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HEADER HYDROLASE 25-OCT-05 2ES4
TITLE CRYSTAL STRUCTURE OF THE BURKHOLDERIA GLUMAE LIPASE-
TITLE 2 SPECIFIC FOLDASE IN COMPLEX WITH ITS COGNATE LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: LIPASE CHAPERONE;
COMPND 8 CHAIN: D, E;
COMPND 9 FRAGMENT: PERIPLASMIC C-TERMINAL DOMAIN;
COMPND 10 SYNONYM: LIPASE FOLDASE, LIPASE HELPER PROTEIN, LIPASE
COMPND 11 ACTIVATOR PROTEIN, LIPASE MODULATOR;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA GLUMAE;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: PG1;
SOURCE 5 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BURKHOLDERIA GLUMAE;
SOURCE 8 ORGANISM_COMMON: BACTERIA;
SOURCE 9 GENE: LIFO, LIPB;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS PROTEIN-PROTEIN COMPLEX, STERIC CHAPERONE, TRIACYLGLYCEROL
KEYWDS 2 HYDROLASE, ALL ALPHA HELIX PROTEIN, A/B HYDROLASE FOLD,
KEYWDS 3 EXTENSIVE INTERACTION AREA
EXPDTA X-RAY DIFFRACTION
AUTHOR K.PAUWELS,L.WYNS,J.TOMMASSEN,S.N.SAVVIDES,P.VAN GELDER
REVDAT 1 07-MAR-06 2ES4 0
JRNL AUTH K.PAUWELS,A.LUSTIG,L.WYNS,J.TOMMASSEN,S.N.SAVVIDES,
JRNL AUTH 2 P.VAN GELDER
JRNL TITL STRUCTURE OF A MEMBRANE-BASED STERIC CHAPERONE IN
JRNL TITL 2 COMPLEX WITH ITS LIPASE SUBSTRATE
JRNL REF NAT.STRUCT.MOL.BIOL. 2006
JRNL REFN US ESSN 1545-9985
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.PAUWELS,R.LORIS,G.VANDENBUSSCHE,J-M.RUYSSCHAERT,
REMARK 1 AUTH 2 L.WYNS,P.VAN GELDER
REMARK 1 TITL CRYSTALLIZATION AND CRYSTAL MANIPULATION OF A
REMARK 1 TITL 2 STERIC CHAPERONE IN COMPLEX WITH ITS LIPASE
REMARK 1 TITL 3 SUBSTRATE
REMARK 1 REF ACTA CRYSTALLOGR., SECT.F V. F61 791 2005
REMARK 1 REFN DK ESSN 1744-3091
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 119309
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) : 0.199
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5974
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 : 8611
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 843
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.93
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 2ES4 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-2005.
REMARK 100 THE RCSB ID CODE IS RCSB035024.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC Q4 DETECTOR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120503
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1CVL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG3350, 0.2 M KI, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 91.50000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.50000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 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, D
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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 220
REMARK 465 LEU A 221
REMARK 465 GLY A 222
REMARK 465 GLY D 1
REMARK 465 HIS D 2
REMARK 465 HIS D 3
REMARK 465 HIS D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 HIS D 11
REMARK 465 SER D 12
REMARK 465 SER D 13
REMARK 465 GLY D 14
REMARK 465 HIS D 15
REMARK 465 ILE D 16
REMARK 465 GLU D 17
REMARK 465 GLY D 18
REMARK 465 ARG D 19
REMARK 465 HIS D 20
REMARK 465 MET D 21
REMARK 465 PRO D 22
REMARK 465 ALA D 23
REMARK 465 ALA D 24
REMARK 465 PRO D 25
REMARK 465 SER D 26
REMARK 465 PRO D 27
REMARK 465 ALA D 28
