HEADER TRANSFERASE 02-AUG-06 2J0F
TITLE STRUCTURAL BASIS FOR NON-COMPETITIVE PRODUCT INHIBITION IN HUMAN
TITLE 2 THYMIDINE PHOSPHORYLASE: IMPLICATION FOR DRUG DESIGN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDINE PHOSPHORYLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: TDRPASE, TP, PLATELET-DERIVED ENDOTHELIAL CELL GROWTH
COMPND 5 FACTOR, GLIOSTATIN, PD-ECGF;
COMPND 6 EC: 2.4.2.4;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HTP, CHEMOTAXIS, TRANSFERASE, POLYMORPHISM, DISEASE MUTATION,
KEYWDS 2 GLYCOSYLTRANSFERASE, ANGIOGENESIS, GROWTH FACTOR, DIFFERENTIATION,
KEYWDS 3 DEVELOPMENTAL PROTEIN, HUMAN THYMIDINE PHOSPHORYLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.EL OMARI,A.BRONCKAERS,S.LIEKENS,M.J.PEREZ-PEREZ,J.BALZARINI,
AUTHOR 2 D.K.STAMMERS
REVDAT 3 13-DEC-23 2J0F 1 REMARK
REVDAT 2 24-FEB-09 2J0F 1 VERSN
REVDAT 1 11-OCT-06 2J0F 0
JRNL AUTH K.EL OMARI,A.BRONCKAERS,S.LIEKENS,M.PEREZ-PEREZ,J.BALZARINI,
JRNL AUTH 2 D.K.STAMMERS
JRNL TITL STRUCTURAL BASIS FOR NON-COMPETITIVE PRODUCT INHIBITION IN
JRNL TITL 2 HUMAN THYMIDINE PHOSPHORYLASE: IMPLICATIONS FOR DRUG DESIGN.
JRNL REF BIOCHEM.J. V. 399 199 2006
JRNL REFN ISSN 0264-6021
JRNL PMID 16803458
JRNL DOI 10.1042/BJ20060513
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 102.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 63091
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) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3368
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) : 2.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4289
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 237
REMARK 3 BIN FREE R VALUE : 0.3940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13036
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.52000
REMARK 3 B22 (A**2) : -1.20000
REMARK 3 B33 (A**2) : 3.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.710
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.314
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.252
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.744
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13247 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17968 ; 1.247 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1780 ; 5.518 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 504 ;37.025 ;23.492
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2216 ;16.279 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 128 ;17.691 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2108 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9935 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6366 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9087 ; 0.292 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 562 ; 0.173 ; 0.200
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): 216 ; 0.342 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.362 ; 0.200
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): 9072 ; 0.829 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13948 ; 1.461 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4615 ; 2.888 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4020 ; 5.404 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 38 A 234 1
REMARK 3 1 B 38 B 234 1
REMARK 3 1 C 38 C 234 1
REMARK 3 1 D 38 D 234 1
REMARK 3 2 A 248 A 269 1
REMARK 3 2 B 248 B 269 1
REMARK 3 2 C 248 C 269 1
