 GLU MET ALA VAL
SEQRES 1 D 290 SER MET PRO PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN
SEQRES 2 D 290 ILE GLN HIS ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP
SEQRES 3 D 290 ARG THR GLY THR GLY THR LEU SER VAL PHE GLY MET GLN
SEQRES 4 D 290 ALA ARG TYR SER LEU ARG ASP GLU PHE PRO LEU LEU THR
SEQRES 5 D 290 THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU
SEQRES 6 D 290 LEU TRP PHE ILE LYS GLY SER THR ASN ALA LYS GLU LEU
SEQRES 7 D 290 SER SER LYS GLY VAL LYS ILE TRP ASP ALA ASN GLY SER
SEQRES 8 D 290 ARG ASP PHE LEU ASP SER LEU GLY PHE SER THR ARG GLU
SEQRES 9 D 290 GLU GLY ASP LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG
SEQRES 10 D 290 HIS PHE GLY ALA GLU TYR ARG ASP MET GLU SER ASP TYR
SEQRES 11 D 290 SER GLY GLN GLY VAL ASP GLN LEU GLN ARG VAL ILE ASP
SEQRES 12 D 290 THR ILE LYS THR ASN PRO ASP ASP ARG ARG ILE ILE MET
SEQRES 13 D 290 CYS ALA TRP ASN PRO ARG ASP LEU PRO LEU MET ALA LEU
SEQRES 14 D 290 PRO PRO CYS HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN
SEQRES 15 D 290 SER GLU LEU SER CYS GLN LEU TYR GLN ARG SER GLY ASP
SEQRES 16 D 290 MET GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 17 D 290 LEU LEU THR TYR MET ILE ALA HIS ILE THR GLY LEU LYS
SEQRES 18 D 290 PRO GLY ASP PHE ILE HIS THR LEU GLY ASP ALA HIS ILE
SEQRES 19 D 290 TYR LEU ASN HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN
SEQRES 20 D 290 ARG GLU PRO ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG
SEQRES 21 D 290 LYS VAL GLU LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE
SEQRES 22 D 290 GLN ILE GLU GLY TYR ASN PRO HIS PRO THR ILE LYS MET
SEQRES 23 D 290 GLU MET ALA VAL
SEQRES 1 E 290 SER MET PRO PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN
SEQRES 2 E 290 ILE GLN HIS ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP
SEQRES 3 E 290 ARG THR GLY THR GLY THR LEU SER VAL PHE GLY MET GLN
SEQRES 4 E 290 ALA ARG TYR SER LEU ARG ASP GLU PHE PRO LEU LEU THR
SEQRES 5 E 290 THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU
SEQRES 6 E 290 LEU TRP PHE ILE LYS GLY SER THR ASN ALA LYS GLU LEU
SEQRES 7 E 290 SER SER LYS GLY VAL LYS ILE TRP ASP ALA ASN GLY SER
SEQRES 8 E 290 ARG ASP PHE LEU ASP SER LEU GLY PHE SER THR ARG GLU
SEQRES 9 E 290 GLU GLY ASP LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG
SEQRES 10 E 290 HIS PHE GLY ALA GLU TYR ARG ASP MET GLU SER ASP TYR
