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Chemical substance (2) PDB-CCD (2) Chemical reaction (1) KEGG ENZYME (1) Gene (1) KEGG GENES (1) Protein sequence (4) UniProt (1) SWISS-PROT (1) PDBSTR (2) Protein domain (5) InterPro (5) Literature (1) PubMed (1) All databases (14)
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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 03-APR-14 4Q1D
TITLE HUMAN DCK C4S-S74E MUTANT IN COMPLEX WITH UDP AND THE INHIBITOR 9 {2-
TITLE 2 {[(1R)-1-{2-[3-(2-FLUOROETHOXY)-4-METHOXYPHENYL]-5-PROPYL-1,3-
TITLE 3 THIAZOL-4-YL}ETHYL]SULFANYL}PYRIMIDINE-4,6-DIAMINE}
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYCYTIDINE KINASE;
COMPND 3 CHAIN: A, B;
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 C41;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS PHOSPHORYL TRANSFER, PHOSPHORYLATION, DEOXYCYTIDINE, TRANSFERASE,
KEYWDS 2 INHIBITOR COMPLEX, KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.NOMME,A.LAVIE
REVDAT 3 20-SEP-23 4Q1D 1 REMARK SEQADV
REVDAT 2 14-MAR-18 4Q1D 1 SEQADV
REVDAT 1 18-FEB-15 4Q1D 0
JRNL AUTH J.NOMME,Z.LI,R.M.GIPSON,J.WANG,A.L.ARMIJO,T.LE,S.PODDAR,
JRNL AUTH 2 T.SMITH,B.D.SANTARSIERO,H.A.NGUYEN,J.CZERNIN,
JRNL AUTH 3 A.N.ALEXANDROVA,M.E.JUNG,C.G.RADU,A.LAVIE
JRNL TITL STRUCTURE-GUIDED DEVELOPMENT OF DEOXYCYTIDINE KINASE
JRNL TITL 2 INHIBITORS WITH NANOMOLAR AFFINITY AND IMPROVED METABOLIC
JRNL TITL 3 STABILITY.
JRNL REF J.MED.CHEM. V. 57 9480 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25341194
JRNL DOI 10.1021/JM501124J
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 35172
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1934
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) : 2574
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 148
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3726
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 112
REMARK 3 SOLVENT ATOMS : 92
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.50000
REMARK 3 B22 (A**2) : -4.50000
REMARK 3 B33 (A**2) : 9.00000
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): 0.037
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.218
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3940 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3644 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5359 ; 1.676 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8363 ; 2.016 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 457 ; 7.248 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;39.917 ;24.339
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 652 ;18.446 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;17.539 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 576 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4397 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 940 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1831 ; 3.458 ; 5.144
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1830 ; 3.458 ; 5.143
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2281 ; 4.704 ; 7.703
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2282 ; 4.703 ; 7.704
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2109 ; 3.114 ; 5.201
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2108 ; 3.114 ; 5.200
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3077 ; 4.146 ; 7.771
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4844 ; 5.929 ;41.728
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4832 ; 5.928 ;41.722
