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HEADER HYDROLASE 14-NOV-06 2NW6
TITLE BURKHOLDERIA CEPACIA LIPASE COMPLEXED WITH S-INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CEPACIA;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 OTHER_DETAILS: THE ENZYME SOURCE WAS A COMMERCIAL
SOURCE 5 PREPARATION OF PSEUDOMONAS (BURKHOLDERIA) CEPACIA LIPASE
SOURCE 6 OBTAINED FROM AMANO PHARMACEUTICALS CO., NAGOYA, JAPAN.
KEYWDS PSEUDOMONAS CEPACIA LIPASE, RACEMIC SEC ALCOHOLS,
KEYWDS 2 TRANSITION STATE (TS) ANALOGUE, CRYSTAL STRUCTURE,
KEYWDS 3 MOLECULAR MODELLING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LUIC,Z.STEFANIC
REVDAT 1 04-DEC-07 2NW6 0
JRNL AUTH M.LUIC,S.TOMIC,I.CEILINGER,D.JANEZIC,M.HODOSCEK,
JRNL AUTH 2 T.LENAC,Z.STEFANIC,D.SEPAC,I.LESCIC
JRNL TITL BURKHOLDERIA CEPACIA LIPASE COMPLEXED WITH
JRNL TITL 2 S-INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 27212
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) : 0.175
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2713
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2852
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 325
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2337
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31000
REMARK 3 B22 (A**2) : 2.93000
REMARK 3 B33 (A**2) : -3.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 63.61
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 : PROST.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NW6 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB040376.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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) : 1.542
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27385
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 23.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS TO 1HQD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1HQD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE, 40% MPD, 0.1M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 44.50750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.29200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.50750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.29200
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 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: MONOMER
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 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 VAL A 320 O
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 THR A 18 -19.21 69.70
REMARK 500 SER A 87 -130.22 57.90
REMARK 500 LEU A 234 -46.08 61.30
REMARK 500 VAL A 266 -12.73 -140.54
REMARK 500 SER A 279 147.82 -175.25
REMARK 500 LEU A 293 59.53 78.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 POT A 612
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 CA A 613 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 242 OD2
REMARK 620 2 ASP A 288 OD1 169.7
REMARK 620 3 VAL A 296 O 89.6 96.8
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LIP RELATED DB: PDB
REMARK 900 3LIP IS ISOMORPHOUS WITH THIS STRUCTURE
REMARK 900 RELATED ID: 1OIL RELATED DB: PDB
REMARK 900 1OIL IS ISOMORPHOUS WITH THIS STRUCTURE
REMARK 900 RELATED ID: 2LIP RELATED DB: PDB
REMARK 900 2LIP IS ISOMORPHOUS WITH THIS STRUCTURE
REMARK 900 RELATED ID: 4LIP RELATED DB: PDB
REMARK 900 4LIP IS ISOMORPHOUS WITH THIS STRUCTURE
REMARK 900 RELATED ID: 5LIP RELATED DB: PDB
REMARK 900 5LIP IS ISOMORPHOUS WITH THIS STRUCTURE
REMARK 900 RELATED ID: 1HQD RELATED DB: PDB
REMARK 900 1HQD AND THIS STRUCTURE ARE CRYSTAL STRUCTURES CONTAINING
REMARK 900 BOUND ENANTIOMERIC INHIBITORS
DBREF 2NW6 A 1 320 UNP P22088 LIP_BURCE 45 364
SEQADV 2NW6 ASP A 2 UNP P22088 ALA 46 CONFLICT
SEQADV 2NW6 ASN A 3 UNP P22088 GLY 47 CONFLICT
SEQADV 2NW6 THR A 18 UNP P22088 SER 62 CONFLICT
SEQADV 2NW6 ARG A 40 UNP P22088 ASN 84 CONFLICT
SEQADV 2NW6 THR A 92 UNP P22088 SER 136 CONFLICT
SEQADV 2NW6 GLY A 125 UNP P22088 ASP 169 CONFLICT
SEQADV 2NW6 THR A 137 UNP P22088 SER 181 CONFLICT
SEQADV 2NW6 ASN A 154 UNP P22088 HIS 198 CONFLICT
SEQADV 2NW6 LYS A 165 UNP P22088 GLN 209 CONFLICT