REMARK 3 2 D 248 D 269 1
REMARK 3 3 A 277 A 442 1
REMARK 3 3 B 277 B 442 1
REMARK 3 3 C 277 C 442 1
REMARK 3 3 D 277 D 442 1
REMARK 3 4 A 450 A 471 1
REMARK 3 4 B 450 B 471 1
REMARK 3 4 C 450 C 471 1
REMARK 3 4 D 450 D 471 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2973 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 2973 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 2973 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 2973 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 2973 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 2973 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 2973 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 2973 ; 0.07 ; 0.50
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 : 1.40
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. PSEUDO TRANSLATION DETECTED. MOLECULE D DISORDERED.
REMARK 4
REMARK 4 2J0F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1290029557.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : MAR345
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63091
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1UOU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% GLYCEROL, 20% PEG3350, PH 7.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 38.04350
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 ALA A 2
REMARK 465 ALA A 3
REMARK 465 LEU A 4
REMARK 465 MET A 5
REMARK 465 THR A 6
REMARK 465 PRO A 7
REMARK 465 GLY A 8
REMARK 465 THR A 9
REMARK 465 GLY A 10
REMARK 465 ALA A 11
REMARK 465 PRO A 12
REMARK 465 PRO A 13
REMARK 465 ALA A 14
REMARK 465 PRO A 15
REMARK 465 GLY A 16
REMARK 465 ASP A 17
REMARK 465 PHE A 18
REMARK 465 SER A 19
REMARK 465 GLY A 20
REMARK 465 GLU A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 GLN A 24
REMARK 465 GLY A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 ASP A 28
REMARK 465 PRO A 29
REMARK 465 SER A 30
REMARK 465 PRO A 31
REMARK 465 GLU A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 480
REMARK 465 GLN A 481
REMARK 465 GLN A 482
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 LEU B 4
REMARK 465 MET B 5
REMARK 465 THR B 6
REMARK 465 PRO B 7
REMARK 465 GLY B 8
REMARK 465 THR B 9
REMARK 465 GLY B 10
REMARK 465 ALA B 11
REMARK 465 PRO B 12
REMARK 465 PRO B 13
REMARK 465 ALA B 14
REMARK 465 PRO B 15
REMARK 465 GLY B 16
REMARK 465 ASP B 17
REMARK 465 PHE B 18
REMARK 465 SER B 19
REMARK 465 GLY B 20
REMARK 465 GLU B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 GLN B 24
REMARK 465 GLY B 25
REMARK 465 LEU B 26
REMARK 465 PRO B 27
REMARK 465 ASP B 28
REMARK 465 PRO B 29
REMARK 465 SER B 30
REMARK 465 PRO B 31
REMARK 465 GLU B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 480
REMARK 465 GLN B 481
REMARK 465 GLN B 482
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ALA C 3
REMARK 465 LEU C 4
REMARK 465 MET C 5
REMARK 465 THR C 6
REMARK 465 PRO C 7
REMARK 465 GLY C 8
REMARK 465 THR C 9
REMARK 465 GLY C 10
REMARK 465 ALA C 11
REMARK 465 PRO C 12
REMARK 465 PRO C 13
REMARK 465 ALA C 14
REMARK 465 PRO C 15
REMARK 465 GLY C 16
REMARK 465 ASP C 17
REMARK 465 PHE C 18
REMARK 465 SER C 19
REMARK 465 GLY C 20
REMARK 465 GLU C 21
REMARK 465 GLY C 22
REMARK 465 SER C 23
REMARK 465 GLN C 24
REMARK 465 GLY C 25
REMARK 465 LEU C 26
REMARK 465 PRO C 27
REMARK 465 ASP C 28
REMARK 465 PRO C 29
REMARK 465 SER C 30
REMARK 465 PRO C 31
REMARK 465 GLU C 32
REMARK 465 PRO C 33
