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HEADER LIPASE 18-AUG-97 4LIP
TITLE PSEUDOMONAS LIPASE COMPLEXED WITH RC-(RP,
TITLE 2 SP)-DIBUTYLCARBAMOYLGLYCERO-3-O-BUTYLPHOSPHONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYL-GLYCEROL-HYDROLASE;
COMPND 3 CHAIN: D, E;
COMPND 4 SYNONYM: LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 BIOLOGICAL_UNIT: MONOMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;
SOURCE 3 COLLECTION: 21808;
SOURCE 4 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 5 PLASMID: PHES12;
SOURCE 6 EXPRESSION_SYSTEM: PSEUDOMONAS SP.;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 21808;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIUM;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHES12
KEYWDS LIPASE, HYDROLASE, PSEUDOMONADACEAE, COVALENT INTERMEDIATE,
KEYWDS 2 TRIGLYCERIDE ANALOGUE, ENANTIOSELECTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.LANG,B.W.DIJKSTRA
REVDAT 1 19-AUG-98 4LIP 0
JRNL AUTH D.A.LANG,M.L.M.MANNESSE,G.DE HAAS,H.M.VERHEIJ,
JRNL AUTH 2 B.W.DIJKSTRA
JRNL TITL STRUCTURAL EVIDENCE FOR THE CHIRAL REGIO
JRNL TITL 2 SELECTIVITY OF THE LIPASE FROM PSEUDOMONAS SPEC.
JRNL TITL 3 ATCC 21808
JRNL REF TO BE PUBLISHED
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.D.SCHRAG,Y.LI,M.CYGLER,D.LANG,T.BURGDORF,
REMARK 1 AUTH 2 H.J.HECHT,R.SCHMID,D.SCHOMBURG,T.J.RYDEL,
REMARK 1 AUTH 3 J.D.OLIVER,L.C.STRICKLAND,C.M.DUNAWAY,S.B.LARSON,
REMARK 1 AUTH 4 J.DAY,A.MCPHERSON
REMARK 1 TITL THE OPEN CONFORMATION OF A PSEUDOMONAS LIPASE
REMARK 1 REF STRUCTURE (LONDON) V. 5 187 1997
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.KORDEL,B.HOFMANN,D.SCHOMBURG,R.D.SCHMID
REMARK 1 TITL EXTRACELLULAR LIPASE OF PSEUDOMONAS SP. STRAIN
REMARK 1 TITL 2 ATCC 21808: PURIFICATION, CHARACTERIZATION,
REMARK 1 TITL 3 CRYSTALLIZATION, AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 4 DATA
REMARK 1 REF J.BACTERIOL. V. 173 4836 1991
REMARK 1 REFN ASTM JOBAAY US ISSN 0021-9193 0767
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.00
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 56677
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6644
REMARK 3 BIN R VALUE (WORKING SET) : 0.22
REMARK 3 BIN FREE R VALUE : 0.232
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4658
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 563
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.2
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.8
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 NCS MODEL : PARTIAL RESTRAINT
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : CCP.PRO
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : CCP.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS INITIALLY
REMARK 3 REFINED WITH STRICT NON-CRYSTALLOGRAPHIC SYMMETRY, AND
REMARK 3 THEN WITH TIGHTLY RESTRAINED NON-CRYSTALLOGRAPHIC
REMARK 3 SYMMETRY FOR ALL PARTS OF THE MOLECULE EXCEPT RESIDUES
REMARK 3 16 - 28, 127 - 159, AND 218 - 224. THE CHAINS ARE NAMED
REMARK 3 D AND E, WITH MOLECULE D AS THE REFERENCE FOR SECONDARY
REMARK 3 STRUCTURE DEFINITION. DEVIATIONS FROM
REMARK 3 NON-CRYSTALLOGRAPHIC SYMMETRY CORRESPOND TO THOSE PARTS
REMARK 3 OF THE PROTEIN EXCLUDED FROM THE NCS-RESTRAINT.
REMARK 4
REMARK 4 4LIP COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 THE STARTING MATERIAL FOR THE INHIBITOR WAS
REMARK 6 RC-(RP,SP)-1,2-DIBUTYLCARBAMOYL-GLYCERO-3-O-P-NITROPHENYL
REMARK 6 BUTYLPHOSPHONATE. BY THE REACTION DESCRIBED IN THE JRNL
REMARK 6 REFERENCE ABOVE, THIS WAS TURNED INTO
REMARK 6 RC-SP-1,2-DIBUTYLCARBAMOYL-GLYCERO-3-O-BUTYLPHOSPHONATE.
