HEADER HYDROLASE(CARBOXYLIC ESTERASE) 19-AUG-94 1LPB
TITLE THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE PANCREATIC LIPASE
TITLE 2 COLIPASE COMPLEX INHIBITED BY A C11 ALKYL PHOSPHONATE
CAVEAT 1LPB BOG B 451 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLIPASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: LIPASE;
COMPND 7 CHAIN: B;
COMPND 8 EC: 3.1.1.3;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: PANCREAS;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 ORGAN: PANCREAS
KEYWDS HYDROLASE(CARBOXYLIC ESTERASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR M.-P.EGLOFF,H.VAN TILBEURGH,C.CAMBILLAU
REVDAT 4 29-JUL-20 1LPB 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE
REVDAT 3 29-NOV-17 1LPB 1 HELIX
REVDAT 2 24-FEB-09 1LPB 1 VERSN
REVDAT 1 01-NOV-94 1LPB 0
JRNL AUTH M.P.EGLOFF,F.MARGUET,G.BUONO,R.VERGER,C.CAMBILLAU,
JRNL AUTH 2 H.VAN TILBEURGH
JRNL TITL THE 2.46 A RESOLUTION STRUCTURE OF THE PANCREATIC
JRNL TITL 2 LIPASE-COLIPASE COMPLEX INHIBITED BY A C11 ALKYL
JRNL TITL 3 PHOSPHONATE.
JRNL REF BIOCHEMISTRY V. 34 2751 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7893686
JRNL DOI 10.1021/BI00009A003
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.VAN TILBEURGH,M.-P.EGLOFF,C.MARTINEZ,N.RUGANI,R.VERGER,
REMARK 1 AUTH 2 C.CAMBILLAU
REMARK 1 TITL INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY
REMARK 1 TITL 2 MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
REMARK 1 REF NATURE V. 362 814 1993
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.VAN TILBEURGH,L.SARDA,R.VERGER,C.CAMBILLAU
REMARK 1 TITL STRUCTURE OF THE PANCREATIC LIPASE-PROCOLIPASE COMPLEX
REMARK 1 REF NATURE V. 359 159 1992
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.183
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
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 : 4129
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 285
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.960
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LPB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174787.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
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) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 66.85000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 66.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.65000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 66.85000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 66.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.65000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 66.85000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.85000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.65000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 66.85000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.85000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.65000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 VAL A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 GLY A 91
REMARK 465 ARG A 92
REMARK 465 SER A 93
REMARK 465 ASP A 94
REMARK 465 SER A 95
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HH11 ARG B 265 H2 HOH B 1080 1.21
REMARK 500 HH22 ARG B 414 H2 HOH B 1015 1.22
REMARK 500 HZ1 LYS B 324 H2 HOH B 1090 1.27
REMARK 500 O HOH B 1060 H2 HOH B 1081 1.55
REMARK 500 O HOH B 1063 H2 HOH B 1120 1.55
REMARK 500 O HOH B 992 H1 HOH B 993 1.59
REMARK 500
REMARK 500 REMARK: NULL
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 CYS B 304 CA - CB - SG ANGL. DEV. = 6.9 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 ILE A 7 73.51 30.95
REMARK 500 ILE A 8 116.64 -176.77
REMARK 500 ARG B 7 -47.29 72.85
REMARK 500 ASP B 13 30.72 -96.08
REMARK 500 ALA B 54 68.60 -68.93
REMARK 500 ILE B 78 -23.54 66.55
REMARK 500 TRP B 106 38.25 -147.92
REMARK 500 ARG B 111 55.95 -94.22
REMARK 500 SER B 152 -116.73 58.49
REMARK 500 PHE B 182 -36.48 -139.03
REMARK 500 ASP B 205 53.38 -148.30
REMARK 500 ASN B 229 19.95 53.10
REMARK 500 LYS B 238 43.11 -75.80
REMARK 500 VAL B 246 55.12 -100.01
REMARK 500 ILE B 248 -14.63 -42.74
REMARK 500 ALA B 260 58.92 -164.89
REMARK 500 ASN B 334 67.46 84.20
REMARK 500 PRO B 410 7.51 -67.17
REMARK 500 LEU B 412 63.68 62.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 USE OF PARTIAL OCCUPANCY FOR THE INHIBITOR (REFINED
REMARK 600 OCCUPANCY) AND FOR BETA-OCTYLGLUCOSIDE MOLECULES.