REMARK 465 PRO C 480
REMARK 465 GLN C 481
REMARK 465 GLN C 482
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 ALA D 3
REMARK 465 LEU D 4
REMARK 465 MET D 5
REMARK 465 THR D 6
REMARK 465 PRO D 7
REMARK 465 GLY D 8
REMARK 465 THR D 9
REMARK 465 GLY D 10
REMARK 465 ALA D 11
REMARK 465 PRO D 12
REMARK 465 PRO D 13
REMARK 465 ALA D 14
REMARK 465 PRO D 15
REMARK 465 GLY D 16
REMARK 465 ASP D 17
REMARK 465 PHE D 18
REMARK 465 SER D 19
REMARK 465 GLY D 20
REMARK 465 GLU D 21
REMARK 465 GLY D 22
REMARK 465 SER D 23
REMARK 465 GLN D 24
REMARK 465 GLY D 25
REMARK 465 LEU D 26
REMARK 465 PRO D 27
REMARK 465 ASP D 28
REMARK 465 PRO D 29
REMARK 465 SER D 30
REMARK 465 PRO D 31
REMARK 465 GLU D 32
REMARK 465 PRO D 33
REMARK 465 PRO D 480
REMARK 465 GLN D 481
REMARK 465 GLN D 482
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 PRO A 479 O
REMARK 470 PRO B 479 O
REMARK 470 PRO C 479 O
REMARK 470 PRO D 479 O
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 NH2 ARG C 329 O HOH C 2123 1.79
REMARK 500 O LEU C 476 NH1 ARG D 376 1.80
REMARK 500 SG CYS D 183 O HOH D 2019 1.96
REMARK 500 NH2 ARG C 453 O HOH C 2166 2.06
REMARK 500 O ALA D 333 O HOH D 2047 2.12
REMARK 500 OD1 ASP D 233 O HOH D 2034 2.12
REMARK 500 O ASP D 443 O HOH D 2063 2.15
REMARK 500 NH2 ARG D 393 O HOH D 2055 2.18
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 OD2 ASP A 178 NH2 ARG B 393 1556 2.11
REMARK 500 OG SER B 364 O GLN D 97 2544 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 LEU C 211 CA - CB - CG ANGL. DEV. = 15.0 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 144 -154.65 -116.45
REMARK 500 VAL A 192 50.37 39.86
REMARK 500 ALA A 238 159.64 -47.06
REMARK 500 PRO A 243 -0.95 -47.57
REMARK 500 HIS A 283 -72.61 -128.22
REMARK 500 ALA A 297 -139.65 -119.80
REMARK 500 LEU A 391 144.30 -170.80
REMARK 500 SER B 144 -156.32 -116.36
REMARK 500 VAL B 192 52.57 38.64
REMARK 500 ALA B 238 -99.65 39.32
REMARK 500 PRO B 243 -5.19 -59.04
REMARK 500 ASP B 274 113.97 -0.89
REMARK 500 LYS B 275 148.65 81.78
REMARK 500 HIS B 283 -73.46 -130.87
REMARK 500 ALA B 297 -139.20 -120.75
REMARK 500 SER C 144 -157.62 -120.26
REMARK 500 VAL C 192 51.80 37.44
REMARK 500 MET C 273 110.55 -160.97
REMARK 500 HIS C 283 -73.02 -130.43
REMARK 500 ALA C 297 -143.92 -125.11
REMARK 500 LEU C 391 144.49 -171.55
REMARK 500 ALA C 446 155.49 166.98
REMARK 500 SER D 144 -154.25 -116.63
REMARK 500 VAL D 192 53.83 36.56
REMARK 500 LYS D 275 121.74 145.20
REMARK 500 HIS D 283 -72.24 -132.02
REMARK 500 ALA D 297 -139.83 -122.93
REMARK 500 LEU D 391 145.03 -171.46
REMARK 500 ALA D 446 -166.08 -164.92
REMARK 500 PRO D 472 136.12 -28.49
REMARK 500 ALA D 474 59.25 -160.23
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 ALA B 272 MET B 273 70.85
REMARK 500 MET B 273 ASP B 274 33.85
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 C2008 DISTANCE = 6.46 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TDR A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TDR B1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TDR C1480
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UOU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN THYMIDINE PHOSPHORYLASE IN COMPLEX WITH
REMARK 900 A SMALL MOLECULE INHIBITOR
DBREF 2J0F A 1 482 UNP P19971 TYPH_HUMAN 1 482
DBREF 2J0F B 1 482 UNP P19971 TYPH_HUMAN 1 482
DBREF 2J0F C 1 482 UNP P19971 TYPH_HUMAN 1 482
DBREF 2J0F D 1 482 UNP P19971 TYPH_HUMAN 1 482
