HEADER TRANSFERASE 13-FEB-08 2ZI5
TITLE C4S DCK VARIANT OF DCK IN COMPLEX WITH L-DA+UDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYCYTIDINE KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DCK;
COMPND 5 EC: 2.7.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DCK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS DCK, PURINE, DEOXYADENOSINE, DEOXYCYTIDINE KINASE, NUCLEOSIDE,
KEYWDS 2 ENANTIOMER, L-DA, UDP, ATP-BINDING, NUCLEOTIDE-BINDING, NUCLEUS,
KEYWDS 3 PHOSPHOPROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.SABINI,A.LAVIE
REVDAT 5 01-NOV-23 2ZI5 1 REMARK
REVDAT 4 10-NOV-21 2ZI5 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2ZI5 1 VERSN
REVDAT 2 20-MAY-08 2ZI5 1 JRNL
REVDAT 1 22-APR-08 2ZI5 0
JRNL AUTH E.SABINI,S.HAZRA,S.ORT,M.KONRAD,A.LAVIE
JRNL TITL STRUCTURAL BASIS FOR SUBSTRATE PROMISCUITY OF DCK
JRNL REF J.MOL.BIOL. V. 378 607 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18377927
JRNL DOI 10.1016/J.JMB.2008.02.061
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.219
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 87594
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7283
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 ANGLE DISTANCES (A) : 0.023
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000028001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : RIGAKU
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 : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110589
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.52200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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 1P5Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M SODIUM CITRATE, 100MM HEPES,
REMARK 280 PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.50500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.50500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 69.18000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.32500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 69.18000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.32500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.50500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 69.18000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.32500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.50500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 69.18000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 69.32500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.3 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -1.000000 0.000000 0.000000 138.36000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 59.50500
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: 3560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 138.36000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -59.50500
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 982
REMARK 465 GLY A 983
REMARK 465 SER A 984
REMARK 465 SER A 985
REMARK 465 HIS A 986
REMARK 465 HIS A 987
REMARK 465 HIS A 988
REMARK 465 HIS A 989
REMARK 465 HIS A 990
REMARK 465 HIS A 991
REMARK 465 SER A 992
REMARK 465 GLY A 993
REMARK 465 LEU A 994
REMARK 465 VAL A 995
REMARK 465 PRO A 996
REMARK 465 ARG A 997
REMARK 465 GLY A 998
REMARK 465 SER A 999
REMARK 465 HIS A 1000
REMARK 465 MET A 1001
REMARK 465 ALA A 1002
REMARK 465 THR A 1003
REMARK 465 PRO A 1004
REMARK 465 PRO A 1005
REMARK 465 LYS A 1006
REMARK 465 ARG A 1007
REMARK 465 SER A 1008
REMARK 465 SER A 1009
REMARK 465 PRO A 1010
REMARK 465 SER A 1011
REMARK 465 PHE A 1012
REMARK 465 SER A 1013
REMARK 465 ALA A 1014
REMARK 465 SER A 1015
REMARK 465 SER A 1016
REMARK 465 GLU A 1017
REMARK 465 GLY A 1018
REMARK 465 THR A 1019
REMARK 465 SER A 1059