REMARK 465 PRO D 29
REMARK 465 ALA D 30
REMARK 465 GLY D 31
REMARK 465 ALA D 32
REMARK 465 VAL D 33
REMARK 465 ALA D 34
REMARK 465 GLY D 35
REMARK 465 GLY D 36
REMARK 465 PRO D 37
REMARK 465 ALA D 38
REMARK 465 ALA D 39
REMARK 465 GLY D 40
REMARK 465 VAL D 41
REMARK 465 PRO D 42
REMARK 465 ALA D 43
REMARK 465 ALA D 44
REMARK 465 ALA D 45
REMARK 465 SER D 46
REMARK 465 GLY D 47
REMARK 465 ALA D 48
REMARK 465 ALA D 49
REMARK 465 GLU D 50
REMARK 465 ALA D 51
REMARK 465 ALA D 52
REMARK 465 GLN D 141
REMARK 465 LEU D 142
REMARK 465 PRO D 143
REMARK 465 GLY D 144
REMARK 465 ASP D 145
REMARK 465 GLY D 146
REMARK 465 ALA D 147
REMARK 465 THR D 201
REMARK 465 PRO D 205
REMARK 465 GLU D 206
REMARK 465 THR B 219
REMARK 465 VAL B 220
REMARK 465 LEU B 221
REMARK 465 GLY B 222
REMARK 465 VAL B 223
REMARK 465 GLY E 1
REMARK 465 HIS E 2
REMARK 465 HIS E 3
REMARK 465 HIS E 4
REMARK 465 HIS E 5
REMARK 465 HIS E 6
REMARK 465 HIS E 7
REMARK 465 HIS E 8
REMARK 465 HIS E 9
REMARK 465 HIS E 10
REMARK 465 HIS E 11
REMARK 465 SER E 12
REMARK 465 SER E 13
REMARK 465 GLY E 14
REMARK 465 HIS E 15
REMARK 465 ILE E 16
REMARK 465 GLU E 17
REMARK 465 GLY E 18
REMARK 465 ARG E 19
REMARK 465 HIS E 20
REMARK 465 MET E 21
REMARK 465 PRO E 22
REMARK 465 ALA E 23
REMARK 465 ALA E 24
REMARK 465 PRO E 25
REMARK 465 SER E 26
REMARK 465 PRO E 27
REMARK 465 ALA E 28
REMARK 465 PRO E 29
REMARK 465 ALA E 30
REMARK 465 GLY E 31
REMARK 465 ALA E 32
REMARK 465 VAL E 33
REMARK 465 ALA E 34
REMARK 465 GLY E 35
REMARK 465 GLY E 36
REMARK 465 PRO E 37
REMARK 465 ALA E 38
REMARK 465 ALA E 39
REMARK 465 GLY E 40
REMARK 465 VAL E 41
REMARK 465 PRO E 42
REMARK 465 ALA E 43
REMARK 465 ALA E 44
REMARK 465 ALA E 45
REMARK 465 SER E 46
REMARK 465 GLY E 47
REMARK 465 ALA E 48
REMARK 465 ALA E 49
REMARK 465 GLU E 50
REMARK 465 ALA E 51
REMARK 465 ALA E 52
REMARK 465 ALA E 331
REMARK 465 GLY E 332
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 HIS A 154 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 158 CG CD OE1 NE2
REMARK 470 GLN A 203 CD OE1 NE2
REMARK 470 ARG D 130 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 148 CG1 CG2
REMARK 470 LEU D 149 CG CD1 CD2
REMARK 470 ASP D 151 CG OD1 OD2
REMARK 470 LYS D 152 CG CD CE NZ
REMARK 470 LEU D 153 CG CD1 CD2
REMARK 470 ASP D 163 CG OD1 OD2
REMARK 470 ARG D 171 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 175 CG CD OE1 OE2
REMARK 470 ARG D 196 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 207 CG CD OE1 NE2
REMARK 470 LYS D 208 CD CE NZ
REMARK 470 ARG D 211 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 218 CG CD OE1 NE2
REMARK 470 GLN D 226 CG CD OE1 NE2
REMARK 470 GLN D 284 CD OE1 NE2
REMARK 470 ARG D 306 CD NE CZ NH1 NH2
REMARK 470 HIS B 154 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 158 CG CD OE1 NE2
REMARK 470 ARG E 78 NE CZ NH1 NH2
REMARK 470 ARG E 109 CZ NH1 NH2
REMARK 470 ARG E 130 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 133 CD NE CZ NH1 NH2
REMARK 470 GLN E 141 CG CD OE1 NE2
REMARK 470 LEU E 142 CG CD1 CD2
REMARK 470 PRO E 143 CG CD
REMARK 470 ASP E 151 OD1 OD2
REMARK 470 LYS E 152 CD CE NZ
REMARK 470 LEU E 153 CG CD1 CD2
REMARK 470 LEU E 160 CG CD1 CD2
REMARK 470 LEU E 162 CD1 CD2
REMARK 470 GLN E 164 CG CD OE1 NE2
REMARK 470 ASP E 170 CG OD1 OD2
REMARK 470 GLU E 175 CG CD OE1 OE2