SEQADV 2J0F ALA A 238 UNP P19971 GLY 238 CONFLICT
SEQADV 2J0F GLY A 239 UNP P19971 ALA 239 CONFLICT
SEQADV 2J0F LEU A 471 UNP P19971 SER 471 CONFLICT
SEQADV 2J0F ALA B 238 UNP P19971 GLY 238 CONFLICT
SEQADV 2J0F GLY B 239 UNP P19971 ALA 239 CONFLICT
SEQADV 2J0F LEU B 471 UNP P19971 SER 471 CONFLICT
SEQADV 2J0F ALA C 238 UNP P19971 GLY 238 CONFLICT
SEQADV 2J0F GLY C 239 UNP P19971 ALA 239 CONFLICT
SEQADV 2J0F LEU C 471 UNP P19971 SER 471 CONFLICT
SEQADV 2J0F ALA D 238 UNP P19971 GLY 238 CONFLICT
SEQADV 2J0F GLY D 239 UNP P19971 ALA 239 CONFLICT
SEQADV 2J0F LEU D 471 UNP P19971 SER 471 CONFLICT
SEQRES 1 A 482 MET ALA ALA LEU MET THR PRO GLY THR GLY ALA PRO PRO
SEQRES 2 A 482 ALA PRO GLY ASP PHE SER GLY GLU GLY SER GLN GLY LEU
SEQRES 3 A 482 PRO ASP PRO SER PRO GLU PRO LYS GLN LEU PRO GLU LEU
SEQRES 4 A 482 ILE ARG MET LYS ARG ASP GLY GLY ARG LEU SER GLU ALA
SEQRES 5 A 482 ASP ILE ARG GLY PHE VAL ALA ALA VAL VAL ASN GLY SER
SEQRES 6 A 482 ALA GLN GLY ALA GLN ILE GLY ALA MET LEU MET ALA ILE
SEQRES 7 A 482 ARG LEU ARG GLY MET ASP LEU GLU GLU THR SER VAL LEU
SEQRES 8 A 482 THR GLN ALA LEU ALA GLN SER GLY GLN GLN LEU GLU TRP
SEQRES 9 A 482 PRO GLU ALA TRP ARG GLN GLN LEU VAL ASP LYS HIS SER
SEQRES 10 A 482 THR GLY GLY VAL GLY ASP LYS VAL SER LEU VAL LEU ALA
SEQRES 11 A 482 PRO ALA LEU ALA ALA CYS GLY CYS LYS VAL PRO MET ILE
SEQRES 12 A 482 SER GLY ARG GLY LEU GLY HIS THR GLY GLY THR LEU ASP
SEQRES 13 A 482 LYS LEU GLU SER ILE PRO GLY PHE ASN VAL ILE GLN SER
SEQRES 14 A 482 PRO GLU GLN MET GLN VAL LEU LEU ASP GLN ALA GLY CYS
SEQRES 15 A 482 CYS ILE VAL GLY GLN SER GLU GLN LEU VAL PRO ALA ASP
SEQRES 16 A 482 GLY ILE LEU TYR ALA ALA ARG ASP VAL THR ALA THR VAL
SEQRES 17 A 482 ASP SER LEU PRO LEU ILE THR ALA SER ILE LEU SER LYS
SEQRES 18 A 482 LYS LEU VAL GLU GLY LEU SER ALA LEU VAL VAL ASP VAL
SEQRES 19 A 482 LYS PHE GLY ALA GLY ALA VAL PHE PRO ASN GLN GLU GLN
SEQRES 20 A 482 ALA ARG GLU LEU ALA LYS THR LEU VAL GLY VAL GLY ALA
SEQRES 21 A 482 SER LEU GLY LEU ARG VAL ALA ALA ALA LEU THR ALA MET
SEQRES 22 A 482 ASP LYS PRO LEU GLY ARG CYS VAL GLY HIS ALA LEU GLU
SEQRES 23 A 482 VAL GLU GLU ALA LEU LEU CYS MET ASP GLY ALA GLY PRO
SEQRES 24 A 482 PRO ASP LEU ARG ASP LEU VAL THR THR LEU GLY GLY ALA
SEQRES 25 A 482 LEU LEU TRP LEU SER GLY HIS ALA GLY THR GLN ALA GLN
SEQRES 26 A 482 GLY ALA ALA ARG VAL ALA ALA ALA LEU ASP ASP GLY SER
SEQRES 27 A 482 ALA LEU GLY ARG PHE GLU ARG MET LEU ALA ALA GLN GLY
SEQRES 28 A 482 VAL ASP PRO GLY LEU ALA ARG ALA LEU CYS SER GLY SER
SEQRES 29 A 482 PRO ALA GLU ARG ARG GLN LEU LEU PRO ARG ALA ARG GLU
SEQRES 30 A 482 GLN GLU GLU LEU LEU ALA PRO ALA ASP GLY THR VAL GLU
SEQRES 31 A 482 LEU VAL ARG ALA LEU PRO LEU ALA LEU VAL LEU HIS GLU
SEQRES 32 A 482 LEU GLY ALA GLY ARG SER ARG ALA GLY GLU PRO LEU ARG
SEQRES 33 A 482 LEU GLY VAL GLY ALA GLU LEU LEU VAL ASP VAL GLY GLN
SEQRES 34 A 482 ARG LEU ARG ARG GLY THR PRO TRP LEU ARG VAL HIS ARG
SEQRES 35 A 482 ASP GLY PRO ALA LEU SER GLY PRO GLN SER ARG ALA LEU
SEQRES 36 A 482 GLN GLU ALA LEU VAL LEU SER ASP ARG ALA PRO PHE ALA
SEQRES 37 A 482 ALA PRO LEU PRO PHE ALA GLU LEU VAL LEU PRO PRO GLN
SEQRES 38 A 482 GLN
SEQRES 1 B 482 MET ALA ALA LEU MET THR PRO GLY THR GLY ALA PRO PRO
SEQRES 2 B 482 ALA PRO GLY ASP PHE SER GLY GLU GLY SER GLN GLY LEU
SEQRES 3 B 482 PRO ASP PRO SER PRO GLU PRO LYS GLN LEU PRO GLU LEU
SEQRES 4 B 482 ILE ARG MET LYS ARG ASP GLY GLY ARG LEU SER GLU ALA