SEQRES 11 E 290 SER GLY GLN GLY VAL ASP GLN LEU GLN ARG VAL ILE ASP
SEQRES 12 E 290 THR ILE LYS THR ASN PRO ASP ASP ARG ARG ILE ILE MET
SEQRES 13 E 290 CYS ALA TRP ASN PRO ARG ASP LEU PRO LEU MET ALA LEU
SEQRES 14 E 290 PRO PRO CYS HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN
SEQRES 15 E 290 SER GLU LEU SER CYS GLN LEU TYR GLN ARG SER GLY ASP
SEQRES 16 E 290 MET GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 17 E 290 LEU LEU THR TYR MET ILE ALA HIS ILE THR GLY LEU LYS
SEQRES 18 E 290 PRO GLY ASP PHE ILE HIS THR LEU GLY ASP ALA HIS ILE
SEQRES 19 E 290 TYR LEU ASN HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN
SEQRES 20 E 290 ARG GLU PRO ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG
SEQRES 21 E 290 LYS VAL GLU LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE
SEQRES 22 E 290 GLN ILE GLU GLY TYR ASN PRO HIS PRO THR ILE LYS MET
SEQRES 23 E 290 GLU MET ALA VAL
SEQRES 1 F 290 SER MET PRO PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN
SEQRES 2 F 290 ILE GLN HIS ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP
SEQRES 3 F 290 ARG THR GLY THR GLY THR LEU SER VAL PHE GLY MET GLN
SEQRES 4 F 290 ALA ARG TYR SER LEU ARG ASP GLU PHE PRO LEU LEU THR
SEQRES 5 F 290 THR LYS ARG VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU
SEQRES 6 F 290 LEU TRP PHE ILE LYS GLY SER THR ASN ALA LYS GLU LEU
SEQRES 7 F 290 SER SER LYS GLY VAL LYS ILE TRP ASP ALA ASN GLY SER
SEQRES 8 F 290 ARG ASP PHE LEU ASP SER LEU GLY PHE SER THR ARG GLU
SEQRES 9 F 290 GLU GLY ASP LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG
SEQRES 10 F 290 HIS PHE GLY ALA GLU TYR ARG ASP MET GLU SER ASP TYR
SEQRES 11 F 290 SER GLY GLN GLY VAL ASP GLN LEU GLN ARG VAL ILE ASP
SEQRES 12 F 290 THR ILE LYS THR ASN PRO ASP ASP ARG ARG ILE ILE MET
SEQRES 13 F 290 CYS ALA TRP ASN PRO ARG ASP LEU PRO LEU MET ALA LEU
SEQRES 14 F 290 PRO PRO CYS HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN
SEQRES 15 F 290 SER GLU LEU SER CYS GLN LEU TYR GLN ARG SER GLY ASP
SEQRES 16 F 290 MET GLY LEU GLY VAL PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 17 F 290 LEU LEU THR TYR MET ILE ALA HIS ILE THR GLY LEU LYS
SEQRES 18 F 290 PRO GLY ASP PHE ILE HIS THR LEU GLY ASP ALA HIS ILE
SEQRES 19 F 290 TYR LEU ASN HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN
SEQRES 20 F 290 ARG GLU PRO ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG
SEQRES 21 F 290 LYS VAL GLU LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE