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 B 453 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 187 O
REMARK 620 2 ARG B 190 O 72.0
REMARK 620 3 ASP B 192 OD1 85.5 93.4
REMARK 620 4 ASP B 195 OD1 147.2 140.8 93.0
REMARK 620 5 ASP B 195 OD2 162.6 90.8 93.6 50.2
REMARK 620 6 HOH B 989 O 90.4 85.9 175.9 90.1 90.5
REMARK 620 7 HOH B1072 O 70.4 141.6 90.6 76.9 127.0 87.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1LPB A 1 95 UNP P02703 COL_PIG 1 95
DBREF 1LPB B 1 449 UNP P16233 LIPP_HUMAN 17 465
SEQRES 1 A 95 VAL PRO ASP PRO ARG GLY ILE ILE ILE ASN LEU ASP GLU
SEQRES 2 A 95 GLY GLU LEU CYS LEU ASN SER ALA GLN CYS LYS SER ASN
SEQRES 3 A 95 CYS CYS GLN HIS ASP THR ILE LEU SER LEU SER ARG CYS
SEQRES 4 A 95 ALA LEU LYS ALA ARG GLU ASN SER GLU CYS SER ALA PHE
SEQRES 5 A 95 THR LEU TYR GLY VAL TYR TYR LYS CYS PRO CYS GLU ARG
SEQRES 6 A 95 GLY LEU THR CYS GLU GLY ASP LYS SER LEU VAL GLY SER
SEQRES 7 A 95 ILE THR ASN THR ASN PHE GLY ILE CYS HIS ASN VAL GLY
SEQRES 8 A 95 ARG SER ASP SER
SEQRES 1 B 449 LYS GLU VAL CYS TYR GLU ARG LEU GLY CYS PHE SER ASP
SEQRES 2 B 449 ASP SER PRO TRP SER GLY ILE THR GLU ARG PRO LEU HIS
SEQRES 3 B 449 ILE LEU PRO TRP SER PRO LYS ASP VAL ASN THR ARG PHE
SEQRES 4 B 449 LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN GLU
SEQRES 5 B 449 VAL ALA ALA ASP SER SER SER ILE SER GLY SER ASN PHE
SEQRES 6 B 449 LYS THR ASN ARG LYS THR ARG PHE ILE ILE HIS GLY PHE
SEQRES 7 B 449 ILE ASP LYS GLY GLU GLU ASN TRP LEU ALA ASN VAL CYS
SEQRES 8 B 449 LYS ASN LEU PHE LYS VAL GLU SER VAL ASN CYS ILE CYS
SEQRES 9 B 449 VAL ASP TRP LYS GLY GLY SER ARG THR GLY TYR THR GLN
SEQRES 10 B 449 ALA SER GLN ASN ILE ARG ILE VAL GLY ALA GLU VAL ALA
SEQRES 11 B 449 TYR PHE VAL GLU PHE LEU GLN SER ALA PHE GLY TYR SER
SEQRES 12 B 449 PRO SER ASN VAL HIS VAL ILE GLY HIS SER LEU GLY ALA
SEQRES 13 B 449 HIS ALA ALA GLY GLU ALA GLY ARG ARG THR ASN GLY THR
SEQRES 14 B 449 ILE GLY ARG ILE THR GLY LEU ASP PRO ALA GLU PRO CYS
SEQRES 15 B 449 PHE GLN GLY THR PRO GLU LEU VAL ARG LEU ASP PRO SER
SEQRES 16 B 449 ASP ALA LYS PHE VAL ASP VAL ILE HIS THR ASP GLY ALA
SEQRES 17 B 449 PRO ILE VAL PRO ASN LEU GLY PHE GLY MET SER GLN VAL
SEQRES 18 B 449 VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY VAL GLU
SEQRES 19 B 449 MET PRO GLY CYS LYS LYS ASN ILE LEU SER GLN ILE VAL
SEQRES 20 B 449 ASP ILE ASP GLY ILE TRP GLU GLY THR ARG ASP PHE ALA
SEQRES 21 B 449 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR THR ASP
SEQRES 22 B 449 SER ILE VAL ASN PRO ASP GLY PHE ALA GLY PHE PRO CYS
SEQRES 23 B 449 ALA SER TYR ASN VAL PHE THR ALA ASN LYS CYS PHE PRO
SEQRES 24 B 449 CYS PRO SER GLY GLY CYS PRO GLN MET GLY HIS TYR ALA
SEQRES 25 B 449 ASP ARG TYR PRO GLY LYS THR ASN ASP VAL GLY GLN LYS
SEQRES 26 B 449 PHE TYR LEU ASP THR GLY ASP ALA SER ASN PHE ALA ARG
SEQRES 27 B 449 TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS LYS
SEQRES 28 B 449 VAL THR GLY HIS ILE LEU VAL SER LEU PHE GLY ASN LYS
SEQRES 29 B 449 GLY ASN SER LYS GLN TYR GLU ILE PHE LYS GLY THR LEU