REMARK 470 ARG E 187 CZ NH1 NH2
REMARK 470 GLN E 218 CG CD OE1 NE2
REMARK 470 GLU E 223 CG CD OE1 OE2
REMARK 470 GLN E 226 CG CD OE1 NE2
REMARK 470 LEU E 230 CD1 CD2
REMARK 470 LYS E 245 CG CD CE NZ
REMARK 470 GLN E 280 CG CD OE1 NE2
REMARK 470 GLN E 284 CG CD OE1 NE2
REMARK 470 GLU E 289 CD OE1 OE2
REMARK 470 GLN E 301 CG CD OE1 NE2
REMARK 470 ARG E 306 CD NE CZ NH1 NH2
REMARK 470 GLN E 309 CG CD OE1 NE2
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
REMARK 500 O HOH 9 O HOH 837 1.85
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 811 O HOH 811 2555 2.11
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 PRO D 179 CB PRO D 179 CG -0.058
REMARK 500 LEU D 192 CG LEU D 192 CD2 -0.066
REMARK 500 LEU D 219 CG LEU D 219 CD2 -0.075
REMARK 500 ALA B 298 CA ALA B 298 CB -0.089
REMARK 500 LEU E 173 CG LEU E 173 CD2 -0.074
REMARK 500 LEU E 215 CG LEU E 215 CD1 -0.052
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 GLY A 16 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 ALA A 18 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 TYR A 31 N - CA - C ANGL. DEV. = 6.7 DEGREES
REMARK 500 GLY A 41 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 LYS A 43 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ASN A 48 N - CA - C ANGL. DEV. = -6.8 DEGREES
REMARK 500 GLY A 57 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 THR A 76 N - CA - C ANGL. DEV. = 6.7 DEGREES
REMARK 500 VAL A 199 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 GLY A 200 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 LEU A 205 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASN A 284 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 THR D 100 N - CA - C ANGL. DEV. = -7.0 DEGREES
REMARK 500 ALA D 317 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ALA B 18 N - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 TYR B 31 N - CA - C ANGL. DEV. = 6.8 DEGREES
REMARK 500 GLY B 41 N - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 LYS B 43 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLY B 57 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO B 58 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 THR B 76 N - CA - C ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASN B 82 N - CA - C ANGL. DEV. = -6.7 DEGREES
REMARK 500 LEU B 205 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 LEU B 234 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 GLY B 260 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 TRP B 283 CB - CA - C ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASN B 284 N - CA - C ANGL. DEV. = -6.7 DEGREES
REMARK 500 THR E 100 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 LEU E 116 N - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 PRO E 143 N - CA - CB ANGL. DEV. = 6.9 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 THR A 20 164.14 66.10
REMARK 500 THR B 20 161.96 69.08
REMARK 500 LEU E 142 138.69 61.15
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 327 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH 552 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH 560 DISTANCE = 18.93 ANGSTROMS
REMARK 525 HOH 581 DISTANCE = 8.36 ANGSTROMS
REMARK 525 HOH 586 DISTANCE = 13.36 ANGSTROMS
REMARK 525 HOH 588 DISTANCE = 12.46 ANGSTROMS
REMARK 525 HOH 590 DISTANCE = 16.87 ANGSTROMS