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 : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.505
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, K, -L
REMARK 3 TWIN FRACTION : 0.495
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4Q1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 93
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
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 : 37712
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3800
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) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.67100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.790
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 4JLN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M TRISODIUM CITRATE DEHYDRATE AND
REMARK 280 25 MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 60.31150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.15575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.46725
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 3820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 PRO A 5
REMARK 465 LYS A 6
REMARK 465 ARG A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 PRO A 10
REMARK 465 SER A 11
REMARK 465 PHE A 12
REMARK 465 SER A 13
REMARK 465 ALA A 14
REMARK 465 SER A 15
REMARK 465 SER A 16
REMARK 465 GLU A 17
REMARK 465 GLY A 18
REMARK 465 THR A 19
REMARK 465 VAL A 61
REMARK 465 GLN A 62
REMARK 465 SER A 63
REMARK 465 THR A 64
REMARK 465 GLN A 65
REMARK 465 ASP A 66
REMARK 465 GLU A 67
REMARK 465 PHE A 68
REMARK 465 GLU A 69
REMARK 465 GLU A 70
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 PRO B 4
REMARK 465 PRO B 5
REMARK 465 LYS B 6
REMARK 465 ARG B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 PRO B 10
REMARK 465 SER B 11
REMARK 465 PHE B 12
REMARK 465 SER B 13
REMARK 465 ALA B 14
REMARK 465 SER B 15
REMARK 465 SER B 16
REMARK 465 GLU B 17
REMARK 465 GLY B 18
REMARK 465 THR B 19
REMARK 465 VAL B 61
REMARK 465 GLN B 62
REMARK 465 SER B 63
REMARK 465 THR B 64
REMARK 465 GLN B 65
REMARK 465 ASP B 66
REMARK 465 GLU B 67
REMARK 465 PHE B 68
REMARK 465 GLU B 69
REMARK 465 GLU B 70
REMARK 465 PHE B 166
REMARK 465 GLY B 167
REMARK 465 GLN B 168
REMARK 465 SER B 169
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 LEU A 71 CG CD1 CD2
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 LYS A 117 CG CD CE NZ
REMARK 470 ASP A 118 CG OD1 OD2
REMARK 470 ASN A 164 CG OD1 ND2
REMARK 470 GLU A 171 CG CD OE1 OE2
REMARK 470 ASN A 195 CG OD1 ND2
REMARK 470 GLU A 196 CG CD OE1 OE2
REMARK 470 GLU A 203 CG CD OE1 OE2
REMARK 470 LYS A 222 CG CD CE NZ
REMARK 470 GLN A 229 CG CD OE1 NE2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 LYS B 42 CG CD CE NZ
REMARK 470 ARG B 57 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 60 CG OD1 ND2
REMARK 470 LEU B 71 CG CD1 CD2
REMARK 470 LYS B 76 CG CD CE NZ
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 ASP B 118 CG OD1 OD2
REMARK 470 HIS B 187 CG ND1 CD2 CE1 NE2
REMARK 470 TYR B 190 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 196 CG CD OE1 OE2
REMARK 470 GLU B 203 CG CD OE1 OE2
REMARK 470 LYS B 222 CG CD CE NZ
REMARK 470 LEU B 228 CG CD1 CD2
REMARK 470 GLN B 229 CG CD OE1 NE2
REMARK 470 GLU B 230 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 O GLU A 251 O HOH A 422 1.65
REMARK 500 N GLU A 255 O HOH A 422 1.69
REMARK 500 O GLU A 90 O HOH A 421 1.99
REMARK 500 O ARG B 194 NE2 GLN B 198 2.00
REMARK 500 OH TYR A 177 O HOH A 448 2.03
REMARK 500 O GLU A 149 OG1 THR A 153 2.07