SEQRES 22 F 290 GLN ILE GLU GLY TYR ASN PRO HIS PRO THR ILE LYS MET
SEQRES 23 F 290 GLU MET ALA VAL
HET UMP A 401 20
HET UMP B 401 20
HET UMP C 401 20
HET UMP D 401 20
HET UMP E 401 20
HET UMP F 401 20
HETNAM UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETSYN UMP DUMP
FORMUL 7 UMP 6(C9 H13 N2 O8 P)
FORMUL 13 HOH *1624(H2 O)
HELIX 1 AA1 GLY A 29 GLY A 44 1 16
HELIX 2 AA2 PHE A 80 LYS A 93 1 14
HELIX 3 AA3 ASN A 97 SER A 103 1 7
HELIX 4 AA4 TRP A 109 SER A 114 1 6
HELIX 5 AA5 SER A 114 LEU A 121 1 8
HELIX 6 AA6 VAL A 134 PHE A 142 1 9
HELIX 7 AA7 ASP A 159 ASN A 171 1 13
HELIX 8 AA8 ASP A 186 MET A 190 5 5
HELIX 9 AA9 GLY A 222 GLY A 242 1 21
HELIX 10 AB1 HIS A 261 GLN A 270 1 10
HELIX 11 AB2 LYS A 287 PHE A 291 5 5
HELIX 12 AB3 LYS A 292 GLU A 294 5 3
HELIX 13 AB4 GLY B 29 GLY B 44 1 16
HELIX 14 AB5 PHE B 80 LYS B 93 1 14
HELIX 15 AB6 ASN B 97 SER B 103 1 7
HELIX 16 AB7 TRP B 109 SER B 114 1 6
HELIX 17 AB8 SER B 114 LEU B 121 1 8
HELIX 18 AB9 VAL B 134 PHE B 142 1 9
HELIX 19 AC1 ASP B 159 ASN B 171 1 13
HELIX 20 AC2 ASP B 186 MET B 190 5 5
HELIX 21 AC3 GLY B 222 GLY B 242 1 21
HELIX 22 AC4 HIS B 261 GLN B 270 1 10
HELIX 23 AC5 LYS B 287 PHE B 291 5 5
HELIX 24 AC6 LYS B 292 GLU B 294 5 3
HELIX 25 AC7 GLY C 29 GLY C 44 1 16
HELIX 26 AC8 PHE C 80 LYS C 93 1 14
HELIX 27 AC9 ASN C 97 SER C 103 1 7
HELIX 28 AD1 ASP C 110 GLY C 113 5 4
HELIX 29 AD2 SER C 114 LEU C 121 1 8
HELIX 30 AD3 VAL C 134 PHE C 142 1 9
HELIX 31 AD4 ASP C 159 ASN C 171 1 13
HELIX 32 AD5 ASP C 186 MET C 190 5 5
HELIX 33 AD6 GLY C 222 GLY C 242 1 21
HELIX 34 AD7 HIS C 261 GLN C 270 1 10
HELIX 35 AD8 LYS C 287 PHE C 291 5 5
HELIX 36 AD9 LYS C 292 GLU C 294 5 3
HELIX 37 AE1 GLY D 29 GLY D 44 1 16
HELIX 38 AE2 PHE D 80 LYS D 93 1 14
HELIX 39 AE3 ASN D 97 SER D 103 1 7
HELIX 40 AE4 TRP D 109 GLY D 113 5 5
HELIX 41 AE5 SER D 114 LEU D 121 1 8
HELIX 42 AE6 VAL D 134 PHE D 142 1 9
HELIX 43 AE7 ASP D 159 ASN D 171 1 13
HELIX 44 AE8 ASP D 186 MET D 190 5 5
HELIX 45 AE9 GLY D 222 GLY D 242 1 21
HELIX 46 AF1 HIS D 261 GLN D 270 1 10
HELIX 47 AF2 LYS D 287 PHE D 291 5 5
HELIX 48 AF3 LYS D 292 GLU D 294 5 3
HELIX 49 AF4 GLY E 29 GLY E 44 1 16
HELIX 50 AF5 PHE E 80 LYS E 93 1 14
HELIX 51 AF6 ASN E 97 SER E 103 1 7
HELIX 52 AF7 TRP E 109 SER E 114 1 6
HELIX 53 AF8 SER E 114 LEU E 121 1 8
HELIX 54 AF9 VAL E 134 PHE E 142 1 9
HELIX 55 AG1 ASP E 159 ASN E 171 1 13