REMARK 525 HOH 598 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH 608 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH 652 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH 654 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH 671 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH 712 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH 715 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH 729 DISTANCE = 8.28 ANGSTROMS
REMARK 525 HOH 754 DISTANCE = 7.89 ANGSTROMS
REMARK 525 HOH 758 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH 762 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH 763 DISTANCE = 8.33 ANGSTROMS
REMARK 525 HOH 764 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH 787 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH 836 DISTANCE = 6.02 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CVL RELATED DB: PDB
REMARK 900 THE SAME LIPASE (LIPA) WITHOUT ITS CHAPERONE (LIPB)
REMARK 900 RELATED ID: 1TAH RELATED DB: PDB
REMARK 900 THE SAME LIPASE (LIPA) WITHOUT ITS CHAPERONE (LIPB)
REMARK 900 RELATED ID: 1QGE RELATED DB: PDB
REMARK 900 THE SAME LIPASE (LIPA) WITHOUT ITS CHAPERONE (LIPB)
DBREF 2ES4 A 1 319 SWS Q05489 LIP_BURGL 40 358
DBREF 2ES4 D 22 332 SWS Q05490 LIFO_BURGL 42 353
DBREF 2ES4 B 1 319 SWS Q05489 LIP_BURGL 40 358
DBREF 2ES4 E 22 332 SWS Q05490 LIFO_BURGL 42 353
SEQADV 2ES4 GLY D 1 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 HIS D 2 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 3 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 4 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 5 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 6 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 7 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 8 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 9 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 10 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS D 11 SWS Q05490 HIS TAG
SEQADV 2ES4 SER D 12 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 SER D 13 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 GLY D 14 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 HIS D 15 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 ILE D 16 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 GLU D 17 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 GLY D 18 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 ARG D 19 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 HIS D 20 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 MET D 21 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 CEA D 92 SWS Q05490 CYS 112 MODIFIED RESIDUE
SEQADV 2ES4 GLY E 1 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 HIS E 2 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 3 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 4 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 5 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 6 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 7 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 8 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 9 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 10 SWS Q05490 HIS TAG
SEQADV 2ES4 HIS E 11 SWS Q05490 HIS TAG