SEQRES 5 B 482 ASP ILE ARG GLY PHE VAL ALA ALA VAL VAL ASN GLY SER
SEQRES 6 B 482 ALA GLN GLY ALA GLN ILE GLY ALA MET LEU MET ALA ILE
SEQRES 7 B 482 ARG LEU ARG GLY MET ASP LEU GLU GLU THR SER VAL LEU
SEQRES 8 B 482 THR GLN ALA LEU ALA GLN SER GLY GLN GLN LEU GLU TRP
SEQRES 9 B 482 PRO GLU ALA TRP ARG GLN GLN LEU VAL ASP LYS HIS SER
SEQRES 10 B 482 THR GLY GLY VAL GLY ASP LYS VAL SER LEU VAL LEU ALA
SEQRES 11 B 482 PRO ALA LEU ALA ALA CYS GLY CYS LYS VAL PRO MET ILE
SEQRES 12 B 482 SER GLY ARG GLY LEU GLY HIS THR GLY GLY THR LEU ASP
SEQRES 13 B 482 LYS LEU GLU SER ILE PRO GLY PHE ASN VAL ILE GLN SER
SEQRES 14 B 482 PRO GLU GLN MET GLN VAL LEU LEU ASP GLN ALA GLY CYS
SEQRES 15 B 482 CYS ILE VAL GLY GLN SER GLU GLN LEU VAL PRO ALA ASP
SEQRES 16 B 482 GLY ILE LEU TYR ALA ALA ARG ASP VAL THR ALA THR VAL
SEQRES 17 B 482 ASP SER LEU PRO LEU ILE THR ALA SER ILE LEU SER LYS
SEQRES 18 B 482 LYS LEU VAL GLU GLY LEU SER ALA LEU VAL VAL ASP VAL
SEQRES 19 B 482 LYS PHE GLY ALA GLY ALA VAL PHE PRO ASN GLN GLU GLN
SEQRES 20 B 482 ALA ARG GLU LEU ALA LYS THR LEU VAL GLY VAL GLY ALA
SEQRES 21 B 482 SER LEU GLY LEU ARG VAL ALA ALA ALA LEU THR ALA MET
SEQRES 22 B 482 ASP LYS PRO LEU GLY ARG CYS VAL GLY HIS ALA LEU GLU
SEQRES 23 B 482 VAL GLU GLU ALA LEU LEU CYS MET ASP GLY ALA GLY PRO
SEQRES 24 B 482 PRO ASP LEU ARG ASP LEU VAL THR THR LEU GLY GLY ALA
SEQRES 25 B 482 LEU LEU TRP LEU SER GLY HIS ALA GLY THR GLN ALA GLN
SEQRES 26 B 482 GLY ALA ALA ARG VAL ALA ALA ALA LEU ASP ASP GLY SER
SEQRES 27 B 482 ALA LEU GLY ARG PHE GLU ARG MET LEU ALA ALA GLN GLY
SEQRES 28 B 482 VAL ASP PRO GLY LEU ALA ARG ALA LEU CYS SER GLY SER
SEQRES 29 B 482 PRO ALA GLU ARG ARG GLN LEU LEU PRO ARG ALA ARG GLU
SEQRES 30 B 482 GLN GLU GLU LEU LEU ALA PRO ALA ASP GLY THR VAL GLU
SEQRES 31 B 482 LEU VAL ARG ALA LEU PRO LEU ALA LEU VAL LEU HIS GLU
SEQRES 32 B 482 LEU GLY ALA GLY ARG SER ARG ALA GLY GLU PRO LEU ARG
SEQRES 33 B 482 LEU GLY VAL GLY ALA GLU LEU LEU VAL ASP VAL GLY GLN
SEQRES 34 B 482 ARG LEU ARG ARG GLY THR PRO TRP LEU ARG VAL HIS ARG
SEQRES 35 B 482 ASP GLY PRO ALA LEU SER GLY PRO GLN SER ARG ALA LEU
SEQRES 36 B 482 GLN GLU ALA LEU VAL LEU SER ASP ARG ALA PRO PHE ALA
SEQRES 37 B 482 ALA PRO LEU PRO PHE ALA GLU LEU VAL LEU PRO PRO GLN
SEQRES 38 B 482 GLN
SEQRES 1 C 482 MET ALA ALA LEU MET THR PRO GLY THR GLY ALA PRO PRO
SEQRES 2 C 482 ALA PRO GLY ASP PHE SER GLY GLU GLY SER GLN GLY LEU
SEQRES 3 C 482 PRO ASP PRO SER PRO GLU PRO LYS GLN LEU PRO GLU LEU
SEQRES 4 C 482 ILE ARG MET LYS ARG ASP GLY GLY ARG LEU SER GLU ALA
SEQRES 5 C 482 ASP ILE ARG GLY PHE VAL ALA ALA VAL VAL ASN GLY SER
SEQRES 6 C 482 ALA GLN GLY ALA GLN ILE GLY ALA MET LEU MET ALA ILE
SEQRES 7 C 482 ARG LEU ARG GLY MET ASP LEU GLU GLU THR SER VAL LEU
SEQRES 8 C 482 THR GLN ALA LEU ALA GLN SER GLY GLN GLN LEU GLU TRP
SEQRES 9 C 482 PRO GLU ALA TRP ARG GLN GLN LEU VAL ASP LYS HIS SER
SEQRES 10 C 482 THR GLY GLY VAL GLY ASP LYS VAL SER LEU VAL LEU ALA
SEQRES 11 C 482 PRO ALA LEU ALA ALA CYS GLY CYS LYS VAL PRO MET ILE
SEQRES 12 C 482 SER GLY ARG GLY LEU GLY HIS THR GLY GLY THR LEU ASP
SEQRES 13 C 482 LYS LEU GLU SER ILE PRO GLY PHE ASN VAL ILE GLN SER
SEQRES 14 C 482 PRO GLU GLN MET GLN VAL LEU LEU ASP GLN ALA GLY CYS
SEQRES 15 C 482 CYS ILE VAL GLY GLN SER GLU GLN LEU VAL PRO ALA ASP
SEQRES 16 C 482 GLY ILE LEU TYR ALA ALA ARG ASP VAL THR ALA THR VAL
SEQRES 17 C 482 ASP SER LEU PRO LEU ILE THR ALA SER ILE LEU SER LYS