REMARK 6 THE INHIBITOR IS COVALENTLY BOUND TO THE PROTEIN, BUT ONLY
REMARK 6 THE BUTYL PHOSPHONATE (SN-3 MOIETY) IS VISIBLE IN THE
REMARK 6 ELECTRON DENSITY. THIS IS NOT CAUSED BY FLEXIBILITY OR
REMARK 6 DISORDER, BUT THE PHOSPHONATE ESTER HAS BEEN CLEAVED BY AN
REMARK 6 AGING REACTION (BENCSURA ET AL. (1995), BIOCHEM. 34, 8989).
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-1996
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
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 : 56937
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.75
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 2.46
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.031
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 45.8
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.059
REMARK 200 <I/SIGMA(I)> FOR SHELL : 26.2
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3LIP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % MPD, 100 MM CACL2, 0.1 M
REMARK 280 TRIS/HCL, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 23.18034
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 D 2 .. 320 E 2 .. 320 0.643
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: TAKEN FROM RELEASED PDB ENTRY 3LIP
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: TAKEN FROM RELEASED PDB ENTRY 3LIP
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACD
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ACE
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: OXD
REMARK 800 SITE_DESCRIPTION: OXYANION HOLE
REMARK 800
REMARK 800 SITE_IDENTIFIER: OXE
REMARK 800 SITE_DESCRIPTION: OXYANION HOLE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 4LIP D SWS P22088 1 - 45 NOT IN ATOMS LIST
REMARK 999 4LIP E SWS P22088 1 - 45 NOT IN ATOMS LIST
REMARK 999
REMARK 999 THIS SEQUENCE MATCHES WITH THE FOLLOWING REFERENCE:
REMARK 999 NAKANISHI ET AL. (1991): CLONING, SEQUENCING, REGULATION
REMARK 999 OF THE LIPASE GENE FROM PSEUDOMONAS SP. M 12-33. IN
REMARK 999 LIPASES: STRUCTURE, MECHANISM, GENETIC ENGINEERING. GBF
REMARK 999 MONOGRAPHS NO. 16 (ALBERGHINA, SCHMID, VERGER EDS.) VCH,
REMARK 999 WEINHEIM, PP. 263-266.
DBREF 4LIP D 2 320 SWS P22088 LIP_BURCE 46 364
DBREF 4LIP E 2 320 SWS P22088 LIP_BURCE 46 364
SEQADV 4LIP ASP D 2 SWS P22088 ALA 46 CONFLICT
SEQADV 4LIP ASN D 3 SWS P22088 GLY 47 CONFLICT
SEQADV 4LIP THR D 18 SWS P22088 SER 62 CONFLICT
SEQADV 4LIP ARG D 40 SWS P22088 ASN 84 CONFLICT
SEQADV 4LIP THR D 92 SWS P22088 SER 136 CONFLICT
SEQADV 4LIP GLY D 125 SWS P22088 ASP 169 CONFLICT
SEQADV 4LIP THR D 137 SWS P22088 SER 181 CONFLICT
SEQADV 4LIP ASN D 154 SWS P22088 HIS 198 CONFLICT
SEQADV 4LIP LYS D 165 SWS P22088 GLN 209 CONFLICT
SEQADV 4LIP GLN D 171 SWS P22088 ARG 215 CONFLICT
SEQADV 4LIP ILE D 218 SWS P22088 LEU 262 CONFLICT
SEQADV 4LIP ILE D 232 SWS P22088 LEU 276 CONFLICT
SEQADV 4LIP ALA D 240 SWS P22088 VAL 284 CONFLICT
SEQADV 4LIP PRO D 243 SWS P22088 LEU 287 CONFLICT
SEQADV 4LIP VAL D 256 SWS P22088 ILE 300 CONFLICT
SEQADV 4LIP VAL D 266 SWS P22088 LEU 310 CONFLICT
SEQADV 4LIP GLN D 276 SWS P22088 LYS 320 CONFLICT
SEQADV 4LIP ASN D 300 SWS P22088 TYR 344 CONFLICT
SEQADV 4LIP ASP E 2 SWS P22088 ALA 46 CONFLICT
SEQADV 4LIP ASN E 3 SWS P22088 GLY 47 CONFLICT
SEQADV 4LIP THR E 18 SWS P22088 SER 62 CONFLICT