SEQADV 2NW6 GLN A 171 UNP P22088 ARG 215 CONFLICT
SEQADV 2NW6 ILE A 218 UNP P22088 LEU 262 CONFLICT
SEQADV 2NW6 ILE A 232 UNP P22088 LEU 276 CONFLICT
SEQADV 2NW6 ALA A 240 UNP P22088 VAL 284 CONFLICT
SEQADV 2NW6 PRO A 243 UNP P22088 LEU 287 CONFLICT
SEQADV 2NW6 VAL A 256 UNP P22088 ILE 300 CONFLICT
SEQADV 2NW6 VAL A 266 UNP P22088 LEU 310 CONFLICT
SEQADV 2NW6 GLN A 276 UNP P22088 LYS 320 CONFLICT
SEQADV 2NW6 ASN A 300 UNP P22088 TYR 344 CONFLICT
SEQRES 1 A 320 ALA ASP ASN TYR ALA ALA THR ARG TYR PRO ILE ILE LEU
SEQRES 2 A 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 A 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 A 320 ARG GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 A 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 A 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 A 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 A 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 A 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 A 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 A 320 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 A 320 ASN VAL PHE GLY ILE LEU THR SER SER SER ASN ASN THR
SEQRES 13 A 320 ASN GLN ASP ALA LEU ALA ALA LEU LYS THR LEU THR THR
SEQRES 14 A 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 A 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 A 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 A 320 TRP ALA GLY THR ALA ILE GLN PRO THR ILE SER VAL PHE
SEQRES 18 A 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 A 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 A 320 LEU PHE GLY THR GLY THR VAL MET VAL ASN ARG GLY SER
SEQRES 21 A 320 GLY GLN ASN ASP GLY VAL VAL SER LYS CYS SER ALA LEU
SEQRES 22 A 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 A 320 LEU ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 A 320 ASN ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 A 320 ASN ARG LEU LYS LEU ALA GLY VAL
HET CA A 613 1
HET NA A 614 1
HET POT A 612 15
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM POT (1S)-1-(PHENOXYMETHYL)PROPYL
HETNAM 2 POT METHYLPHOSPHONOCHLORIDOATE
HETSYN POT (RP,SP)-O-(2S)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC
HETSYN 2 POT ACID CHLORIDE
FORMUL 2 CA CA 2+
FORMUL 3 NA NA 1+
FORMUL 4 POT C11 H16 CL O3 P
FORMUL 5 HOH *279(H2 O)
HELIX 1 1 ALA A 24 VAL A 26 5 3
HELIX 2 2 GLY A 32 ARG A 40 1 9
HELIX 3 3 GLY A 60 GLY A 77 1 18
HELIX 4 4 SER A 87 ALA A 100 1 14
HELIX 5 5 SER A 117 TYR A 129 1 13
HELIX 6 6 GLY A 133 SER A 151 1 19
HELIX 7 7 ASP A 159 LEU A 167 1 9
HELIX 8 8 THR A 168 TYR A 179 1 12
HELIX 9 9 PRO A 237 ASP A 242 1 6
HELIX 10 10 PRO A 243 ASN A 257 1 15
HELIX 11 11 LEU A 287 ASN A 291 5 5
HELIX 12 12 ASP A 303 ALA A 318 1 16
SHEET 1 A 6 VAL A 44 VAL A 46 0
SHEET 2 A 6 ILE A 11 VAL A 14 1 N ILE A 11 O TYR A 45
SHEET 3 A 6 VAL A 81 HIS A 86 1 O VAL A 84 N VAL A 14
SHEET 4 A 6 VAL A 104 ILE A 110 1 O ALA A 105 N VAL A 81
SHEET 5 A 6 ASN A 202 GLY A 211 1 O TYR A 207 N VAL A 107
SHEET 6 A 6 THR A 196 VAL A 199 -1 N GLU A 197 O HIS A 204
SHEET 1 B 6 VAL A 44 VAL A 46 0
SHEET 2 B 6 ILE A 11 VAL A 14 1 N ILE A 11 O TYR A 45
SHEET 3 B 6 VAL A 81 HIS A 86 1 O VAL A 84 N VAL A 14
SHEET 4 B 6 VAL A 104 ILE A 110 1 O ALA A 105 N VAL A 81
SHEET 5 B 6 ASN A 202 GLY A 211 1 O TYR A 207 N VAL A 107
SHEET 6 B 6 GLN A 276 TYR A 282 1 O LEU A 278 N SER A 208
SHEET 1 C 2 LYS A 22 TYR A 23 0
SHEET 2 C 2 LEU A 27 GLU A 28 -1 O LEU A 27 N TYR A 23
SHEET 1 D 2 ILE A 214 VAL A 220 0
SHEET 2 D 2 VAL A 223 ASP A 228 -1 O GLY A 225 N ILE A 218
SSBOND 1 CYS A 190 CYS A 270 1555 1555 2.04
LINK P POT A 612 OG SER A 87 1555 1555 1.55
LINK OD2 ASP A 242 CA CA A 613 1555 1555 2.48
LINK OD1 ASP A 288 CA CA A 613 1555 1555 2.49
LINK O VAL A 296 CA CA A 613 1555 1555 2.43
CRYST1 89.015 46.584 84.244 90.00 121.05 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 0.011234 0.000000 0.006762 0.00000
SCALE2 0.000000 0.021467 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013855 0.00000
TER 2338 VAL A 320
MASTER 283 0 3 12 16 0 0 6 2633 1 22 25
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