SEQRES 30 B 449 LYS PRO ASP SER THR HIS SER ASN GLU PHE ASP SER ASP
SEQRES 31 B 449 VAL ASP VAL GLY ASP LEU GLN MET VAL LYS PHE ILE TRP
SEQRES 32 B 449 TYR ASN ASN VAL ILE ASN PRO THR LEU PRO ARG VAL GLY
SEQRES 33 B 449 ALA SER LYS ILE ILE VAL GLU THR ASN VAL GLY LYS GLN
SEQRES 34 B 449 PHE ASN PHE CYS SER PRO GLU THR VAL ARG GLU GLU VAL
SEQRES 35 B 449 LEU LEU THR LEU THR PRO CYS
HET BOG A 96 24
HET BOG A 97 24
HET BOG B 450 24
HET BOG B 451 48
HET BOG B 452 48
HET CA B 453 1
HET MUP B 901 30
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM CA CALCIUM ION
HETNAM MUP METHOXYUNDECYLPHOSPHINIC ACID
FORMUL 3 BOG 5(C14 H28 O6)
FORMUL 8 CA CA 2+
FORMUL 9 MUP C12 H27 O3 P
FORMUL 10 HOH *285(H2 O)
HELIX 1 A ASP A 31 LEU A 34 1 4
HELIX 2 B GLY A 56 CYS A 61 1 6
HELIX 3 J LEU A 75 THR A 80 1 6
HELIX 4 D LYS B 107 SER B 110 1 4
HELIX 5 E TYR B 114 PHE B 139 1 26
HELIX 6 F LEU B 153 ARG B 163 1 11
HELIX 7 G ILE B 241 ILE B 245 1THE TWO HELICES OF THE LID 5
HELIX 8 H ILE B 251 ILE B 274 1 24
HELIX 9 I TYR B 288 THR B 292 1 5
SHEET 1 SA 2 GLU B 2 TYR B 5 0
SHEET 2 SA 2 ILE A 9 ASP A 12 -1
SHEET 1 SB 9 SER A 37 LEU A 41 0
SHEET 2 SB 9 SER A 50 PHE A 52 -1
SHEET 3 SB 9 GLU A 70 SER A 74 -1
SHEET 4 SB 9 ASN B 100 ASP B 105 1
SHEET 5 SB 9 VAL B 146 HIS B 151 1
SHEET 6 SB 9 ARG B 171 LEU B 175 1
SHEET 7 SB 9 VAL B 199 ILE B 202 1
SHEET 8 SB 9 LEU B 224 PRO B 228 1
SHEET 9 SB 9 GLN B 323 LEU B 327 1
SHEET 1 SC 4 TRP B 338 GLY B 348 0
SHEET 2 SC 4 THR B 381 SER B 388 -1
SHEET 3 SC 4 VAL B 415 THR B 424 -1
SHEET 4 SC 4 GLN B 429 CYS B 433 -1
SHEET 1 SD 4 VAL B 351 GLY B 361 0
SHEET 2 SD 4 TYR B 369 LEU B 376 -1
SHEET 3 SD 4 LEU B 395 TYR B 403 -1
SHEET 4 SD 4 LEU B 444 PRO B 448 -1
SHEET 1 SE 1 LEU A 67 GLU A 70 0
SHEET 1 SF 1 PHE A 84 ASN A 89 0
SSBOND 1 CYS A 17 CYS A 28 1555 1555 2.03
SSBOND 2 CYS A 23 CYS A 39 1555 1555 2.04
SSBOND 3 CYS A 27 CYS A 61 1555 1555 2.04
SSBOND 4 CYS A 49 CYS A 69 1555 1555 2.03
SSBOND 5 CYS A 63 CYS A 87 1555 1555 2.03
SSBOND 6 CYS B 4 CYS B 10 1555 1555 2.03
SSBOND 7 CYS B 90 CYS B 101 1555 1555 2.04
SSBOND 8 CYS B 237 CYS B 261 1555 1555 2.04
SSBOND 9 CYS B 285 CYS B 296 1555 1555 2.03
SSBOND 10 CYS B 299 CYS B 304 1555 1555 2.05
SSBOND 11 CYS B 433 CYS B 449 1555 1555 2.01
LINK OG SER B 152 P AMUP B 901 1555 1555 1.60
LINK OG SER B 152 P BMUP B 901 1555 1555 1.65
LINK O GLU B 187 CA CA B 453 1555 1555 2.29
LINK O ARG B 190 CA CA B 453 1555 1555 2.26
LINK OD1 ASP B 192 CA CA B 453 1555 1555 2.26
LINK OD1 ASP B 195 CA CA B 453 1555 1555 2.50
LINK OD2 ASP B 195 CA CA B 453 1555 1555 2.54
LINK CA CA B 453 O HOH B 989 1555 1555 2.18
LINK CA CA B 453 O HOH B1072 1555 1555 2.23
CISPEP 1 SER B 15 PRO B 16 0 0.64
CISPEP 2 VAL B 210 PRO B 211 0 0.48
CISPEP 3 PHE B 297 PRO B 298 0 0.72
SITE 1 CAT 3 SER B 152 ASP B 176 HIS B 263
CRYST1 133.700 133.700 93.300 90.00 90.00 90.00 P 42 21 2 8
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 0.007479 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010718 0.00000
(ATOM LINES ARE NOT SHOWN.)
END