HELIX 56 AG2 ASP E 186 MET E 190 5 5
HELIX 57 AG3 GLY E 222 GLY E 242 1 21
HELIX 58 AG4 HIS E 261 GLN E 270 1 10
HELIX 59 AG5 LYS E 287 PHE E 291 5 5
HELIX 60 AG6 LYS E 292 GLU E 294 5 3
HELIX 61 AG7 GLY F 29 GLY F 44 1 16
HELIX 62 AG8 PHE F 80 LYS F 93 1 14
HELIX 63 AG9 ASN F 97 SER F 103 1 7
HELIX 64 AH1 ASP F 110 GLY F 113 5 4
HELIX 65 AH2 SER F 114 LEU F 121 1 8
HELIX 66 AH3 VAL F 134 PHE F 142 1 9
HELIX 67 AH4 ASP F 159 ASN F 171 1 13
HELIX 68 AH5 ASP F 186 MET F 190 5 5
HELIX 69 AH6 GLY F 222 GLY F 242 1 21
HELIX 70 AH7 HIS F 261 GLN F 270 1 10
HELIX 71 AH8 LYS F 287 PHE F 291 5 5
HELIX 72 AH9 LYS F 292 GLU F 294 5 3
SHEET 1 AA1 6 VAL A 45 LYS A 47 0
SHEET 2 AA1 6 THR A 55 SER A 66 -1 O SER A 57 N VAL A 45
SHEET 3 AA1 6 LYS A 244 TYR A 258 -1 O PHE A 248 N TYR A 65
SHEET 4 AA1 6 GLU A 207 ASP A 218 1 N LEU A 208 O GLY A 246
SHEET 5 AA1 6 HIS A 196 VAL A 204 -1 N TYR A 202 O SER A 209
SHEET 6 AA1 6 ILE A 178 CYS A 180 -1 N MET A 179 O CYS A 199
SHEET 1 AA2 2 LYS A 278 ILE A 281 0
SHEET 2 AA2 2 PHE A 296 GLU A 299 -1 O GLU A 299 N LYS A 278
SHEET 1 AA3 6 VAL B 45 LYS B 47 0
SHEET 2 AA3 6 THR B 55 SER B 66 -1 O SER B 57 N VAL B 45
SHEET 3 AA3 6 LYS B 244 TYR B 258 -1 O PHE B 248 N TYR B 65
SHEET 4 AA3 6 GLU B 207 ASP B 218 1 N LEU B 208 O GLY B 246
SHEET 5 AA3 6 HIS B 196 VAL B 204 -1 N TYR B 202 O SER B 209
SHEET 6 AA3 6 ILE B 178 CYS B 180 -1 N MET B 179 O CYS B 199
SHEET 1 AA4 2 LYS B 278 ILE B 281 0
SHEET 2 AA4 2 PHE B 296 GLU B 299 -1 O GLU B 299 N LYS B 278
SHEET 1 AA5 6 VAL C 45 LYS C 47 0
SHEET 2 AA5 6 THR C 55 SER C 66 -1 O SER C 57 N VAL C 45
SHEET 3 AA5 6 LYS C 244 TYR C 258 -1 O PHE C 248 N TYR C 65
SHEET 4 AA5 6 GLU C 207 ASP C 218 1 N LEU C 208 O GLY C 246
SHEET 5 AA5 6 HIS C 196 VAL C 204 -1 N TYR C 202 O SER C 209
SHEET 6 AA5 6 ILE C 178 CYS C 180 -1 N MET C 179 O CYS C 199
SHEET 1 AA6 2 LYS C 278 ILE C 281 0
SHEET 2 AA6 2 PHE C 296 GLU C 299 -1 O GLU C 299 N LYS C 278
SHEET 1 AA7 6 VAL D 45 LYS D 47 0
SHEET 2 AA7 6 THR D 55 SER D 66 -1 O SER D 57 N VAL D 45
SHEET 3 AA7 6 LYS D 244 TYR D 258 -1 O PHE D 248 N TYR D 65
SHEET 4 AA7 6 GLU D 207 ASP D 218 1 N LEU D 208 O GLY D 246
SHEET 5 AA7 6 HIS D 196 VAL D 204 -1 N TYR D 202 O SER D 209
SHEET 6 AA7 6 ILE D 178 CYS D 180 -1 N MET D 179 O CYS D 199
SHEET 1 AA8 2 LYS D 278 ILE D 281 0
SHEET 2 AA8 2 PHE D 296 GLU D 299 -1 O GLU D 299 N LYS D 278
SHEET 1 AA9 6 VAL E 45 LYS E 47 0
SHEET 2 AA9 6 THR E 55 SER E 66 -1 O SER E 57 N VAL E 45