SEQRES 18 C 482 LYS LEU VAL GLU GLY LEU SER ALA LEU VAL VAL ASP VAL
SEQRES 19 C 482 LYS PHE GLY ALA GLY ALA VAL PHE PRO ASN GLN GLU GLN
SEQRES 20 C 482 ALA ARG GLU LEU ALA LYS THR LEU VAL GLY VAL GLY ALA
SEQRES 21 C 482 SER LEU GLY LEU ARG VAL ALA ALA ALA LEU THR ALA MET
SEQRES 22 C 482 ASP LYS PRO LEU GLY ARG CYS VAL GLY HIS ALA LEU GLU
SEQRES 23 C 482 VAL GLU GLU ALA LEU LEU CYS MET ASP GLY ALA GLY PRO
SEQRES 24 C 482 PRO ASP LEU ARG ASP LEU VAL THR THR LEU GLY GLY ALA
SEQRES 25 C 482 LEU LEU TRP LEU SER GLY HIS ALA GLY THR GLN ALA GLN
SEQRES 26 C 482 GLY ALA ALA ARG VAL ALA ALA ALA LEU ASP ASP GLY SER
SEQRES 27 C 482 ALA LEU GLY ARG PHE GLU ARG MET LEU ALA ALA GLN GLY
SEQRES 28 C 482 VAL ASP PRO GLY LEU ALA ARG ALA LEU CYS SER GLY SER
SEQRES 29 C 482 PRO ALA GLU ARG ARG GLN LEU LEU PRO ARG ALA ARG GLU
SEQRES 30 C 482 GLN GLU GLU LEU LEU ALA PRO ALA ASP GLY THR VAL GLU
SEQRES 31 C 482 LEU VAL ARG ALA LEU PRO LEU ALA LEU VAL LEU HIS GLU
SEQRES 32 C 482 LEU GLY ALA GLY ARG SER ARG ALA GLY GLU PRO LEU ARG
SEQRES 33 C 482 LEU GLY VAL GLY ALA GLU LEU LEU VAL ASP VAL GLY GLN
SEQRES 34 C 482 ARG LEU ARG ARG GLY THR PRO TRP LEU ARG VAL HIS ARG
SEQRES 35 C 482 ASP GLY PRO ALA LEU SER GLY PRO GLN SER ARG ALA LEU
SEQRES 36 C 482 GLN GLU ALA LEU VAL LEU SER ASP ARG ALA PRO PHE ALA
SEQRES 37 C 482 ALA PRO LEU PRO PHE ALA GLU LEU VAL LEU PRO PRO GLN
SEQRES 38 C 482 GLN
SEQRES 1 D 482 MET ALA ALA LEU MET THR PRO GLY THR GLY ALA PRO PRO
SEQRES 2 D 482 ALA PRO GLY ASP PHE SER GLY GLU GLY SER GLN GLY LEU
SEQRES 3 D 482 PRO ASP PRO SER PRO GLU PRO LYS GLN LEU PRO GLU LEU
SEQRES 4 D 482 ILE ARG MET LYS ARG ASP GLY GLY ARG LEU SER GLU ALA
SEQRES 5 D 482 ASP ILE ARG GLY PHE VAL ALA ALA VAL VAL ASN GLY SER
SEQRES 6 D 482 ALA GLN GLY ALA GLN ILE GLY ALA MET LEU MET ALA ILE
SEQRES 7 D 482 ARG LEU ARG GLY MET ASP LEU GLU GLU THR SER VAL LEU
SEQRES 8 D 482 THR GLN ALA LEU ALA GLN SER GLY GLN GLN LEU GLU TRP
SEQRES 9 D 482 PRO GLU ALA TRP ARG GLN GLN LEU VAL ASP LYS HIS SER
SEQRES 10 D 482 THR GLY GLY VAL GLY ASP LYS VAL SER LEU VAL LEU ALA
SEQRES 11 D 482 PRO ALA LEU ALA ALA CYS GLY CYS LYS VAL PRO MET ILE
SEQRES 12 D 482 SER GLY ARG GLY LEU GLY HIS THR GLY GLY THR LEU ASP
SEQRES 13 D 482 LYS LEU GLU SER ILE PRO GLY PHE ASN VAL ILE GLN SER
SEQRES 14 D 482 PRO GLU GLN MET GLN VAL LEU LEU ASP GLN ALA GLY CYS
SEQRES 15 D 482 CYS ILE VAL GLY GLN SER GLU GLN LEU VAL PRO ALA ASP
SEQRES 16 D 482 GLY ILE LEU TYR ALA ALA ARG ASP VAL THR ALA THR VAL
SEQRES 17 D 482 ASP SER LEU PRO LEU ILE THR ALA SER ILE LEU SER LYS
SEQRES 18 D 482 LYS LEU VAL GLU GLY LEU SER ALA LEU VAL VAL ASP VAL
SEQRES 19 D 482 LYS PHE GLY ALA GLY ALA VAL PHE PRO ASN GLN GLU GLN
SEQRES 20 D 482 ALA ARG GLU LEU ALA LYS THR LEU VAL GLY VAL GLY ALA
SEQRES 21 D 482 SER LEU GLY LEU ARG VAL ALA ALA ALA LEU THR ALA MET
SEQRES 22 D 482 ASP LYS PRO LEU GLY ARG CYS VAL GLY HIS ALA LEU GLU
SEQRES 23 D 482 VAL GLU GLU ALA LEU LEU CYS MET ASP GLY ALA GLY PRO
SEQRES 24 D 482 PRO ASP LEU ARG ASP LEU VAL THR THR LEU GLY GLY ALA
SEQRES 25 D 482 LEU LEU TRP LEU SER GLY HIS ALA GLY THR GLN ALA GLN
SEQRES 26 D 482 GLY ALA ALA ARG VAL ALA ALA ALA LEU ASP ASP GLY SER
SEQRES 27 D 482 ALA LEU GLY ARG PHE GLU ARG MET LEU ALA ALA GLN GLY
SEQRES 28 D 482 VAL ASP PRO GLY LEU ALA ARG ALA LEU CYS SER GLY SER
SEQRES 29 D 482 PRO ALA GLU ARG ARG GLN LEU LEU PRO ARG ALA ARG GLU
SEQRES 30 D 482 GLN GLU GLU LEU LEU ALA PRO ALA ASP GLY THR VAL GLU