REMARK 465 ASN A 1060
REMARK 465 VAL A 1061
REMARK 465 GLN A 1062
REMARK 465 SER A 1063
REMARK 465 THR A 1064
REMARK 465 GLN A 1065
REMARK 465 ASP A 1066
REMARK 465 GLU A 1067
REMARK 465 PHE A 1068
REMARK 465 GLU A 1069
REMARK 465 GLU A 1070
REMARK 465 LEU A 1071
REMARK 465 THR A 1072
REMARK 465 MET A 1073
REMARK 465 SER A 1074
REMARK 465 GLN A 1075
REMARK 465 GLY A 1114
REMARK 465 LYS A 1115
REMARK 465 LEU A 1116
REMARK 465 LYS A 1117
REMARK 465 ASP A 1118
REMARK 465 MET B 1982
REMARK 465 GLY B 1983
REMARK 465 SER B 1984
REMARK 465 SER B 1985
REMARK 465 HIS B 1986
REMARK 465 HIS B 1987
REMARK 465 HIS B 1988
REMARK 465 HIS B 1989
REMARK 465 HIS B 1990
REMARK 465 HIS B 1991
REMARK 465 SER B 1992
REMARK 465 GLY B 1993
REMARK 465 LEU B 1994
REMARK 465 VAL B 1995
REMARK 465 PRO B 1996
REMARK 465 ARG B 1997
REMARK 465 GLY B 1998
REMARK 465 SER B 1999
REMARK 465 HIS B 2000
REMARK 465 MET B 2001
REMARK 465 ALA B 2002
REMARK 465 THR B 2003
REMARK 465 PRO B 2004
REMARK 465 PRO B 2005
REMARK 465 LYS B 2006
REMARK 465 ARG B 2007
REMARK 465 SER B 2008
REMARK 465 SER B 2009
REMARK 465 PRO B 2010
REMARK 465 SER B 2011
REMARK 465 PHE B 2012
REMARK 465 SER B 2013
REMARK 465 ALA B 2014
REMARK 465 SER B 2015
REMARK 465 SER B 2016
REMARK 465 GLU B 2017
REMARK 465 GLY B 2018
REMARK 465 THR B 2019
REMARK 465 VAL B 2061
REMARK 465 GLN B 2062
REMARK 465 SER B 2063
REMARK 465 THR B 2064
REMARK 465 GLN B 2065
REMARK 465 ASP B 2066
REMARK 465 GLU B 2067
REMARK 465 PHE B 2068
REMARK 465 GLU B 2069
REMARK 465 GLU B 2070
REMARK 465 LEU B 2071
REMARK 465 THR B 2072
REMARK 465 LYS B 2117
REMARK 465 ASP B 2118
REMARK 465 ALA B 2119
REMARK 465 PHE B 2166
REMARK 465 GLY B 2167
REMARK 465 GLN B 2168
REMARK 465 MET C 2982
REMARK 465 GLY C 2983
REMARK 465 SER C 2984
REMARK 465 SER C 2985
REMARK 465 HIS C 2986
REMARK 465 HIS C 2987
REMARK 465 HIS C 2988
REMARK 465 HIS C 2989
REMARK 465 HIS C 2990
REMARK 465 HIS C 2991
REMARK 465 SER C 2992
REMARK 465 GLY C 2993
REMARK 465 LEU C 2994
REMARK 465 VAL C 2995
REMARK 465 PRO C 2996
REMARK 465 ARG C 2997
REMARK 465 GLY C 2998
REMARK 465 SER C 2999
REMARK 465 HIS C 3000
REMARK 465 MET C 3001
REMARK 465 ALA C 3002
REMARK 465 THR C 3003
REMARK 465 PRO C 3004
REMARK 465 PRO C 3005
REMARK 465 LYS C 3006
REMARK 465 ARG C 3007
REMARK 465 SER C 3008
REMARK 465 SER C 3009
REMARK 465 PRO C 3010
REMARK 465 SER C 3011
REMARK 465 PHE C 3012
REMARK 465 SER C 3013
REMARK 465 ALA C 3014
REMARK 465 SER C 3015
REMARK 465 SER C 3016
REMARK 465 GLU C 3017
REMARK 465 GLY C 3018
REMARK 465 THR C 3019
REMARK 465 ASN C 3060
REMARK 465 VAL C 3061
REMARK 465 GLN C 3062
REMARK 465 SER C 3063
REMARK 465 THR C 3064
REMARK 465 GLN C 3065
REMARK 465 ASP C 3066
REMARK 465 GLU C 3067
REMARK 465 PHE C 3068
REMARK 465 GLU C 3069
REMARK 465 GLU C 3070
REMARK 465 LEU C 3071
REMARK 465 THR C 3072
REMARK 465 GLY C 3114
REMARK 465 LYS C 3115
REMARK 465 LEU C 3116
REMARK 465 LYS C 3117
REMARK 465 ASP C 3118
REMARK 465 ALA C 3119
REMARK 465 GLY C 3167
REMARK 465 GLN C 3168
REMARK 465 SER C 3169
REMARK 465 MET D 3982
REMARK 465 GLY D 3983
REMARK 465 SER D 3984
REMARK 465 SER D 3985
REMARK 465 HIS D 3986
REMARK 465 HIS D 3987
REMARK 465 HIS D 3988
REMARK 465 HIS D 3989
REMARK 465 HIS D 3990
REMARK 465 HIS D 3991
REMARK 465 SER D 3992
REMARK 465 GLY D 3993
REMARK 465 LEU D 3994
REMARK 465 VAL D 3995
REMARK 465 PRO D 3996
REMARK 465 ARG D 3997
REMARK 465 GLY D 3998
REMARK 465 SER D 3999
REMARK 465 HIS D 4000
REMARK 465 MET D 4001
REMARK 465 ALA D 4002
REMARK 465 THR D 4003
REMARK 465 PRO D 4004
REMARK 465 PRO D 4005
REMARK 465 LYS D 4006
REMARK 465 ARG D 4007
REMARK 465 SER D 4008
REMARK 465 SER D 4009
REMARK 465 PRO D 4010
REMARK 465 SER D 4011
REMARK 465 PHE D 4012
REMARK 465 SER D 4013
REMARK 465 ALA D 4014
REMARK 465 SER D 4015