SEQADV 4LIP ARG E 40 SWS P22088 ASN 84 CONFLICT
SEQADV 4LIP THR E 92 SWS P22088 SER 136 CONFLICT
SEQADV 4LIP GLY E 125 SWS P22088 ASP 169 CONFLICT
SEQADV 4LIP THR E 137 SWS P22088 SER 181 CONFLICT
SEQADV 4LIP ASN E 154 SWS P22088 HIS 198 CONFLICT
SEQADV 4LIP LYS E 165 SWS P22088 GLN 209 CONFLICT
SEQADV 4LIP GLN E 171 SWS P22088 ARG 215 CONFLICT
SEQADV 4LIP ILE E 218 SWS P22088 LEU 262 CONFLICT
SEQADV 4LIP ILE E 232 SWS P22088 LEU 276 CONFLICT
SEQADV 4LIP ALA E 240 SWS P22088 VAL 284 CONFLICT
SEQADV 4LIP PRO E 243 SWS P22088 LEU 287 CONFLICT
SEQADV 4LIP VAL E 256 SWS P22088 ILE 300 CONFLICT
SEQADV 4LIP VAL E 266 SWS P22088 LEU 310 CONFLICT
SEQADV 4LIP GLN E 276 SWS P22088 LYS 320 CONFLICT
SEQADV 4LIP ASN E 300 SWS P22088 TYR 344 CONFLICT
SEQRES 1 D 320 ALA ASP ASN TYR ALA ALA THR ARG TYR PRO ILE ILE LEU
SEQRES 2 D 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 D 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 D 320 ARG GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 D 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 D 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 D 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 D 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 D 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 D 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 D 320 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 D 320 ASN VAL PHE GLY ILE LEU THR SER SER SER ASN ASN THR
SEQRES 13 D 320 ASN GLN ASP ALA LEU ALA ALA LEU LYS THR LEU THR THR
SEQRES 14 D 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 D 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 D 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 D 320 TRP ALA GLY THR ALA ILE GLN PRO THR ILE SER VAL PHE
SEQRES 18 D 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 D 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 D 320 LEU PHE GLY THR GLY THR VAL MET VAL ASN ARG GLY SER
SEQRES 21 D 320 GLY GLN ASN ASP GLY VAL VAL SER LYS CYS SER ALA LEU
SEQRES 22 D 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 D 320 LEU ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 D 320 ASN ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 D 320 ASN ARG LEU LYS LEU ALA GLY VAL
SEQRES 1 E 320 ALA ASP ASN TYR ALA ALA THR ARG TYR PRO ILE ILE LEU
SEQRES 2 E 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 E 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 E 320 ARG GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 E 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 E 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 E 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 E 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 E 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 E 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 E 320 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 E 320 ASN VAL PHE GLY ILE LEU THR SER SER SER ASN ASN THR
SEQRES 13 E 320 ASN GLN ASP ALA LEU ALA ALA LEU LYS THR LEU THR THR
SEQRES 14 E 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 E 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 E 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 E 320 TRP ALA GLY THR ALA ILE GLN PRO THR ILE SER VAL PHE