SEQRES 31 D 482 LEU VAL ARG ALA LEU PRO LEU ALA LEU VAL LEU HIS GLU
SEQRES 32 D 482 LEU GLY ALA GLY ARG SER ARG ALA GLY GLU PRO LEU ARG
SEQRES 33 D 482 LEU GLY VAL GLY ALA GLU LEU LEU VAL ASP VAL GLY GLN
SEQRES 34 D 482 ARG LEU ARG ARG GLY THR PRO TRP LEU ARG VAL HIS ARG
SEQRES 35 D 482 ASP GLY PRO ALA LEU SER GLY PRO GLN SER ARG ALA LEU
SEQRES 36 D 482 GLN GLU ALA LEU VAL LEU SER ASP ARG ALA PRO PHE ALA
SEQRES 37 D 482 ALA PRO LEU PRO PHE ALA GLU LEU VAL LEU PRO PRO GLN
SEQRES 38 D 482 GLN
HET TDR A1480 9
HET TDR B1480 9
HET TDR C1480 9
HETNAM TDR THYMINE
FORMUL 5 TDR 3(C5 H6 N2 O2)
FORMUL 8 HOH *450(H2 O)
HELIX 1 1 GLN A 35 ASP A 45 1 11
HELIX 2 2 SER A 50 GLY A 64 1 15
HELIX 3 3 GLN A 67 GLY A 82 1 16
HELIX 4 4 ASP A 84 GLN A 97 1 14
HELIX 5 5 PRO A 105 ARG A 109 5 5
HELIX 6 6 LYS A 124 CYS A 136 1 13
HELIX 7 7 GLY A 153 GLU A 159 1 7
HELIX 8 8 SER A 169 ALA A 180 1 12
HELIX 9 9 VAL A 192 THR A 205 1 14
HELIX 10 10 SER A 210 GLU A 225 1 16
HELIX 11 11 ASN A 244 LEU A 262 1 19
HELIX 12 12 HIS A 283 ASP A 295 1 13
HELIX 13 13 PRO A 299 SER A 317 1 19
HELIX 14 14 THR A 322 ASP A 336 1 15
HELIX 15 15 GLY A 337 GLN A 350 1 14
HELIX 16 16 ASP A 353 SER A 362 1 10
HELIX 17 17 SER A 364 LEU A 372 1 9
HELIX 18 18 ARG A 393 LEU A 404 1 12
HELIX 19 19 SER A 448 GLU A 457 1 10
HELIX 20 20 GLN B 35 ASP B 45 1 11
HELIX 21 21 SER B 50 GLY B 64 1 15
HELIX 22 22 GLN B 67 GLY B 82 1 16
HELIX 23 23 ASP B 84 SER B 98 1 15
HELIX 24 24 PRO B 105 ARG B 109 5 5
HELIX 25 25 LYS B 124 CYS B 136 1 13
HELIX 26 26 GLY B 153 GLU B 159 1 7
HELIX 27 27 SER B 169 ALA B 180 1 12
HELIX 28 28 VAL B 192 THR B 205 1 14
HELIX 29 29 SER B 210 GLU B 225 1 16
HELIX 30 30 ASN B 244 LEU B 262 1 19
HELIX 31 31 HIS B 283 ASP B 295 1 13
HELIX 32 32 PRO B 299 SER B 317 1 19
HELIX 33 33 THR B 322 ASP B 336 1 15
HELIX 34 34 GLY B 337 GLN B 350 1 14
HELIX 35 35 ASP B 353 SER B 362 1 10
HELIX 36 36 SER B 364 LEU B 372 1 9
HELIX 37 37 ARG B 393 LEU B 404 1 12
HELIX 38 38 SER B 448 GLU B 457 1 10
HELIX 39 39 GLN C 35 ASP C 45 1 11
HELIX 40 40 SER C 50 ASN C 63 1 14
HELIX 41 41 GLN C 67 GLY C 82 1 16
HELIX 42 42 ASP C 84 GLN C 97 1 14
HELIX 43 43 PRO C 105 ARG C 109 5 5
HELIX 44 44 LYS C 124 CYS C 136 1 13
HELIX 45 45 GLY C 153 GLU C 159 1 7
HELIX 46 46 SER C 169 ALA C 180 1 12
HELIX 47 47 VAL C 192 VAL C 204 1 13
HELIX 48 48 SER C 210 GLU C 225 1 16
HELIX 49 49 ASN C 244 LEU C 262 1 19
HELIX 50 50 HIS C 283 ASP C 295 1 13
HELIX 51 51 PRO C 299 SER C 317 1 19
HELIX 52 52 THR C 322 ASP C 336 1 15
HELIX 53 53 GLY C 337 GLN C 350 1 14
HELIX 54 54 ASP C 353 GLY C 363 1 11
HELIX 55 55 SER C 364 LEU C 372 1 9
HELIX 56 56 ARG C 393 LEU C 404 1 12
HELIX 57 57 SER C 448 GLU C 457 1 10
HELIX 58 58 GLN D 35 ASP D 45 1 11
HELIX 59 59 SER D 50 GLY D 64 1 15
HELIX 60 60 GLN D 67 GLY D 82 1 16
HELIX 61 61 ASP D 84 GLN D 97 1 14
HELIX 62 62 PRO D 105 ARG D 109 5 5
HELIX 63 63 LYS D 124 CYS D 136 1 13
HELIX 64 64 GLY D 153 GLU D 159 1 7
HELIX 65 65 SER D 169 ALA D 180 1 12
HELIX 66 66 VAL D 192 VAL D 204 1 13
HELIX 67 67 SER D 210 GLU D 225 1 16
HELIX 68 68 GLN D 245 LEU D 262 1 18
HELIX 69 69 HIS D 283 ASP D 295 1 13
HELIX 70 70 PRO D 299 SER D 317 1 19
HELIX 71 71 THR D 322 ASP D 336 1 15
HELIX 72 72 GLY D 337 GLN D 350 1 14
HELIX 73 73 ASP D 353 SER D 362 1 10
HELIX 74 74 SER D 364 LEU D 372 1 9
HELIX 75 75 ARG D 393 LEU D 404 1 12
HELIX 76 76 SER D 448 GLU D 457 1 10
SHEET 1 AA 4 VAL A 113 SER A 117 0
