HEADER TRANSFERASE 12-JUL-10 3AKC
TITLE CRYSTAL STRUCTURE OF CMP KINASE IN COMPLEX WITH CDP AND ADP FROM
TITLE 2 THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTIDYLATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CK, CYTIDINE MONOPHOSPHATE KINASE, CMP KINASE;
COMPND 5 EC: 2.7.4.14;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: TTHA0458;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS CMP KINASE, CDP AND ADP COMPLEX, CLOSED CONFORMATION, NUCLEOTIDE
KEYWDS 2 METABOLISM, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MEGA,N.NAKAGAWA,S.KURAMITSU,R.MASUI
REVDAT 2 01-NOV-23 3AKC 1 REMARK LINK
REVDAT 1 06-JUL-11 3AKC 0
JRNL AUTH R.MEGA,N.NAKAGAWA,S.KURAMITSU,R.MASUI
JRNL TITL THE CRYSTAL STRUCTURE OF THE TERTIARY COMPLEX OF CMP KINASE
JRNL TITL 2 WITH A PHOSPHORYL GROUP ACCEPTOR AND A DONOR FROM THERMUS
JRNL TITL 3 THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1483992.760
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 28577
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 SET) : 0.199
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2839
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3936
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 434
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1591
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.49000
REMARK 3 B22 (A**2) : 4.49000
REMARK 3 B33 (A**2) : -8.98000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 2.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 3.540
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 43.96
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CDP.PARAM
REMARK 3 PARAMETER FILE 3 : ADP.PARAM
REMARK 3 PARAMETER FILE 4 : WATER.PARAM
REMARK 3 PARAMETER FILE 5 : GD3+.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CDP.TOP
REMARK 3 TOPOLOGY FILE 3 : ADP.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER.TOP
REMARK 3 TOPOLOGY FILE 5 : GD3+.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3AKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000029358.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL45XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : TRANSPARENT DIAMOND DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28624
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.28700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: ARP/WARP 7.1
REMARK 200 STARTING MODEL: PDB ENTRY 2CMK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PROPANE, 3.5M SODIUM
REMARK 280 FORMATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.96733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.98367
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 55.47550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 18.49183
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 92.45917
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD A 211 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 16 OG
REMARK 620 2 CDP A 209 O2B 139.2
REMARK 620 3 ADP A 210 O3B 76.9 99.9
REMARK 620 4 ADP A 210 O2A 84.7 132.9 69.2
REMARK 620 5 ADP A 210 O2B 128.7 69.1 53.2 68.3
REMARK 620 6 HOH A 218 O 62.6 76.9 76.9 137.4 110.3
REMARK 620 7 HOH A 223 O 137.1 78.4 124.7 72.8 76.2 149.8
REMARK 620 8 HOH A 226 O 71.5 127.7 131.8 72.5 132.4 116.8 67.1
REMARK 620 9 HOH A 269 O 93.0 67.9 147.8 141.1 135.2 71.4 83.4 70.1
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDP A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GD A 211
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AKD RELATED DB: PDB
REMARK 900 RELATED ID: 3AKE RELATED DB: PDB