REMARK 465 SER D 4016
REMARK 465 GLU D 4017
REMARK 465 GLY D 4018
REMARK 465 THR D 4019
REMARK 465 SER D 4059
REMARK 465 ASN D 4060
REMARK 465 VAL D 4061
REMARK 465 GLN D 4062
REMARK 465 SER D 4063
REMARK 465 THR D 4064
REMARK 465 GLN D 4065
REMARK 465 ASP D 4066
REMARK 465 GLU D 4067
REMARK 465 PHE D 4068
REMARK 465 GLU D 4069
REMARK 465 GLU D 4070
REMARK 465 LEU D 4071
REMARK 465 THR D 4072
REMARK 465 MET D 4073
REMARK 465 SER D 4074
REMARK 465 GLN D 4075
REMARK 465 LYS D 4076
REMARK 465 LYS D 4117
REMARK 465 ASP D 4118
REMARK 465 ALA D 4119
REMARK 465 GLN D 4168
REMARK 465 SER D 4169
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 GLU A1120 CG CD OE1 OE2
REMARK 470 SER A1169 OG
REMARK 470 LYS A1222 CG CD CE NZ
REMARK 470 GLU A1230 CG CD OE1 OE2
REMARK 470 ARG B2057 CG CD NE CZ NH1 NH2
REMARK 470 MET B2073 CG SD CE
REMARK 470 ASN B2113 CG OD1 ND2
REMARK 470 LEU B2116 O
REMARK 470 TYR B2190 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B2196 CG CD OE1 OE2
REMARK 470 GLU B2230 CG CD OE1 OE2
REMARK 470 ARG C3057 CG CD NE CZ NH1 NH2
REMARK 470 MET C3073 CG SD CE
REMARK 470 ASN C3113 O
REMARK 470 GLU C3120 CG CD OE1 OE2
REMARK 470 TYR C3190 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR C3210 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN C3229 CG CD OE1 NE2
REMARK 470 GLU C3230 CG CD OE1 OE2
REMARK 470 GLU C3240 CG CD OE1 OE2
REMARK 470 ARG D4057 CG CD NE CZ NH1 NH2
REMARK 470 LYS D4115 CG CD CE NZ
REMARK 470 LEU D4116 O
REMARK 470 TYR D4210 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN D4229 CG CD OE1 NE2
REMARK 470 GLU D4230 CG CD OE1 OE2
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 N SER A 1129 O HOH A 6180 1.42
REMARK 500 O GLU B 2203 O HOH B 6066 1.56
REMARK 500 O HOH D 6100 O HOH D 6162 1.63
REMARK 500 O HOH C 6086 O HOH C 6161 1.71
REMARK 500 O ALA A 1056 O HOH A 6137 1.91
REMARK 500 C ARG A 1128 O HOH A 6180 1.93
REMARK 500 OE1 GLU A 1027 O HOH A 6180 2.13
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 TYR A1177 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG B2128 CD - NE - CZ ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG B2128 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG B2134 CD - NE - CZ ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG C3104 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG C3128 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C3188 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D4020 CD - NE - CZ ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG D4020 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PHE D4094 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 PHE D4094 CG - CD1 - CE1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 PHE D4094 CZ - CE2 - CD2 ANGL. DEV. = -9.0 DEGREES
REMARK 500 TYR D4155 CB - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TYR D4155 CB - CG - CD1 ANGL. DEV. = -3.9 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 ASN A1029 172.49 -47.21
REMARK 500 LYS A1088 68.94 -151.39
REMARK 500 THR A1098 -77.42 -48.63
REMARK 500 LEU A1112 -11.55 -47.72
REMARK 500 ARG A1128 -178.23 85.68
REMARK 500 SER A1139 -73.42 -45.13
REMARK 500 ASN A1164 -48.46 -135.47
REMARK 500 GLN A1168 83.10 -54.53
REMARK 500 ASN A1195 -90.53 -56.42
REMARK 500 HIS A1209 -75.88 -57.28
REMARK 500 TYR A1210 -37.59 -34.59
REMARK 500 LEU A1217 -64.49 -106.56
REMARK 500 THR A1223 -143.92 -133.35
REMARK 500 ASN A1224 27.52 -147.92
REMARK 500 ASP A1226 -45.57 -27.59
REMARK 500 GLN A1229 24.99 -78.82
REMARK 500 GLU A1230 -51.94 -140.03
REMARK 500 LYS A1245 64.94 -164.27
REMARK 500 SER B2059 74.36 -69.72
REMARK 500 LYS B2088 72.50 -167.67
REMARK 500 ASN B2113 -107.10 -77.02
REMARK 500 ARG B2128 167.73 59.45
REMARK 500 ILE B2200 118.10 -34.64