SHEET 2 AA 4 ALA A 229 LYS A 235 1 O ALA A 229 N ASP A 114
SHEET 3 AA 4 VAL A 266 ALA A 272 1 O ALA A 267 N VAL A 232
SHEET 4 AA 4 PHE A 473 VAL A 477 -1 O PHE A 473 N ALA A 272
SHEET 1 AB 2 VAL A 140 ILE A 143 0
SHEET 2 AB 2 CYS A 182 VAL A 185 1 O CYS A 183 N MET A 142
SHEET 1 AC 4 CYS A 280 GLY A 282 0
SHEET 2 AC 4 GLY A 420 LEU A 423 -1 O ALA A 421 N VAL A 281
SHEET 3 AC 4 PRO A 436 ARG A 442 -1 O ARG A 439 N GLU A 422
SHEET 4 AC 4 GLU A 377 LEU A 382 -1 O GLU A 377 N ARG A 442
SHEET 1 AD 3 ARG A 430 LEU A 431 0
SHEET 2 AD 3 GLY A 387 VAL A 392 -1 O GLY A 387 N LEU A 431
SHEET 3 AD 3 LEU A 459 SER A 462 -1 O VAL A 460 N GLU A 390
SHEET 1 BA 4 VAL B 113 SER B 117 0
SHEET 2 BA 4 ALA B 229 PHE B 236 1 O ALA B 229 N ASP B 114
SHEET 3 BA 4 VAL B 266 ALA B 272 1 O ALA B 267 N VAL B 232
SHEET 4 BA 4 GLU B 475 VAL B 477 -1 O GLU B 475 N LEU B 270
SHEET 1 BB 2 VAL B 140 ILE B 143 0
SHEET 2 BB 2 CYS B 182 VAL B 185 1 O CYS B 183 N MET B 142
SHEET 1 BC 4 CYS B 280 GLY B 282 0
SHEET 2 BC 4 GLY B 420 LEU B 423 -1 O ALA B 421 N VAL B 281
SHEET 3 BC 4 PRO B 436 ARG B 442 -1 O ARG B 439 N GLU B 422
SHEET 4 BC 4 GLU B 377 LEU B 382 -1 O GLU B 377 N ARG B 442
SHEET 1 BD 3 ARG B 430 LEU B 431 0
SHEET 2 BD 3 GLY B 387 VAL B 392 -1 O GLY B 387 N LEU B 431
SHEET 3 BD 3 LEU B 459 SER B 462 -1 O VAL B 460 N GLU B 390
SHEET 1 CA 4 VAL C 113 SER C 117 0
SHEET 2 CA 4 ALA C 229 PHE C 236 1 O ALA C 229 N ASP C 114
SHEET 3 CA 4 VAL C 266 ALA C 272 1 O ALA C 267 N VAL C 232
SHEET 4 CA 4 GLU C 475 VAL C 477 -1 O GLU C 475 N LEU C 270
SHEET 1 CB 2 VAL C 140 ILE C 143 0
SHEET 2 CB 2 CYS C 182 VAL C 185 1 O CYS C 183 N MET C 142
SHEET 1 CC 4 CYS C 280 GLY C 282 0
SHEET 2 CC 4 GLY C 420 LEU C 423 -1 O ALA C 421 N VAL C 281
SHEET 3 CC 4 PRO C 436 ARG C 442 -1 O ARG C 439 N GLU C 422
SHEET 4 CC 4 GLU C 377 LEU C 382 -1 O GLU C 377 N ARG C 442
SHEET 1 CD 3 ARG C 430 LEU C 431 0
SHEET 2 CD 3 GLY C 387 VAL C 392 -1 O GLY C 387 N LEU C 431
SHEET 3 CD 3 LEU C 459 SER C 462 -1 O VAL C 460 N GLU C 390
SHEET 1 DA 4 VAL D 113 SER D 117 0
SHEET 2 DA 4 ALA D 229 PHE D 236 1 O ALA D 229 N ASP D 114
SHEET 3 DA 4 VAL D 266 ALA D 272 1 O ALA D 267 N VAL D 232
SHEET 4 DA 4 GLU D 475 VAL D 477 -1 O GLU D 475 N LEU D 270
SHEET 1 DB 2 VAL D 140 ILE D 143 0
SHEET 2 DB 2 CYS D 182 VAL D 185 1 O CYS D 183 N MET D 142
SHEET 1 DC 4 CYS D 280 GLY D 282 0
SHEET 2 DC 4 GLY D 420 LEU D 423 -1 O ALA D 421 N VAL D 281
SHEET 3 DC 4 PRO D 436 ARG D 442 -1 O ARG D 439 N GLU D 422
SHEET 4 DC 4 GLU D 377 LEU D 382 -1 O GLU D 377 N ARG D 442
SHEET 1 DD 3 ARG D 430 LEU D 431 0
SHEET 2 DD 3 GLY D 387 VAL D 392 -1 O GLY D 387 N LEU D 431
SHEET 3 DD 3 LEU D 459 SER D 462 -1 O VAL D 460 N GLU D 390
SITE 1 AC1 10 HIS A 116 SER A 117 THR A 118 LEU A 148
SITE 2 AC1 10 TYR A 199 ARG A 202 ILE A 214 SER A 217
SITE 3 AC1 10 ILE A 218 LYS A 221
SITE 1 AC2 10 HIS B 116 SER B 117 THR B 118 LEU B 148
SITE 2 AC2 10 TYR B 199 ARG B 202 ILE B 214 SER B 217
SITE 3 AC2 10 ILE B 218 LYS B 221
SITE 1 AC3 10 HIS C 116 SER C 117 THR C 118 LEU C 148
SITE 2 AC3 10 TYR C 199 ARG C 202 ILE C 214 SER C 217
SITE 3 AC3 10 LYS C 221 HOH C2036
CRYST1 103.078 76.087 99.575 90.00 98.61 90.00 P 1 21 1 8
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 0.009701 0.000000 0.001469 0.00000
SCALE2 0.000000 0.013143 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010157 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