DBREF 3AKC A 1 208 UNP Q5SL35 KCY_THET8 1 208
SEQRES 1 A 208 MET ARG GLY ILE VAL THR ILE ASP GLY PRO SER ALA SER
SEQRES 2 A 208 GLY LYS SER SER VAL ALA ARG ARG VAL ALA ALA ALA LEU
SEQRES 3 A 208 GLY VAL PRO TYR LEU SER SER GLY LEU LEU TYR ARG ALA
SEQRES 4 A 208 ALA ALA PHE LEU ALA LEU ARG ALA GLY VAL ASP PRO GLY
SEQRES 5 A 208 ASP GLU GLU GLY LEU LEU ALA LEU LEU GLU GLY LEU GLY
SEQRES 6 A 208 VAL ARG LEU LEU ALA GLN ALA GLU GLY ASN ARG VAL LEU
SEQRES 7 A 208 ALA ASP GLY GLU ASP LEU THR SER PHE LEU HIS THR PRO
SEQRES 8 A 208 GLU VAL ASP ARG VAL VAL SER ALA VAL ALA ARG LEU PRO
SEQRES 9 A 208 GLY VAL ARG ALA TRP VAL ASN ARG ARG LEU LYS GLU VAL
SEQRES 10 A 208 PRO PRO PRO PHE VAL ALA GLU GLY ARG ASP MET GLY THR
SEQRES 11 A 208 ALA VAL PHE PRO GLU ALA ALA HIS LYS PHE TYR LEU THR
SEQRES 12 A 208 ALA SER PRO GLU VAL ARG ALA TRP ARG ARG ALA ARG GLU
SEQRES 13 A 208 ARG PRO GLN ALA TYR GLU GLU VAL LEU ARG ASP LEU LEU
SEQRES 14 A 208 ARG ARG ASP GLU ARG ASP LYS ALA GLN SER ALA PRO ALA
SEQRES 15 A 208 PRO ASP ALA LEU VAL LEU ASP THR GLY GLY MET THR LEU
SEQRES 16 A 208 ASP GLU VAL VAL ALA TRP VAL LEU ALA HIS ILE ARG ARG
HET CDP A 209 25
HET ADP A 210 27
HET GD A 211 1
HETNAM CDP CYTIDINE-5'-DIPHOSPHATE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM GD GADOLINIUM ATOM
FORMUL 2 CDP C9 H15 N3 O11 P2
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 GD GD
FORMUL 5 HOH *116(H2 O)
HELIX 1 1 GLY A 14 GLY A 27 1 14
HELIX 2 2 SER A 33 GLY A 48 1 16
HELIX 3 3 ASP A 53 GLY A 65 1 13
HELIX 4 4 THR A 85 LEU A 88 5 4
HELIX 5 5 THR A 90 ARG A 102 1 13
HELIX 6 6 LEU A 103 GLU A 116 1 14
HELIX 7 7 SER A 145 ARG A 155 1 11
HELIX 8 8 ALA A 160 ASP A 175 1 16
HELIX 9 9 LYS A 176 SER A 179 5 4
HELIX 10 10 THR A 194 ARG A 207 1 14
SHEET 1 A 5 TYR A 30 SER A 32 0
SHEET 2 A 5 PHE A 121 GLY A 125 1 O GLU A 124 N LEU A 31
SHEET 3 A 5 ILE A 4 ASP A 8 1 N VAL A 5 O ALA A 123
SHEET 4 A 5 HIS A 138 THR A 143 1 O LEU A 142 N ASP A 8
SHEET 5 A 5 LEU A 186 ASP A 189 1 O LEU A 186 N TYR A 141
SHEET 1 B 3 VAL A 66 LEU A 69 0
SHEET 2 B 3 ARG A 76 ALA A 79 -1 O ARG A 76 N LEU A 69
SHEET 3 B 3 GLU A 82 ASP A 83 -1 O GLU A 82 N ALA A 79
LINK OG SER A 16 GD GD A 211 1555 1555 2.40
LINK O2B CDP A 209 GD GD A 211 1555 1555 2.37
LINK O3B ADP A 210 GD GD A 211 1555 1555 2.43
LINK O2A ADP A 210 GD GD A 211 1555 1555 2.59
LINK O2B ADP A 210 GD GD A 211 1555 1555 2.96
LINK GD GD A 211 O HOH A 218 1555 1555 2.47
LINK GD GD A 211 O HOH A 223 1555 1555 2.43
LINK GD GD A 211 O HOH A 226 1555 1555 2.48
LINK GD GD A 211 O HOH A 269 1555 1555 2.41
CISPEP 1 PRO A 119 PRO A 120 0 0.67
SITE 1 AC1 21 SER A 11 LYS A 15 SER A 33 GLY A 34
SITE 2 AC1 21 TYR A 37 ARG A 38 VAL A 97 ALA A 101
SITE 3 AC1 21 ARG A 107 ARG A 126 ASP A 127 ARG A 153
SITE 4 AC1 21 ARG A 171 ASP A 175 GLN A 178 ADP A 210
SITE 5 AC1 21 GD A 211 HOH A 218 HOH A 219 HOH A 223
SITE 6 AC1 21 HOH A 269
SITE 1 AC2 24 PRO A 10 ALA A 12 SER A 13 GLY A 14
SITE 2 AC2 24 LYS A 15 SER A 16 SER A 17 ASP A 80
SITE 3 AC2 24 GLU A 82 ARG A 152 ARG A 153 ARG A 155
SITE 4 AC2 24 GLU A 156 MET A 193 THR A 194 LEU A 195
SITE 5 AC2 24 CDP A 209 GD A 211 HOH A 218 HOH A 223
SITE 6 AC2 24 HOH A 226 HOH A 247 HOH A 256 HOH A 257
SITE 1 AC3 7 SER A 16 CDP A 209 ADP A 210 HOH A 218
SITE 2 AC3 7 HOH A 223 HOH A 226 HOH A 269
CRYST1 62.206 62.206 110.951 90.00 90.00 120.00 P 65 6
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 0.016076 0.009281 0.000000 0.00000
SCALE2 0.000000 0.018563 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009013 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