REMARK 500 LEU B2228 21.17 -73.21
REMARK 500 ASP B2241 151.37 -48.02
REMARK 500 LYS B2245 58.85 -143.23
REMARK 500 ILE C3021 152.76 -29.26
REMARK 500 ALA C3031 25.47 37.47
REMARK 500 TRP C3058 -17.63 -47.95
REMARK 500 ARG C3128 178.81 77.94
REMARK 500 ILE C3136 -77.78 -98.05
REMARK 500 ASN C3164 31.47 -89.70
REMARK 500 ASN C3164 31.97 -89.70
REMARK 500 ILE C3200 132.53 -36.64
REMARK 500 THR C3220 47.58 -103.47
REMARK 500 LYS C3245 73.32 -152.93
REMARK 500 SER C3258 43.44 -98.60
REMARK 500 ASN D4029 163.33 -44.43
REMARK 500 ALA D4031 19.65 53.87
REMARK 500 LYS D4088 79.29 -159.47
REMARK 500 LEU D4102 -75.52 -35.23
REMARK 500 ARG D4128 -178.28 61.91
REMARK 500 ILE D4136 -74.25 -106.28
REMARK 500 PHE D4166 73.15 -116.08
REMARK 500 LEU D4217 -61.49 -90.07
REMARK 500 ASP D4237 99.44 -69.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L1 A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 2301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L1 B 2401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP C 3301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L1 C 3401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP D 4301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L1 D 4401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P60 RELATED DB: PDB
REMARK 900 WT DCK IN COMPLEX WITH D-DC+ADP
REMARK 900 RELATED ID: 2NO1 RELATED DB: PDB
REMARK 900 C4S DCK VARIANT OF DCK IN COMPLEX WITH D-DC+ADP
REMARK 900 RELATED ID: 2NO7 RELATED DB: PDB
REMARK 900 C4S DCK VARIANT OF DCK IN COMPLEX WITH L-DC+ADP
REMARK 900 RELATED ID: 2ZI3 RELATED DB: PDB
REMARK 900 C4S-E247A DCK VARIANT OF DCK IN COMPLEX WITH D-DA+ADP
REMARK 900 RELATED ID: 2ZI4 RELATED DB: PDB
REMARK 900 C4S DCK VARIANT OF DCK IN COMPLEX WITH L-DA+ADP
REMARK 900 RELATED ID: 2ZI6 RELATED DB: PDB
REMARK 900 C4S DCK VARIANT OF DCK IN COMPLEX WITH D-DA+UDP
REMARK 900 RELATED ID: 2ZI7 RELATED DB: PDB
REMARK 900 C4S DCK VARIANT OF DCK IN COMPLEX WITH D-DG+UDP
REMARK 900 RELATED ID: 2ZI9 RELATED DB: PDB
REMARK 900 C4S-E247A DCK VARIANT OF DCK IN COMPLEX WITH CLADRIBINE+ADP
REMARK 900 RELATED ID: 2ZIA RELATED DB: PDB
REMARK 900 C4S DCK VARIANT OF DCK IN COMPLEX WITH CLADRIBINE+UDP
DBREF 2ZI5 A 1001 1260 UNP P27707 DCK_HUMAN 1 260
DBREF 2ZI5 B 2001 2260 UNP P27707 DCK_HUMAN 1 260
DBREF 2ZI5 C 3001 3260 UNP P27707 DCK_HUMAN 1 260
DBREF 2ZI5 D 4001 4260 UNP P27707 DCK_HUMAN 1 260
SEQADV 2ZI5 MET A 982 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY A 983 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER A 984 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER A 985 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS A 986 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS A 987 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS A 988 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS A 989 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS A 990 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS A 991 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER A 992 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY A 993 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 LEU A 994 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 VAL A 995 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 PRO A 996 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 ARG A 997 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY A 998 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER A 999 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS A 1000 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER A 1009 UNP P27707 CYS 9 ENGINEERED MUTATION
SEQADV 2ZI5 SER A 1045 UNP P27707 CYS 45 ENGINEERED MUTATION
SEQADV 2ZI5 SER A 1059 UNP P27707 CYS 59 ENGINEERED MUTATION