REMARK 500 OE1 GLU B 247 O HOH B 409 2.08
REMARK 500 O TRP A 48 O HOH A 430 2.13
REMARK 500 O LYS B 42 O HOH B 430 2.15
REMARK 500 OE2 GLU A 145 O HOH A 428 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 O HOH A 429 O HOH B 436 3655 2.02
REMARK 500 NE2 GLN A 83 O HOH A 416 4564 2.11
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 GLU A 230 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 ARG B 194 CB - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG B 194 N - CA - C ANGL. DEV. = -22.0 DEGREES
REMARK 500 THR B 220 CB - CA - C ANGL. DEV. = -25.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 88 82.69 -155.19
REMARK 500 ARG A 128 178.49 64.79
REMARK 500 ARG A 134 -62.57 -90.36
REMARK 500 ILE A 136 -61.16 -122.43
REMARK 500 PRO A 201 -173.90 -56.99
REMARK 500 TYR A 204 -70.05 -50.32
REMARK 500 LEU A 217 -55.51 -125.38
REMARK 500 ALA B 31 15.75 58.73
REMARK 500 SER B 59 37.22 -89.45
REMARK 500 THR B 72 -167.26 -103.09
REMARK 500 LYS B 88 77.91 -157.23
REMARK 500 ARG B 128 174.24 63.58
REMARK 500 ILE B 200 125.41 -36.85
REMARK 500 LEU B 216 -63.33 -98.37
REMARK 500 LYS B 245 72.77 -162.75
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 2Y1 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2Y1 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Q18 RELATED DB: PDB
REMARK 900 RELATED ID: 4Q19 RELATED DB: PDB
REMARK 900 RELATED ID: 4Q1A RELATED DB: PDB
REMARK 900 RELATED ID: 4Q1B RELATED DB: PDB
REMARK 900 RELATED ID: 4Q1C RELATED DB: PDB
REMARK 900 RELATED ID: 4Q1E RELATED DB: PDB
REMARK 900 RELATED ID: 4Q1F RELATED DB: PDB
DBREF 4Q1D A 1 260 UNP P27707 DCK_HUMAN 1 260
DBREF 4Q1D B 1 260 UNP P27707 DCK_HUMAN 1 260
SEQADV 4Q1D MET A -19 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D GLY A -18 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER A -17 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER A -16 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS A -15 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS A -14 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS A -13 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS A -12 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS A -11 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS A -10 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER A -9 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER A -8 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D GLY A -7 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D LEU A -6 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D VAL A -5 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D PRO A -4 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D ARG A -3 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D GLY A -2 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER A -1 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS A 0 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER A 9 UNP P27707 CYS 9 ENGINEERED MUTATION
SEQADV 4Q1D SER A 45 UNP P27707 CYS 45 ENGINEERED MUTATION
SEQADV 4Q1D SER A 59 UNP P27707 CYS 59 ENGINEERED MUTATION
SEQADV 4Q1D GLU A 74 UNP P27707 SER 74 ENGINEERED MUTATION
SEQADV 4Q1D SER A 146 UNP P27707 CYS 146 ENGINEERED MUTATION