SEQADV 2ES4 SER E 12 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 SER E 13 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 GLY E 14 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 HIS E 15 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 ILE E 16 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 GLU E 17 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 GLY E 18 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 ARG E 19 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 HIS E 20 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 MET E 21 SWS Q05490 CLONING ARTIFACT
SEQADV 2ES4 CEA E 92 SWS Q05490 CYS 112 MODIFIED RESIDUE
SEQRES 1 A 319 ALA ASP THR TYR ALA ALA THR ARG TYR PRO VAL ILE LEU
SEQRES 2 A 319 VAL HIS GLY LEU ALA GLY THR ASP LYS PHE ALA ASN VAL
SEQRES 3 A 319 VAL ASP TYR TRP TYR GLY ILE GLN SER ASP LEU GLN SER
SEQRES 4 A 319 HIS GLY ALA LYS VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 A 319 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 A 319 LEU ALA TYR VAL LYS GLN VAL LEU ALA ALA THR GLY ALA
SEQRES 7 A 319 THR LYS VAL ASN LEU ILE GLY HIS SER GLN GLY GLY LEU
SEQRES 8 A 319 THR SER ARG TYR VAL ALA ALA VAL ALA PRO GLN LEU VAL
SEQRES 9 A 319 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 A 319 GLU PHE ALA ASP PHE VAL GLN ASP VAL LEU LYS THR ASP
SEQRES 11 A 319 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 A 319 ASN VAL PHE GLY THR LEU VAL SER SER SER HIS ASN THR
SEQRES 13 A 319 ASP GLN ASP ALA LEU ALA ALA LEU ARG THR LEU THR THR
SEQRES 14 A 319 ALA GLN THR ALA THR TYR ASN ARG ASN PHE PRO SER ALA
SEQRES 15 A 319 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA ALA
SEQRES 16 A 319 THR GLU THR VAL GLY GLY SER GLN HIS LEU LEU TYR SER
SEQRES 17 A 319 TRP GLY GLY THR ALA ILE GLN PRO THR SER THR VAL LEU
SEQRES 18 A 319 GLY VAL THR GLY ALA THR ASP THR SER THR GLY THR LEU
SEQRES 19 A 319 ASP VAL ALA ASN VAL THR ASP PRO SER THR LEU ALA LEU
SEQRES 20 A 319 LEU ALA THR GLY ALA VAL MET ILE ASN ARG ALA SER GLY
SEQRES 21 A 319 GLN ASN ASP GLY LEU VAL SER ARG CYS SER SER LEU PHE
SEQRES 22 A 319 GLY GLN VAL ILE SER THR SER TYR HIS TRP ASN HIS LEU
SEQRES 23 A 319 ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA ASN
SEQRES 24 A 319 ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS VAL ASN
SEQRES 25 A 319 ARG LEU LYS LEU GLN GLY VAL
SEQRES 1 D 332 GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 D 332 GLY HIS ILE GLU GLY ARG HIS MET PRO ALA ALA PRO SER
SEQRES 3 D 332 PRO ALA PRO ALA GLY ALA VAL ALA GLY GLY PRO ALA ALA
SEQRES 4 D 332 GLY VAL PRO ALA ALA ALA SER GLY ALA ALA GLU ALA ALA
SEQRES 5 D 332 MET PRO LEU PRO ALA ALA LEU PRO GLY ALA LEU ALA GLY
SEQRES 6 D 332 SER HIS ALA PRO ARG LEU PRO LEU ALA ALA GLY GLY ARG
SEQRES 7 D 332 LEU ALA ARG THR ARG ALA VAL ARG GLU PHE PHE ASP TYR
SEQRES 8 D 332 CEA LEU THR ALA GLN GLY GLU LEU THR PRO ALA ALA LEU
SEQRES 9 D 332 ASP ALA LEU VAL ARG ARG GLU ILE ALA ALA GLN LEU ASP
SEQRES 10 D 332 GLY SER PRO ALA GLN ALA GLU ALA LEU GLY VAL TRP ARG
SEQRES 11 D 332 ARG TYR ARG ALA TYR PHE ASP ALA LEU ALA GLN LEU PRO
SEQRES 12 D 332 GLY ASP GLY ALA VAL LEU GLY ASP LYS LEU ASP PRO ALA
SEQRES 13 D 332 ALA MET GLN LEU ALA LEU ASP GLN ARG ALA ALA LEU ALA
SEQRES 14 D 332 ASP ARG THR LEU GLY GLU TRP ALA GLU PRO PHE PHE GLY
SEQRES 15 D 332 ASP GLU GLN ARG ARG GLN ARG HIS ASP LEU GLU ARG ILE