SEQADV 2ZI5 SER A 1146 UNP P27707 CYS 146 ENGINEERED MUTATION
SEQADV 2ZI5 MET B 1982 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY B 1983 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER B 1984 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER B 1985 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS B 1986 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS B 1987 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS B 1988 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS B 1989 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS B 1990 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS B 1991 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER B 1992 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY B 1993 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 LEU B 1994 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 VAL B 1995 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 PRO B 1996 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 ARG B 1997 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY B 1998 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER B 1999 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS B 2000 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER B 2009 UNP P27707 CYS 9 ENGINEERED MUTATION
SEQADV 2ZI5 SER B 2045 UNP P27707 CYS 45 ENGINEERED MUTATION
SEQADV 2ZI5 SER B 2059 UNP P27707 CYS 59 ENGINEERED MUTATION
SEQADV 2ZI5 SER B 2146 UNP P27707 CYS 146 ENGINEERED MUTATION
SEQADV 2ZI5 MET C 2982 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY C 2983 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER C 2984 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER C 2985 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS C 2986 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS C 2987 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS C 2988 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS C 2989 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS C 2990 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS C 2991 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER C 2992 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY C 2993 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 LEU C 2994 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 VAL C 2995 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 PRO C 2996 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 ARG C 2997 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY C 2998 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER C 2999 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS C 3000 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER C 3009 UNP P27707 CYS 9 ENGINEERED MUTATION
SEQADV 2ZI5 SER C 3045 UNP P27707 CYS 45 ENGINEERED MUTATION
SEQADV 2ZI5 SER C 3059 UNP P27707 CYS 59 ENGINEERED MUTATION
SEQADV 2ZI5 SER C 3146 UNP P27707 CYS 146 ENGINEERED MUTATION
SEQADV 2ZI5 MET D 3982 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY D 3983 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER D 3984 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER D 3985 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS D 3986 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS D 3987 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS D 3988 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS D 3989 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS D 3990 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS D 3991 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER D 3992 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY D 3993 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 LEU D 3994 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 VAL D 3995 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 PRO D 3996 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 ARG D 3997 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 GLY D 3998 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER D 3999 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 HIS D 4000 UNP P27707 EXPRESSION TAG
