HEADER TRANSFERASE 12-SEP-03 1UNQ
TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
TITLE 2 PROTEIN KINASE B/AKT BOUND TO INS(1,3,4,5)-TETRAKISPHOPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAC-ALPHA SERINE/THREONINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PLECKSTRIN HOMOLOGY DOMAIN RESIDUES 1-123;
COMPND 5 SYNONYM: PROTEIN KINASE B, RAC-PK-ALPHA, PKB, C-AKT;
COMPND 6 EC: 2.7.1.-;
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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1
KEYWDS TRANSFERASE, PLECKSTRIN HOMOLOGY DOMAIN, PKB, AKT, PHOSPHOINOSITIDE,
KEYWDS 2 SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING, PHOSPHORYLATION,
KEYWDS 3 NUCLEAR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.C.MILBURN,M.DEAK,S.M.KELLY,N.C.PRICE,D.R.ALESSI,D.M.F.VAN AALTEN
REVDAT 4 13-DEC-23 1UNQ 1 LINK
REVDAT 3 28-FEB-18 1UNQ 1 SOURCE AUTHOR JRNL
REVDAT 2 24-FEB-09 1UNQ 1 VERSN
REVDAT 1 16-SEP-04 1UNQ 0
JRNL AUTH C.C.MILBURN,M.DEAK,S.M.KELLY,N.C.PRICE,D.R.ALESSI,
JRNL AUTH 2 D.M.VAN AALTEN
JRNL TITL BINDING OF PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE TO THE
JRNL TITL 2 PLECKSTRIN HOMOLOGY DOMAIN OF PROTEIN KINASE B INDUCES A
JRNL TITL 3 CONFORMATIONAL CHANGE.
JRNL REF BIOCHEM. J. V. 375 531 2003
JRNL REFN ESSN 1470-8728
JRNL PMID 12964941
JRNL DOI 10.1042/BJ20031229
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.C.MILBURN,M.DEAK,D.R.ALESSI,D.M.F.VAN AALTEN
REMARK 1 TITL HIGH RESOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN
REMARK 1 TITL 2 OF PROTEIN KINASE B/AKT BOUND TO PHOSPHATIDYLINOSITOL
REMARK 1 TITL 3 (3,4,5)-TRISPHOSPHATE
REMARK 1 REF CURR.BIOL. V. 12 1256 2002
REMARK 1 REFN ISSN 0960-9822
REMARK 1 PMID 12176338
REMARK 1 DOI 10.1016/S0960-9822(02)00972-7
REMARK 2
REMARK 2 RESOLUTION. 0.98 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) : 0.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.151
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.154
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2429
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 60005
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.142
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)) : 46229
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 985
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1167.5
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 961.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 10
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 10871
REMARK 3 NUMBER OF RESTRAINTS : 13466
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.066
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.078
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.068
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.050
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.077
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UNQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1290013513.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.920177
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60005
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.980
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.55700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1H10
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M AMMONIUM ACETATE, 30 % PEG
REMARK 280 4000, 0.1 M SODIUM ACETATE (4.6), PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 41.45200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 17.19400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.45200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 17.19400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: PQS
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2055 LIES ON A SPECIAL POSITION.