SEQADV 4Q1D MET B -19 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D GLY B -18 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER B -17 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER B -16 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS B -15 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS B -14 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS B -13 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS B -12 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS B -11 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS B -10 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER B -9 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER B -8 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D GLY B -7 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D LEU B -6 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D VAL B -5 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D PRO B -4 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D ARG B -3 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D GLY B -2 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER B -1 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D HIS B 0 UNP P27707 EXPRESSION TAG
SEQADV 4Q1D SER B 9 UNP P27707 CYS 9 ENGINEERED MUTATION
SEQADV 4Q1D SER B 45 UNP P27707 CYS 45 ENGINEERED MUTATION
SEQADV 4Q1D SER B 59 UNP P27707 CYS 59 ENGINEERED MUTATION
SEQADV 4Q1D GLU B 74 UNP P27707 SER 74 ENGINEERED MUTATION
SEQADV 4Q1D SER B 146 UNP P27707 CYS 146 ENGINEERED MUTATION
SEQRES 1 A 280 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 280 LEU VAL PRO ARG GLY SER HIS MET ALA THR PRO PRO LYS
SEQRES 3 A 280 ARG SER SER PRO SER PHE SER ALA SER SER GLU GLY THR
SEQRES 4 A 280 ARG ILE LYS LYS ILE SER ILE GLU GLY ASN ILE ALA ALA
SEQRES 5 A 280 GLY LYS SER THR PHE VAL ASN ILE LEU LYS GLN LEU SER
SEQRES 6 A 280 GLU ASP TRP GLU VAL VAL PRO GLU PRO VAL ALA ARG TRP
SEQRES 7 A 280 SER ASN VAL GLN SER THR GLN ASP GLU PHE GLU GLU LEU
SEQRES 8 A 280 THR MET GLU GLN LYS ASN GLY GLY ASN VAL LEU GLN MET
SEQRES 9 A 280 MET TYR GLU LYS PRO GLU ARG TRP SER PHE THR PHE GLN
SEQRES 10 A 280 THR TYR ALA CYS LEU SER ARG ILE ARG ALA GLN LEU ALA
SEQRES 11 A 280 SER LEU ASN GLY LYS LEU LYS ASP ALA GLU LYS PRO VAL
SEQRES 12 A 280 LEU PHE PHE GLU ARG SER VAL TYR SER ASP ARG TYR ILE
SEQRES 13 A 280 PHE ALA SER ASN LEU TYR GLU SER GLU SER MET ASN GLU
SEQRES 14 A 280 THR GLU TRP THR ILE TYR GLN ASP TRP HIS ASP TRP MET
SEQRES 15 A 280 ASN ASN GLN PHE GLY GLN SER LEU GLU LEU ASP GLY ILE
SEQRES 16 A 280 ILE TYR LEU GLN ALA THR PRO GLU THR CYS LEU HIS ARG
SEQRES 17 A 280 ILE TYR LEU ARG GLY ARG ASN GLU GLU GLN GLY ILE PRO
SEQRES 18 A 280 LEU GLU TYR LEU GLU LYS LEU HIS TYR LYS HIS GLU SER
SEQRES 19 A 280 TRP LEU LEU HIS ARG THR LEU LYS THR ASN PHE ASP TYR
SEQRES 20 A 280 LEU GLN GLU VAL PRO ILE LEU THR LEU ASP VAL ASN GLU
SEQRES 21 A 280 ASP PHE LYS ASP LYS TYR GLU SER LEU VAL GLU LYS VAL
SEQRES 22 A 280 LYS GLU PHE LEU SER THR LEU
SEQRES 1 B 280 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 280 LEU VAL PRO ARG GLY SER HIS MET ALA THR PRO PRO LYS
SEQRES 3 B 280 ARG SER SER PRO SER PHE SER ALA SER SER GLU GLY THR
SEQRES 4 B 280 ARG ILE LYS LYS ILE SER ILE GLU GLY ASN ILE ALA ALA
SEQRES 5 B 280 GLY LYS SER THR PHE VAL ASN ILE LEU LYS GLN LEU SER
SEQRES 6 B 280 GLU ASP TRP GLU VAL VAL PRO GLU PRO VAL ALA ARG TRP
SEQRES 7 B 280 SER ASN VAL GLN SER THR GLN ASP GLU PHE GLU GLU LEU
SEQRES 8 B 280 THR MET GLU GLN LYS ASN GLY GLY ASN VAL LEU GLN MET
SEQRES 9 B 280 MET TYR GLU LYS PRO GLU ARG TRP SER PHE THR PHE GLN
SEQRES 10 B 280 THR TYR ALA CYS LEU SER ARG ILE ARG ALA GLN LEU ALA
SEQRES 11 B 280 SER LEU ASN GLY LYS LEU LYS ASP ALA GLU LYS PRO VAL
SEQRES 12 B 280 LEU PHE PHE GLU ARG SER VAL TYR SER ASP ARG TYR ILE
SEQRES 13 B 280 PHE ALA SER ASN LEU TYR GLU SER GLU SER MET ASN GLU