SEQADV 2ZI5 SER D 4009 UNP P27707 CYS 9 ENGINEERED MUTATION
SEQADV 2ZI5 SER D 4045 UNP P27707 CYS 45 ENGINEERED MUTATION
SEQADV 2ZI5 SER D 4059 UNP P27707 CYS 59 ENGINEERED MUTATION
SEQADV 2ZI5 SER D 4146 UNP P27707 CYS 146 ENGINEERED MUTATION
SEQRES 1 A 279 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU
SEQRES 2 A 279 VAL PRO ARG GLY SER HIS MET ALA THR PRO PRO LYS ARG
SEQRES 3 A 279 SER SER PRO SER PHE SER ALA SER SER GLU GLY THR ARG
SEQRES 4 A 279 ILE LYS LYS ILE SER ILE GLU GLY ASN ILE ALA ALA GLY
SEQRES 5 A 279 LYS SER THR PHE VAL ASN ILE LEU LYS GLN LEU SER GLU
SEQRES 6 A 279 ASP TRP GLU VAL VAL PRO GLU PRO VAL ALA ARG TRP SER
SEQRES 7 A 279 ASN VAL GLN SER THR GLN ASP GLU PHE GLU GLU LEU THR
SEQRES 8 A 279 MET SER GLN LYS ASN GLY GLY ASN VAL LEU GLN MET MET
SEQRES 9 A 279 TYR GLU LYS PRO GLU ARG TRP SER PHE THR PHE GLN THR
SEQRES 10 A 279 TYR ALA CYS LEU SER ARG ILE ARG ALA GLN LEU ALA SER
SEQRES 11 A 279 LEU ASN GLY LYS LEU LYS ASP ALA GLU LYS PRO VAL LEU
SEQRES 12 A 279 PHE PHE GLU ARG SER VAL TYR SER ASP ARG TYR ILE PHE
SEQRES 13 A 279 ALA SER ASN LEU TYR GLU SER GLU SER MET ASN GLU THR
SEQRES 14 A 279 GLU TRP THR ILE TYR GLN ASP TRP HIS ASP TRP MET ASN
SEQRES 15 A 279 ASN GLN PHE GLY GLN SER LEU GLU LEU ASP GLY ILE ILE
SEQRES 16 A 279 TYR LEU GLN ALA THR PRO GLU THR CYS LEU HIS ARG ILE
SEQRES 17 A 279 TYR LEU ARG GLY ARG ASN GLU GLU GLN GLY ILE PRO LEU
SEQRES 18 A 279 GLU TYR LEU GLU LYS LEU HIS TYR LYS HIS GLU SER TRP
SEQRES 19 A 279 LEU LEU HIS ARG THR LEU LYS THR ASN PHE ASP TYR LEU
SEQRES 20 A 279 GLN GLU VAL PRO ILE LEU THR LEU ASP VAL ASN GLU ASP
SEQRES 21 A 279 PHE LYS ASP LYS TYR GLU SER LEU VAL GLU LYS VAL LYS
SEQRES 22 A 279 GLU PHE LEU SER THR LEU
SEQRES 1 B 279 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU
SEQRES 2 B 279 VAL PRO ARG GLY SER HIS MET ALA THR PRO PRO LYS ARG
SEQRES 3 B 279 SER SER PRO SER PHE SER ALA SER SER GLU GLY THR ARG
SEQRES 4 B 279 ILE LYS LYS ILE SER ILE GLU GLY ASN ILE ALA ALA GLY
SEQRES 5 B 279 LYS SER THR PHE VAL ASN ILE LEU LYS GLN LEU SER GLU
SEQRES 6 B 279 ASP TRP GLU VAL VAL PRO GLU PRO VAL ALA ARG TRP SER
SEQRES 7 B 279 ASN VAL GLN SER THR GLN ASP GLU PHE GLU GLU LEU THR
SEQRES 8 B 279 MET SER GLN LYS ASN GLY GLY ASN VAL LEU GLN MET MET
SEQRES 9 B 279 TYR GLU LYS PRO GLU ARG TRP SER PHE THR PHE GLN THR
SEQRES 10 B 279 TYR ALA CYS LEU SER ARG ILE ARG ALA GLN LEU ALA SER
SEQRES 11 B 279 LEU ASN GLY LYS LEU LYS ASP ALA GLU LYS PRO VAL LEU
SEQRES 12 B 279 PHE PHE GLU ARG SER VAL TYR SER ASP ARG TYR ILE PHE
SEQRES 13 B 279 ALA SER ASN LEU TYR GLU SER GLU SER MET ASN GLU THR
SEQRES 14 B 279 GLU TRP THR ILE TYR GLN ASP TRP HIS ASP TRP MET ASN
SEQRES 15 B 279 ASN GLN PHE GLY GLN SER LEU GLU LEU ASP GLY ILE ILE
SEQRES 16 B 279 TYR LEU GLN ALA THR PRO GLU THR CYS LEU HIS ARG ILE
SEQRES 17 B 279 TYR LEU ARG GLY ARG ASN GLU GLU GLN GLY ILE PRO LEU
SEQRES 18 B 279 GLU TYR LEU GLU LYS LEU HIS TYR LYS HIS GLU SER TRP
SEQRES 19 B 279 LEU LEU HIS ARG THR LEU LYS THR ASN PHE ASP TYR LEU
SEQRES 20 B 279 GLN GLU VAL PRO ILE LEU THR LEU ASP VAL ASN GLU ASP
SEQRES 21 B 279 PHE LYS ASP LYS TYR GLU SER LEU VAL GLU LYS VAL LYS
SEQRES 22 B 279 GLU PHE LEU SER THR LEU
SEQRES 1 C 279 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU
SEQRES 2 C 279 VAL PRO ARG GLY SER HIS MET ALA THR PRO PRO LYS ARG
SEQRES 3 C 279 SER SER PRO SER PHE SER ALA SER SER GLU GLY THR ARG