SEQRES 18 E 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 E 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 E 320 LEU PHE GLY THR GLY THR VAL MET VAL ASN ARG GLY SER
SEQRES 21 E 320 GLY GLN ASN ASP GLY VAL VAL SER LYS CYS SER ALA LEU
SEQRES 22 E 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 E 320 LEU ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 E 320 ASN ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 E 320 ASN ARG LEU LYS LEU ALA GLY VAL
HET CA D 321 1
HET CCP D 950 7
HET CA E 321 1
HET CCP E 950 7
HETNAM CA CALCIUM ION
HETNAM CCP BUTYLPHOSPHONATE
FORMUL 3 CA 2(CA1 2+)
FORMUL 4 CCP 2(C4 H11 O3 P1)
FORMUL 5 HOH *563(H2 O1)
HELIX 1 1 ILE D 33 ARG D 40 1 8
HELIX 2 2 ARG D 61 THR D 76 1 16
HELIX 3 3 SER D 87 VAL D 99 5 13
HELIX 4 4 GLU D 118 TYR D 129 1 12
HELIX 5 5 LEU D 134 THR D 150 1 17
HELIX 6 6 ALA D 160 THR D 166 1 7
HELIX 7 7 THR D 169 ASN D 178 1 10
HELIX 8 8 PRO D 237 LEU D 241 5 5
HELIX 9 9 PRO D 243 ARG D 258 1 16
HELIX 10 10 LYS D 269 ALA D 272 1 4
HELIX 11 11 PRO D 304 LEU D 317 1 14
HELIX 12 12 ILE E 33 GLN E 39 1 7
HELIX 13 13 ARG E 61 THR E 76 1 16
HELIX 14 14 SER E 87 VAL E 99 5 13
HELIX 15 15 GLU E 118 TYR E 129 1 12
HELIX 16 16 LEU E 134 THR E 150 1 17
HELIX 17 17 ALA E 160 LEU E 167 1 8
HELIX 18 18 THR E 169 ASN E 178 1 10
HELIX 19 19 PRO E 237 LEU E 241 5 5
HELIX 20 20 PRO E 243 ARG E 258 1 16
HELIX 21 21 LYS E 269 ALA E 272 1 4
HELIX 22 22 PRO E 304 LEU E 317 1 14
SHEET 1 A1 6 VAL D 44 VAL D 46 0
SHEET 2 A1 6 PRO D 10 VAL D 14 1 N ILE D 11 O TYR D 45
SHEET 3 A1 6 VAL D 81 HIS D 86 1 N ASN D 82 O PRO D 10
SHEET 4 A1 6 VAL D 104 ILE D 110 1 N ALA D 105 O VAL D 81
SHEET 5 A1 6 ASN D 202 GLY D 211 1 N LEU D 205 O VAL D 107
SHEET 6 A1 6 THR D 196 VAL D 199 -1 N VAL D 199 O ASN D 202
SHEET 1 A2 2 ASN D 202 GLY D 211 0
SHEET 2 A2 2 GLN D 276 TYR D 282 1 N SER D 279 O SER D 208
SHEET 1 A3 2 LYS D 22 TYR D 23 0
SHEET 2 A3 2 LEU D 27 GLU D 28 -1 N LEU D 27 O TYR D 23
SHEET 1 A4 2 ILE D 214 VAL D 220 0
SHEET 2 A4 2 VAL D 223 ASP D 228 -1 N THR D 227 O GLN D 215
SHEET 1 B1 6 VAL E 44 VAL E 46 0
SHEET 2 B1 6 PRO E 10 VAL E 14 1 N ILE E 11 O TYR E 45
SHEET 3 B1 6 VAL E 81 HIS E 86 1 N ASN E 82 O PRO E 10
SHEET 4 B1 6 VAL E 104 ILE E 110 1 N ALA E 105 O VAL E 81
SHEET 5 B1 6 ASN E 202 GLY E 211 1 N LEU E 205 O VAL E 107
SHEET 6 B1 6 THR E 196 VAL E 199 -1 N VAL E 199 O ASN E 202
SHEET 1 B2 2 ASN E 202 GLY E 211 0
SHEET 2 B2 2 GLN E 276 TYR E 282 1 N SER E 279 O SER E 208
SHEET 1 B3 2 LYS E 22 TYR E 23 0
SHEET 2 B3 2 LEU E 27 GLU E 28 -1 N LEU E 27 O TYR E 23
SHEET 1 B4 2 ILE E 214 VAL E 220 0
SHEET 2 B4 2 VAL E 223 ASP E 228 -1 N THR E 227 O GLN E 215
LINK P CCP D 950 OG SER D 87
LINK P CCP E 950 OG SER E 87
LINK P CCP D 950 OG SER D 87
LINK P CCP E 950 OG SER E 87
CISPEP 1 GLN D 292 LEU D 293 0 -6.58
CISPEP 2 GLN E 292 LEU E 293 0 -7.16
SITE 1 ACD 3 SER D 87 HIS D 286 ASP D 264
SITE 1 ACE 3 SER E 87 HIS E 286 ASP E 264
SITE 1 OXD 2 LEU D 17 GLN D 88
SITE 1 OXE 2 LEU E 17 GLN E 88
CRYST1 84.040 46.360 85.380 90.00 116.53 90.00 P 1 21 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 0.011899 0.000000 0.005940 0.00000
SCALE2 0.000000 0.021570 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013091 0.00000
MTRIX1 1 -0.999800 0.020800 0.001000 22.93100 1
MTRIX2 1 0.020800 0.999600 -0.018700 0.44100 1
MTRIX3 1 -0.001400 -0.018700 -0.999800 38.11100 1 |