SEQRES 14 B 280 THR GLU TRP THR ILE TYR GLN ASP TRP HIS ASP TRP MET
SEQRES 15 B 280 ASN ASN GLN PHE GLY GLN SER LEU GLU LEU ASP GLY ILE
SEQRES 16 B 280 ILE TYR LEU GLN ALA THR PRO GLU THR CYS LEU HIS ARG
SEQRES 17 B 280 ILE TYR LEU ARG GLY ARG ASN GLU GLU GLN GLY ILE PRO
SEQRES 18 B 280 LEU GLU TYR LEU GLU LYS LEU HIS TYR LYS HIS GLU SER
SEQRES 19 B 280 TRP LEU LEU HIS ARG THR LEU LYS THR ASN PHE ASP TYR
SEQRES 20 B 280 LEU GLN GLU VAL PRO ILE LEU THR LEU ASP VAL ASN GLU
SEQRES 21 B 280 ASP PHE LYS ASP LYS TYR GLU SER LEU VAL GLU LYS VAL
SEQRES 22 B 280 LYS GLU PHE LEU SER THR LEU
HET 2Y1 A 301 31
HET UDP A 302 25
HET 2Y1 B 301 31
HET UDP B 302 25
HETNAM 2Y1 (R)-2-((1-(2-(3-(2-FLUOROETHOXY)-4-METHOXYPHENYL)-5-
HETNAM 2 2Y1 PROPYLTHIAZOL-4-YL)ETHYL)THIO)PYRIMIDINE-4,6-DIAMINE
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETSYN 2Y1 2-{[(1R)-1-{2-[3-(2-FLUOROETHOXY)-4-METHOXYPHENYL]-5-
HETSYN 2 2Y1 PROPYL-1,3-THIAZOL-4-YL}ETHYL]SULFANYL}PYRIMIDINE-4,6-
HETSYN 3 2Y1 DIAMINE
FORMUL 3 2Y1 2(C21 H26 F N5 O2 S2)
FORMUL 4 UDP 2(C9 H14 N2 O12 P2)
FORMUL 7 HOH *92(H2 O)
HELIX 1 1 GLY A 33 GLN A 43 1 11
HELIX 2 2 GLU A 53 SER A 59 1 7
HELIX 3 3 THR A 72 LYS A 88 1 17
HELIX 4 4 LYS A 88 LEU A 112 1 25
HELIX 5 5 SER A 129 ILE A 136 1 8
HELIX 6 6 ILE A 136 SER A 144 1 9
HELIX 7 7 ASN A 148 PHE A 166 1 19
HELIX 8 8 GLY A 167 GLU A 171 5 5
HELIX 9 9 THR A 181 GLY A 193 1 13
HELIX 10 10 ASN A 195 ILE A 200 5 6
HELIX 11 11 LEU A 202 LEU A 217 1 16
HELIX 12 12 PHE A 225 GLU A 230 5 6
HELIX 13 13 TYR A 246 THR A 259 1 14
HELIX 14 14 GLY B 33 GLN B 43 1 11
HELIX 15 15 GLU B 53 TRP B 58 1 6
HELIX 16 16 THR B 72 LYS B 88 1 17
HELIX 17 17 LYS B 88 ASN B 113 1 26
HELIX 18 18 SER B 129 ILE B 136 1 8
HELIX 19 19 ILE B 136 SER B 144 1 9
HELIX 20 20 ASN B 148 ASN B 164 1 17
HELIX 21 21 THR B 181 GLY B 193 1 13
HELIX 22 22 ARG B 194 ILE B 200 1 7
HELIX 23 23 PRO B 201 LEU B 216 1 16
HELIX 24 24 PHE B 225 GLU B 230 5 6
HELIX 25 25 ASP B 241 LYS B 245 5 5
HELIX 26 26 TYR B 246 THR B 259 1 14
SHEET 1 A 5 TRP A 48 VAL A 51 0
SHEET 2 A 5 VAL A 123 GLU A 127 1 O PHE A 125 N GLU A 49
SHEET 3 A 5 LYS A 22 GLU A 27 1 N ILE A 24 O PHE A 126
SHEET 4 A 5 GLY A 174 GLN A 179 1 O ILE A 176 N SER A 25
SHEET 5 A 5 ILE A 233 ASP A 237 1 O LEU A 236 N TYR A 177
SHEET 1 B 5 TRP B 48 VAL B 51 0
SHEET 2 B 5 VAL B 123 GLU B 127 1 O PHE B 125 N GLU B 49
SHEET 3 B 5 LYS B 22 GLY B 28 1 N LYS B 22 O LEU B 124
SHEET 4 B 5 GLY B 174 GLN B 179 1 O ILE B 176 N GLU B 27
SHEET 5 B 5 ILE B 233 ASP B 237 1 O LEU B 234 N TYR B 177
SITE 1 AC1 14 GLU A 53 VAL A 55 LEU A 82 MET A 85
SITE 2 AC1 14 TYR A 86 PRO A 89 GLN A 97 ARG A 128
SITE 3 AC1 14 ASP A 133 PHE A 137 LEU A 141 SER A 144
SITE 4 AC1 14 SER A 146 TYR A 204
SITE 1 AC2 12 ALA A 31 ALA A 32 GLY A 33 LYS A 34
SITE 2 AC2 12 SER A 35 THR A 36 ARG A 188 ARG A 192
SITE 3 AC2 12 ASP A 241 PHE A 242 HOH A 412 HOH A 435
SITE 1 AC3 14 ILE B 30 GLU B 53 VAL B 55 LEU B 82
SITE 2 AC3 14 MET B 85 TYR B 86 PRO B 89 PHE B 96
SITE 3 AC3 14 GLN B 97 ARG B 128 ASP B 133 PHE B 137
SITE 4 AC3 14 SER B 144 TYR B 204
SITE 1 AC4 15 ASN B 29 ALA B 31 ALA B 32 GLY B 33
SITE 2 AC4 15 LYS B 34 SER B 35 THR B 36 GLU B 127
SITE 3 AC4 15 ARG B 188 ARG B 192 ASP B 241 PHE B 242
SITE 4 AC4 15 LYS B 243 HOH B 412 HOH B 434
CRYST1 68.734 68.734 120.623 90.00 90.00 90.00 P 41 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 0.014549 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014549 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008290 0.00000
(ATOM LINES ARE NOT SHOWN.)
END