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HEADER HYDROLASE 15-DEC-00 1HQD
TITLE PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE
TITLE 2 ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE
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 CEPACIA LIPASE (LPS AW 02513)
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
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LUIC,S.TOMIC,I.LESCIC,E.LJUBOVIC,D.SEPAC,V.SUNJIC,
AUTHOR 2 L.VITALE,W.SAENGER,B.KOJIC-PRODIC
REVDAT 1 22-AUG-01 1HQD 0
JRNL AUTH M.LUIC,S.TOMIC,I.LESCIC,E.LJUBOVIC,D.SEPAC,
JRNL AUTH 2 V.SUNJIC,L.VITALE,W.SAENGER,B.KOJIC-PRODIC
JRNL TITL COMPLEX OF BURKHOLDERIA CEPACIA LIPASE WITH
JRNL TITL 2 TRANSITION STATE ANALOGUE OF
JRNL TITL 3 1-PHENOXY-2-ACETOXYBUTANE, BIOCATALYTIC,
JRNL TITL 4 STRUCTURAL AND MODELLING STUDY
JRNL REF EUR.J.BIOCHEM. V. 268 3964 2001
JRNL REFN ASTM EJBCAI IX ISSN 0014-2956
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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 : ENG & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 12797
REMARK 3
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) : 0.154
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1320
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1818
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE : 0.2300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 231
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2338
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 288
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 2.78000
REMARK 3 B33 (A**2) : -2.85000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.22000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.13
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.68
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) : 0.69 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.09 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.11 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.52 ; 2.500
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.49
REMARK 3 BSOL : 93.32
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 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PROTEIN.LINK
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : PROST.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HQD COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-2001.
REMARK 100 THE RCSB ID CODE IS RCSB012515.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-1999
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.4; 8.6
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 : YALE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12973
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 5.60000
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 5.60000
REMARK 200 FOR SHELL : 5.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY CODE 3LIP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-45 % (V/V) MPD, 100 MM
REMARK 280 SODIUM CITRATE, 100 MM HEPES
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 44.53000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.31500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.53000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.31500
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 1 CA ALA A 1 N 0.029
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR A 20 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 GLY A 41 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 THR A 43 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 SER A 54 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 PRO A 216 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ILE A 232 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 LEU A 234 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 VAL A 235 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 GLY A 261 N - CA - C ANGL. DEV. = -7.2 DEGREES
REMARK 500 ASN A 285 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 HIS A 286 N - CA - C ANGL. DEV. = 7.2 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 LEU A 234 -56.20 72.54
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
DBREF 1HQD A 1 320 SWS P22088 LIP_BURSE 45 364
SEQADV 1HQD ASP A 2 SWS P22088 ALA 46 CONFLICT
SEQADV 1HQD ASN A 3 SWS P22088 GLY 47 CONFLICT
SEQADV 1HQD THR A 18 SWS P22088 SER 62 CONFLICT
SEQADV 1HQD ARG A 40 SWS P22088 ASN 84 CONFLICT
SEQADV 1HQD THR A 92 SWS P22088 SER 136 CONFLICT
SEQADV 1HQD GLY A 125 SWS P22088 ASP 169 CONFLICT
SEQADV 1HQD THR A 137 SWS P22088 SER 181 CONFLICT
SEQADV 1HQD ASN A 154 SWS P22088 HIS 198 CONFLICT
SEQADV 1HQD LYS A 165 SWS P22088 GLN 209 CONFLICT
SEQADV 1HQD GLN A 171 SWS P22088 ARG 215 CONFLICT
SEQADV 1HQD ILE A 218 SWS P22088 LEU 262 CONFLICT
SEQADV 1HQD ILE A 232 SWS P22088 LEU 276 CONFLICT
SEQADV 1HQD ALA A 240 SWS P22088 VAL 284 CONFLICT
SEQADV 1HQD PRO A 243 SWS P22088 LEU 287 CONFLICT
SEQADV 1HQD VAL A 256 SWS P22088 ILE 300 CONFLICT
SEQADV 1HQD VAL A 266 SWS P22088 LEU 310 CONFLICT
SEQADV 1HQD GLN A 276 SWS P22088 LYS 320 CONFLICT
SEQADV 1HQD ASN A 300 SWS 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 INK A 612 15
HETNAM CA CALCIUM ION
HETNAM INK (RP,SP)-O-(2R)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC
HETNAM 2 INK ACID CHLORIDE
FORMUL 2 CA CA1 2+
FORMUL 3 INK C11 H16 O3 CL1 P1
FORMUL 4 HOH *288(H2 O1)
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 SER A 268 LEU A 273 1 6
HELIX 12 12 LEU A 287 ASN A 291 5 5
HELIX 13 13 ASP A 303 GLY A 319 1 17
SHEET 1 A 6 GLN A 276 TYR A 282 0
SHEET 2 A 6 ASN A 202 GLY A 211 1 O LEU A 206 N GLN A 276
SHEET 3 A 6 VAL A 104 ILE A 110 1 O ALA A 105 N LEU A 205
SHEET 4 A 6 VAL A 81 HIS A 86 1 O VAL A 81 N ALA A 105
SHEET 5 A 6 ILE A 11 VAL A 14 1 O ILE A 12 N VAL A 84
SHEET 6 A 6 VAL A 44 VAL A 46 1 N TYR A 45 O ILE A 11
SHEET 1 B 3 GLN A 276 TYR A 282 0
SHEET 2 B 3 ASN A 202 GLY A 211 1 O LEU A 206 N GLN A 276
SHEET 3 B 3 THR A 196 VAL A 199 -1 O GLU A 197 N HIS A 204
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 VAL A 223 N VAL A 220
SSBOND 1 CYS A 190 CYS A 270
LINK OG SER A 87 P INK A 612
CISPEP 1 GLN A 292 LEU A 293 0 -0.15
CRYST1 89.060 46.630 84.300 90.00 120.86 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 0.011228 0.000000 0.006709 0.00000
SCALE2 0.000000 0.021445 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013819 0.00000
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