SHEET 3 AA9 6 LYS E 244 TYR E 258 -1 O PHE E 248 N TYR E 65
SHEET 4 AA9 6 GLU E 207 ASP E 218 1 N LEU E 208 O GLY E 246
SHEET 5 AA9 6 HIS E 196 VAL E 204 -1 N TYR E 202 O SER E 209
SHEET 6 AA9 6 ILE E 178 CYS E 180 -1 N MET E 179 O CYS E 199
SHEET 1 AB1 2 LYS E 278 ILE E 281 0
SHEET 2 AB1 2 PHE E 296 GLU E 299 -1 O GLU E 299 N LYS E 278
SHEET 1 AB2 6 VAL F 45 LYS F 47 0
SHEET 2 AB2 6 THR F 55 SER F 66 -1 O SER F 57 N VAL F 45
SHEET 3 AB2 6 LYS F 244 TYR F 258 -1 O PHE F 248 N TYR F 65
SHEET 4 AB2 6 GLU F 207 ASP F 218 1 N LEU F 208 O GLY F 246
SHEET 5 AB2 6 HIS F 196 VAL F 204 -1 N TYR F 202 O SER F 209
SHEET 6 AB2 6 ILE F 178 CYS F 180 -1 N MET F 179 O CYS F 199
SHEET 1 AB3 2 LYS F 278 ILE F 281 0
SHEET 2 AB3 2 PHE F 296 GLU F 299 -1 O GLU F 299 N LYS F 278
SITE 1 AC1 16 CYS A 195 HIS A 196 GLN A 214 ARG A 215
SITE 2 AC1 16 SER A 216 GLY A 217 ASP A 218 GLY A 222
SITE 3 AC1 16 ASN A 226 HIS A 256 TYR A 258 HOH A 521
SITE 4 AC1 16 HOH A 569 HOH A 682 ARG D 175 ARG D 176
SITE 1 AC2 17 ARG B 50 CYS B 195 HIS B 196 GLN B 214
SITE 2 AC2 17 ARG B 215 SER B 216 GLY B 217 ASP B 218
SITE 3 AC2 17 GLY B 222 ASN B 226 HIS B 256 TYR B 258
SITE 4 AC2 17 HOH B 528 HOH B 568 HOH B 599 ARG E 175
SITE 5 AC2 17 ARG E 176
SITE 1 AC3 16 ARG C 50 CYS C 195 HIS C 196 GLN C 214
SITE 2 AC3 16 ARG C 215 SER C 216 GLY C 217 ASP C 218
SITE 3 AC3 16 GLY C 222 ASN C 226 HIS C 256 TYR C 258
SITE 4 AC3 16 HOH C 513 HOH C 529 ARG F 175 ARG F 176
SITE 1 AC4 17 ARG A 175 ARG A 176 ARG D 50 CYS D 195
SITE 2 AC4 17 HIS D 196 GLN D 214 ARG D 215 SER D 216
SITE 3 AC4 17 GLY D 217 ASP D 218 GLY D 222 ASN D 226
SITE 4 AC4 17 HIS D 256 TYR D 258 HOH D 528 HOH D 541
SITE 5 AC4 17 HOH D 551
SITE 1 AC5 15 ARG B 175 ARG B 176 CYS E 195 HIS E 196
SITE 2 AC5 15 GLN E 214 ARG E 215 SER E 216 GLY E 217
SITE 3 AC5 15 ASP E 218 GLY E 222 ASN E 226 HIS E 256
SITE 4 AC5 15 TYR E 258 HOH E 508 HOH E 590
SITE 1 AC6 15 ARG C 175 ARG C 176 ARG F 50 CYS F 195
SITE 2 AC6 15 HIS F 196 GLN F 214 ARG F 215 SER F 216
SITE 3 AC6 15 GLY F 217 ASP F 218 ASN F 226 HIS F 256
SITE 4 AC6 15 TYR F 258 HOH F 554 HOH F 570
CRYST1 109.742 109.742 317.690 90.00 90.00 90.00 P 43 21 2 48
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 0.009112 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009112 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003148 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