SEQRES 4 C 279 ILE LYS LYS ILE SER ILE GLU GLY ASN ILE ALA ALA GLY
SEQRES 5 C 279 LYS SER THR PHE VAL ASN ILE LEU LYS GLN LEU SER GLU
SEQRES 6 C 279 ASP TRP GLU VAL VAL PRO GLU PRO VAL ALA ARG TRP SER
SEQRES 7 C 279 ASN VAL GLN SER THR GLN ASP GLU PHE GLU GLU LEU THR
SEQRES 8 C 279 MET SER GLN LYS ASN GLY GLY ASN VAL LEU GLN MET MET
SEQRES 9 C 279 TYR GLU LYS PRO GLU ARG TRP SER PHE THR PHE GLN THR
SEQRES 10 C 279 TYR ALA CYS LEU SER ARG ILE ARG ALA GLN LEU ALA SER
SEQRES 11 C 279 LEU ASN GLY LYS LEU LYS ASP ALA GLU LYS PRO VAL LEU
SEQRES 12 C 279 PHE PHE GLU ARG SER VAL TYR SER ASP ARG TYR ILE PHE
SEQRES 13 C 279 ALA SER ASN LEU TYR GLU SER GLU SER MET ASN GLU THR
SEQRES 14 C 279 GLU TRP THR ILE TYR GLN ASP TRP HIS ASP TRP MET ASN
SEQRES 15 C 279 ASN GLN PHE GLY GLN SER LEU GLU LEU ASP GLY ILE ILE
SEQRES 16 C 279 TYR LEU GLN ALA THR PRO GLU THR CYS LEU HIS ARG ILE
SEQRES 17 C 279 TYR LEU ARG GLY ARG ASN GLU GLU GLN GLY ILE PRO LEU
SEQRES 18 C 279 GLU TYR LEU GLU LYS LEU HIS TYR LYS HIS GLU SER TRP
SEQRES 19 C 279 LEU LEU HIS ARG THR LEU LYS THR ASN PHE ASP TYR LEU
SEQRES 20 C 279 GLN GLU VAL PRO ILE LEU THR LEU ASP VAL ASN GLU ASP
SEQRES 21 C 279 PHE LYS ASP LYS TYR GLU SER LEU VAL GLU LYS VAL LYS
SEQRES 22 C 279 GLU PHE LEU SER THR LEU
SEQRES 1 D 279 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY LEU
SEQRES 2 D 279 VAL PRO ARG GLY SER HIS MET ALA THR PRO PRO LYS ARG
SEQRES 3 D 279 SER SER PRO SER PHE SER ALA SER SER GLU GLY THR ARG
SEQRES 4 D 279 ILE LYS LYS ILE SER ILE GLU GLY ASN ILE ALA ALA GLY
SEQRES 5 D 279 LYS SER THR PHE VAL ASN ILE LEU LYS GLN LEU SER GLU
SEQRES 6 D 279 ASP TRP GLU VAL VAL PRO GLU PRO VAL ALA ARG TRP SER
SEQRES 7 D 279 ASN VAL GLN SER THR GLN ASP GLU PHE GLU GLU LEU THR
SEQRES 8 D 279 MET SER GLN LYS ASN GLY GLY ASN VAL LEU GLN MET MET
SEQRES 9 D 279 TYR GLU LYS PRO GLU ARG TRP SER PHE THR PHE GLN THR
SEQRES 10 D 279 TYR ALA CYS LEU SER ARG ILE ARG ALA GLN LEU ALA SER
SEQRES 11 D 279 LEU ASN GLY LYS LEU LYS ASP ALA GLU LYS PRO VAL LEU
SEQRES 12 D 279 PHE PHE GLU ARG SER VAL TYR SER ASP ARG TYR ILE PHE
SEQRES 13 D 279 ALA SER ASN LEU TYR GLU SER GLU SER MET ASN GLU THR
SEQRES 14 D 279 GLU TRP THR ILE TYR GLN ASP TRP HIS ASP TRP MET ASN
SEQRES 15 D 279 ASN GLN PHE GLY GLN SER LEU GLU LEU ASP GLY ILE ILE
SEQRES 16 D 279 TYR LEU GLN ALA THR PRO GLU THR CYS LEU HIS ARG ILE
SEQRES 17 D 279 TYR LEU ARG GLY ARG ASN GLU GLU GLN GLY ILE PRO LEU
SEQRES 18 D 279 GLU TYR LEU GLU LYS LEU HIS TYR LYS HIS GLU SER TRP
SEQRES 19 D 279 LEU LEU HIS ARG THR LEU LYS THR ASN PHE ASP TYR LEU
SEQRES 20 D 279 GLN GLU VAL PRO ILE LEU THR LEU ASP VAL ASN GLU ASP
SEQRES 21 D 279 PHE LYS ASP LYS TYR GLU SER LEU VAL GLU LYS VAL LYS
SEQRES 22 D 279 GLU PHE LEU SER THR LEU
HET UDP A1301 25
HET 3L1 A1401 18
HET UDP B2301 25
HET 3L1 B2401 18
HET UDP C3301 25
HET 3L1 C3401 18
HET UDP D4301 25
HET 3L1 D4401 18
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETNAM 3L1 (2S,3R,5S)-5-(6-AMINO-9H-PURIN-9-YL)-TETRAHYDRO-2-
HETNAM 2 3L1 (HYDROXYMETHYL)FURAN-3-OL
HETSYN 3L1 L-2'-DEOXYADENOSINE
FORMUL 5 UDP 4(C9 H14 N2 O12 P2)
FORMUL 6 3L1 4(C10 H13 N5 O3)
FORMUL 13 HOH *211(H2 O)
HELIX 1 1 GLY A 1033 GLN A 1043 1 11
HELIX 2 2 GLU A 1053 TRP A 1058 1 6
HELIX 3 3 LYS A 1076 LYS A 1088 1 13
HELIX 4 4 LYS A 1088 LEU A 1112 1 25
HELIX 5 5 SER A 1129 ILE A 1136 1 8
HELIX 6 6 ILE A 1136 SER A 1144 1 9
HELIX 7 7 ASN A 1148 ASN A 1163 1 16
HELIX 8 8 THR A 1181 ARG A 1192 1 12
HELIX 9 9 ASN A 1195 ILE A 1200 5 6
HELIX 10 10 PRO A 1201 LEU A 1217 1 17
HELIX 11 11 PHE A 1225 GLU A 1230 5 6
HELIX 12 12 TYR A 1246 SER A 1258 1 13
HELIX 13 13 GLY B 2033 LEU B 2041 1 9
HELIX 14 14 LYS B 2042 SER B 2045 5 4
HELIX 15 15 GLU B 2053 SER B 2059 1 7
HELIX 16 16 MET B 2073 LYS B 2088 1 16