SEQRES 16 D 332 ARG ILE ALA ASN ASP THR THR LEU SER PRO GLU GLN LYS
SEQRES 17 D 332 ALA ALA ARG LEU ALA ALA LEU ASP ALA GLN LEU THR PRO
SEQRES 18 D 332 ASP GLU ARG ALA GLN GLN ALA ALA LEU HIS ALA GLN GLN
SEQRES 19 D 332 ASP ALA VAL THR LYS ILE ALA ASP LEU GLN LYS ALA GLY
SEQRES 20 D 332 ALA THR PRO ASP GLN MET ARG ALA GLN ILE ALA GLN THR
SEQRES 21 D 332 LEU GLY PRO GLU ALA ALA ALA ARG ALA ALA GLN MET GLN
SEQRES 22 D 332 GLN ASP ASP GLU ALA TRP GLN THR ARG TYR GLN ALA TYR
SEQRES 23 D 332 ALA ALA GLU ARG ASP ARG ILE ALA ALA GLN GLY LEU ALA
SEQRES 24 D 332 PRO GLN ASP ARG ASP ALA ARG ILE ALA GLN LEU ARG GLN
SEQRES 25 D 332 GLN THR PHE THR ALA PRO GLY GLU ALA ILE ARG ALA ALA
SEQRES 26 D 332 SER LEU ASP ARG GLY ALA GLY
SEQRES 1 B 319 ALA ASP THR TYR ALA ALA THR ARG TYR PRO VAL ILE LEU
SEQRES 2 B 319 VAL HIS GLY LEU ALA GLY THR ASP LYS PHE ALA ASN VAL
SEQRES 3 B 319 VAL ASP TYR TRP TYR GLY ILE GLN SER ASP LEU GLN SER
SEQRES 4 B 319 HIS GLY ALA LYS VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 B 319 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 B 319 LEU ALA TYR VAL LYS GLN VAL LEU ALA ALA THR GLY ALA
SEQRES 7 B 319 THR LYS VAL ASN LEU ILE GLY HIS SER GLN GLY GLY LEU
SEQRES 8 B 319 THR SER ARG TYR VAL ALA ALA VAL ALA PRO GLN LEU VAL
SEQRES 9 B 319 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 B 319 GLU PHE ALA ASP PHE VAL GLN ASP VAL LEU LYS THR ASP
SEQRES 11 B 319 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 B 319 ASN VAL PHE GLY THR LEU VAL SER SER SER HIS ASN THR
SEQRES 13 B 319 ASP GLN ASP ALA LEU ALA ALA LEU ARG THR LEU THR THR
SEQRES 14 B 319 ALA GLN THR ALA THR TYR ASN ARG ASN PHE PRO SER ALA
SEQRES 15 B 319 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA ALA
SEQRES 16 B 319 THR GLU THR VAL GLY GLY SER GLN HIS LEU LEU TYR SER
SEQRES 17 B 319 TRP GLY GLY THR ALA ILE GLN PRO THR SER THR VAL LEU
SEQRES 18 B 319 GLY VAL THR GLY ALA THR ASP THR SER THR GLY THR LEU
SEQRES 19 B 319 ASP VAL ALA ASN VAL THR ASP PRO SER THR LEU ALA LEU
SEQRES 20 B 319 LEU ALA THR GLY ALA VAL MET ILE ASN ARG ALA SER GLY
SEQRES 21 B 319 GLN ASN ASP GLY LEU VAL SER ARG CYS SER SER LEU PHE
SEQRES 22 B 319 GLY GLN VAL ILE SER THR SER TYR HIS TRP ASN HIS LEU
SEQRES 23 B 319 ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA ASN
SEQRES 24 B 319 ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS VAL ASN
SEQRES 25 B 319 ARG LEU LYS LEU GLN GLY VAL
SEQRES 1 E 332 GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 E 332 GLY HIS ILE GLU GLY ARG HIS MET PRO ALA ALA PRO SER
SEQRES 3 E 332 PRO ALA PRO ALA GLY ALA VAL ALA GLY GLY PRO ALA ALA
SEQRES 4 E 332 GLY VAL PRO ALA ALA ALA SER GLY ALA ALA GLU ALA ALA
SEQRES 5 E 332 MET PRO LEU PRO ALA ALA LEU PRO GLY ALA LEU ALA GLY
SEQRES 6 E 332 SER HIS ALA PRO ARG LEU PRO LEU ALA ALA GLY GLY ARG
SEQRES 7 E 332 LEU ALA ARG THR ARG ALA VAL ARG GLU PHE PHE ASP TYR
SEQRES 8 E 332 CEA LEU THR ALA GLN GLY GLU LEU THR PRO ALA ALA LEU
SEQRES 9 E 332 ASP ALA LEU VAL ARG ARG GLU ILE ALA ALA GLN LEU ASP
SEQRES 10 E 332 GLY SER PRO ALA GLN ALA GLU ALA LEU GLY VAL TRP ARG
SEQRES 11 E 332 ARG TYR ARG ALA TYR PHE ASP ALA LEU ALA GLN LEU PRO
SEQRES 12 E 332 GLY ASP GLY ALA VAL LEU GLY ASP LYS LEU ASP PRO ALA
SEQRES 13 E 332 ALA MET GLN LEU ALA LEU ASP GLN ARG ALA ALA LEU ALA