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 118
REMARK 465 ASP A 119
REMARK 465 PHE A 120
REMARK 465 ARG A 121
REMARK 465 SER A 122
REMARK 465 GLY A 123
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 A 117 CA C O CB CG CD OE1
REMARK 470 GLU A 117 OE2
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 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 67 NE - CZ - NH2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 69 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 69 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 76 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 76 NE - CZ - NH1 ANGL. DEV. = 7.8 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 TRP A 80 -93.40 62.67
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 4IP A1117
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H10 RELATED DB: PDB
REMARK 900 HIGH RESOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
REMARK 900 PROTEIN KINASE B/AKT BOUND TO INS(1,3,4,5)-TETRAKISPHOPHATE
REMARK 900 RELATED ID: 1UNP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF PKB ALPHA
REMARK 900 RELATED ID: 1UNR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PH DOMAIN OF PKB ALPHA IN COMPLEX WITH A
REMARK 900 SULFATE MOLECULE
DBREF 1UNQ A -1 0 PDB 1UNQ 1UNQ -1 0
DBREF 1UNQ A 1 123 UNP P31749 KRAC_HUMAN 1 123
SEQRES 1 A 125 ACE SER MET SER ASP VAL ALA ILE VAL LYS GLU GLY TRP
SEQRES 2 A 125 LEU HIS LYS ARG GLY GLU TYR ILE LYS THR TRP ARG PRO
SEQRES 3 A 125 ARG TYR PHE LEU LEU LYS ASN ASP GLY THR PHE ILE GLY
SEQRES 4 A 125 TYR LYS GLU ARG PRO GLN ASP VAL ASP GLN ARG GLU ALA
SEQRES 5 A 125 PRO LEU ASN ASN PHE SER VAL ALA GLN CYS GLN LEU MET
SEQRES 6 A 125 LYS THR GLU ARG PRO ARG PRO ASN THR PHE ILE ILE ARG
SEQRES 7 A 125 CYS LEU GLN TRP THR THR VAL ILE GLU ARG THR PHE HIS
SEQRES 8 A 125 VAL GLU THR PRO GLU GLU ARG GLU GLU TRP THR THR ALA
SEQRES 9 A 125 ILE GLN THR VAL ALA ASP GLY LEU LYS LYS GLN GLU GLU
SEQRES 10 A 125 GLU GLU MET ASP PHE ARG SER GLY
HET ACE A -1 3
HET 4IP A1117 28
HETNAM ACE ACETYL GROUP
HETNAM 4IP INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE
FORMUL 1 ACE C2 H4 O
FORMUL 2 4IP C6 H16 O18 P4
FORMUL 3 HOH *155(H2 O)
HELIX 1 1 MET A 1 VAL A 4 5 4
HELIX 2 2 ASP A 44 GLU A 49 1 6
HELIX 3 3 THR A 92 GLU A 116 1 25
SHEET 1 AA 7 ASN A 53 SER A 56 0
SHEET 2 AA 7 THR A 34 TYR A 38 -1 O PHE A 35 N PHE A 55
SHEET 3 AA 7 TRP A 22 LYS A 30 -1 O TYR A 26 N TYR A 38
SHEET 4 AA 7 ILE A 6 ARG A 15 -1 N VAL A 7 O LEU A 29
SHEET 5 AA 7 THR A 82 HIS A 89 -1 O THR A 87 N ARG A 15
SHEET 6 AA 7 THR A 72 GLN A 79 -1 O PHE A 73 N PHE A 88
SHEET 7 AA 7 GLN A 61 THR A 65 -1 O GLN A 61 N ARG A 76
LINK C ACE A -1 N SER A 0 1555 1555 1.33
CISPEP 1 ARG A 67 PRO A 68 0 7.76
SITE 1 AC1 28 ACE A -1 SER A 0 MET A 1 SER A 2
SITE 2 AC1 28 HIS A 13 LYS A 14 GLY A 16 GLU A 17
SITE 3 AC1 28 TYR A 18 ILE A 19 ARG A 23 ARG A 25
SITE 4 AC1 28 LEU A 52 ASN A 53 PHE A 55 ARG A 86
SITE 5 AC1 28 HOH A2007 HOH A2105 HOH A2146 HOH A2147
SITE 6 AC1 28 HOH A2148 HOH A2149 HOH A2150 HOH A2151
SITE 7 AC1 28 HOH A2152 HOH A2153 HOH A2154 HOH A2155
CRYST1 82.904 34.388 44.292 90.00 115.29 90.00 C 1 2 1 4
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 0.012062 0.000000 0.005699 0.00000
SCALE2 0.000000 0.029080 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024971 0.00000
HETATM 1 C ACE A -1 25.842 13.738 -11.519 1.00 14.57 C
ANISOU 1 C ACE A -1 1596 2356 1583 -446 162 141 C
HETATM 2 O ACE A -1 25.616 13.709 -10.308 1.00 19.54 O
ANISOU 2 O ACE A -1 2186 3548 1689 -1087 329 171 O
HETATM 3 CH3 ACE A -1 27.218 13.295 -12.006 1.00 17.56 C
ANISOU 3 CH3 ACE A -1 2058 2378 2236 311 189 237 C
(ATOM LINES ARE NOT SHOWN.)
END