HELIX 17 17 LYS B 2088 ALA B 2110 1 23
HELIX 18 18 ALA B 2110 LYS B 2115 1 6
HELIX 19 19 SER B 2129 ILE B 2136 1 8
HELIX 20 20 ILE B 2136 SER B 2144 1 9
HELIX 21 21 ASN B 2148 GLN B 2165 1 18
HELIX 22 22 THR B 2181 GLY B 2193 1 13
HELIX 23 23 ARG B 2194 ILE B 2200 1 7
HELIX 24 24 PRO B 2201 LEU B 2217 1 17
HELIX 25 25 PHE B 2225 GLU B 2230 5 6
HELIX 26 26 TYR B 2246 THR B 2259 1 14
HELIX 27 27 GLY C 3033 LYS C 3042 1 10
HELIX 28 28 GLU C 3053 TRP C 3058 1 6
HELIX 29 29 MET C 3073 LYS C 3088 1 16
HELIX 30 30 LYS C 3088 SER C 3111 1 24
HELIX 31 31 SER C 3129 ILE C 3136 1 8
HELIX 32 32 ILE C 3136 SER C 3144 1 9
HELIX 33 33 ASN C 3148 ASN C 3164 1 17
HELIX 34 34 THR C 3181 GLY C 3193 1 13
HELIX 35 35 ARG C 3194 GLY C 3199 1 6
HELIX 36 36 PRO C 3201 LEU C 3217 1 17
HELIX 37 37 PHE C 3225 GLU C 3230 5 6
HELIX 38 38 TYR C 3246 SER C 3258 1 13
HELIX 39 39 GLY D 4033 SER D 4045 1 13
HELIX 40 40 GLU D 4053 TRP D 4058 1 6
HELIX 41 41 ASN D 4077 LYS D 4088 1 12
HELIX 42 42 LYS D 4088 LYS D 4115 1 28
HELIX 43 43 SER D 4129 ILE D 4136 1 8
HELIX 44 44 ILE D 4136 SER D 4144 1 9
HELIX 45 45 ASN D 4148 ASN D 4164 1 17
HELIX 46 46 THR D 4181 GLY D 4193 1 13
HELIX 47 47 ARG D 4194 GLY D 4199 1 6
HELIX 48 48 PRO D 4201 LEU D 4216 1 16
HELIX 49 49 ASP D 4226 VAL D 4231 5 6
HELIX 50 50 TYR D 4246 THR D 4259 1 14
SHEET 1 A 5 TRP A1048 PRO A1052 0
SHEET 2 A 5 VAL A1123 GLU A1127 1 O GLU A1127 N VAL A1051
SHEET 3 A 5 LYS A1022 GLU A1027 1 N LYS A1022 O LEU A1124
SHEET 4 A 5 GLY A1174 GLN A1179 1 O ILE A1176 N SER A1025
SHEET 5 A 5 ILE A1233 ASP A1237 1 O LEU A1236 N GLN A1179
SHEET 1 B 5 TRP B2048 VAL B2051 0
SHEET 2 B 5 VAL B2123 GLU B2127 1 O PHE B2125 N VAL B2051
SHEET 3 B 5 LYS B2022 GLU B2027 1 N ILE B2024 O PHE B2126
SHEET 4 B 5 GLY B2174 GLN B2179 1 O LEU B2178 N GLU B2027
SHEET 5 B 5 ILE B2233 ASP B2237 1 O LEU B2234 N TYR B2177
SHEET 1 C 5 TRP C3048 VAL C3051 0
SHEET 2 C 5 VAL C3123 GLU C3127 1 O PHE C3125 N GLU C3049
SHEET 3 C 5 LYS C3022 GLY C3028 1 N ILE C3026 O PHE C3126
SHEET 4 C 5 GLY C3174 GLN C3179 1 O ILE C3176 N GLU C3027
SHEET 5 C 5 ILE C3233 ASP C3237 1 O LEU C3236 N TYR C3177
SHEET 1 D 5 TRP D4048 VAL D4051 0
SHEET 2 D 5 VAL D4123 GLU D4127 1 O PHE D4125 N GLU D4049
SHEET 3 D 5 LYS D4022 GLU D4027 1 N ILE D4026 O PHE D4126
SHEET 4 D 5 GLY D4174 GLN D4179 1 O LEU D4178 N GLU D4027
SHEET 5 D 5 ILE D4233 ASP D4237 1 O LEU D4234 N TYR D4177
SITE 1 AC1 11 ALA A1031 ALA A1032 GLY A1033 LYS A1034
SITE 2 AC1 11 SER A1035 THR A1036 ARG A1188 ARG A1192
SITE 3 AC1 11 ASP A1241 PHE A1242 LYS A1243
SITE 1 AC2 8 GLU A1053 MET A1085 TYR A1086 PHE A1096
SITE 2 AC2 8 GLN A1097 ASP A1133 PHE A1137 TYR A1204
SITE 1 AC3 11 ALA B2031 ALA B2032 GLY B2033 LYS B2034
SITE 2 AC3 11 SER B2035 THR B2036 ARG B2188 ARG B2192
SITE 3 AC3 11 ASP B2241 PHE B2242 LYS B2243
SITE 1 AC4 9 ILE B2030 GLU B2053 MET B2085 TYR B2086
SITE 2 AC4 9 PHE B2096 GLN B2097 ASP B2133 PHE B2137
SITE 3 AC4 9 TYR B2204
SITE 1 AC5 12 ALA C3031 ALA C3032 GLY C3033 LYS C3034
SITE 2 AC5 12 SER C3035 THR C3036 GLU C3127 ARG C3188
SITE 3 AC5 12 ARG C3192 ASP C3241 PHE C3242 LYS C3243
SITE 1 AC6 10 ILE C3030 GLU C3053 TYR C3086 PHE C3096
SITE 2 AC6 10 GLN C3097 ARG C3128 ASP C3133 PHE C3137
SITE 3 AC6 10 ILE C3200 TYR C3204
SITE 1 AC7 11 ALA D4031 ALA D4032 GLY D4033 LYS D4034
SITE 2 AC7 11 SER D4035 THR D4036 ARG D4188 ARG D4192
SITE 3 AC7 11 ASP D4241 PHE D4242 LYS D4243
SITE 1 AC8 10 ILE D4030 GLU D4053 TYR D4086 PHE D4096
SITE 2 AC8 10 GLN D4097 ARG D4128 ASP D4133 PHE D4137
SITE 3 AC8 10 ILE D4200 TYR D4204
CRYST1 138.360 138.650 119.010 90.00 90.00 90.00 C 2 2 21 32
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 0.007228 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008403 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