SEQRES 14 E 332 ASP ARG THR LEU GLY GLU TRP ALA GLU PRO PHE PHE GLY
SEQRES 15 E 332 ASP GLU GLN ARG ARG GLN ARG HIS ASP LEU GLU ARG ILE
SEQRES 16 E 332 ARG ILE ALA ASN ASP THR THR LEU SER PRO GLU GLN LYS
SEQRES 17 E 332 ALA ALA ARG LEU ALA ALA LEU ASP ALA GLN LEU THR PRO
SEQRES 18 E 332 ASP GLU ARG ALA GLN GLN ALA ALA LEU HIS ALA GLN GLN
SEQRES 19 E 332 ASP ALA VAL THR LYS ILE ALA ASP LEU GLN LYS ALA GLY
SEQRES 20 E 332 ALA THR PRO ASP GLN MET ARG ALA GLN ILE ALA GLN THR
SEQRES 21 E 332 LEU GLY PRO GLU ALA ALA ALA ARG ALA ALA GLN MET GLN
SEQRES 22 E 332 GLN ASP ASP GLU ALA TRP GLN THR ARG TYR GLN ALA TYR
SEQRES 23 E 332 ALA ALA GLU ARG ASP ARG ILE ALA ALA GLN GLY LEU ALA
SEQRES 24 E 332 PRO GLN ASP ARG ASP ALA ARG ILE ALA GLN LEU ARG GLN
SEQRES 25 E 332 GLN THR PHE THR ALA PRO GLY GLU ALA ILE ARG ALA ALA
SEQRES 26 E 332 SER LEU ASP ARG GLY ALA GLY
MODRES 2ES4 CEA D 92 CYS S-HYDROXY-CYSTEINE
MODRES 2ES4 CEA E 92 CYS S-HYDROXY-CYSTEINE
HET CEA D 92 7
HET CEA E 92 7
HET CA 999 1
HET CA 998 1
HET IOD 901 1
HET IOD 902 1
HET IOD 903 1
HET IOD 904 1
HET IOD 905 1
HET IOD 906 1
HET IOD 907 1
HET IOD 908 1
HETNAM CEA S-HYDROXY-CYSTEINE
HETNAM CA CALCIUM ION
HETNAM IOD IODIDE ION
HETSYN CEA CYSTEINE SULFENIC ACID
FORMUL 2 CEA 2(C3 H7 N1 O3 S1)
FORMUL 5 CA 2(CA1 2+)
FORMUL 7 IOD 8(I1 1-)
FORMUL 15 HOH *843(H2 O1)
HELIX 1 1 GLY A 32 HIS A 40 1 9
HELIX 2 2 GLY A 60 GLY A 77 1 18
HELIX 3 3 SER A 87 ALA A 100 1 14
HELIX 4 4 SER A 117 LEU A 127 1 11
HELIX 5 5 SER A 136 THR A 148 1 13
HELIX 6 6 ASN A 155 ALA A 163 1 9
HELIX 7 7 LEU A 164 LEU A 167 5 4
HELIX 8 8 THR A 168 PHE A 179 1 12
HELIX 9 9 VAL A 236 ASP A 241 1 6
HELIX 10 10 PRO A 242 ASN A 256 1 15
HELIX 11 11 SER A 267 LEU A 272 1 6
HELIX 12 12 LEU A 286 ASN A 290 5 5
HELIX 13 13 ASP A 302 GLN A 317 1 16
HELIX 14 14 ARG D 83 THR D 94 1 12
HELIX 15 15 ALA D 95 LEU D 99 5 5
HELIX 16 16 THR D 100 ASP D 117 1 18
HELIX 17 17 SER D 119 ALA D 138 1 20
HELIX 18 18 ASP D 154 ASP D 170 1 17
HELIX 19 19 TRP D 176 ASN D 199 1 24
HELIX 20 20 GLN D 207 ASP D 216 1 10
HELIX 21 21 THR D 220 ALA D 246 1 27
HELIX 22 22 THR D 249 GLN D 259 1 11
HELIX 23 23 GLY D 262 ALA D 295 1 34
HELIX 24 24 ALA D 299 PHE D 315 1 17
HELIX 25 25 GLY D 319 ARG D 329 1 11
HELIX 26 26 GLY B 32 HIS B 40 1 9
HELIX 27 27 GLY B 60 GLY B 77 1 18
HELIX 28 28 SER B 87 ALA B 100 1 14
HELIX 29 29 SER B 117 LYS B 128 1 12
HELIX 30 30 SER B 136 GLY B 147 1 12
HELIX 31 31 THR B 148 VAL B 150 5 3
HELIX 32 32 ASN B 155 ALA B 163 1 9
HELIX 33 33 LEU B 164 LEU B 167 5 4
HELIX 34 34 THR B 168 PHE B 179 1 12
HELIX 35 35 VAL B 236 ASP B 241 1 6
HELIX 36 36 PRO B 242 ARG B 257 1 16
HELIX 37 37 SER B 267 LEU B 272 1 6
HELIX 38 38 LEU B 286 ASN B 290 5 5
HELIX 39 39 ASP B 302 GLN B 317 1 16
HELIX 40 40 THR E 82 THR E 94 1 13
HELIX 41 41 ALA E 95 LEU E 99 5 5
HELIX 42 42 THR E 100 ASP E 117 1 18
HELIX 43 43 SER E 119 ALA E 138 1 20
HELIX 44 44 ASP E 154 ALA E 169 1 16
HELIX 45 45 ARG E 171 GLU E 175 5 5
HELIX 46 46 TRP E 176 ASN E 199 1 24
HELIX 47 47 SER E 204 ASP E 216 1 13
HELIX 48 48 ALA E 217 LEU E 219 5 3
HELIX 49 49 THR E 220 ALA E 246 1 27
HELIX 50 50 THR E 249 GLY E 262 1 14
HELIX 51 51 GLY E 262 ALA E 294 1 33
HELIX 52 52 GLN E 301 PHE E 315 1 15
HELIX 53 53 GLY E 319 GLY E 330 1 12
SHEET 1 A 6 VAL A 44 VAL A 46 0
SHEET 2 A 6 VAL A 11 VAL A 14 1 N VAL A 11 O TYR A 45
SHEET 3 A 6 VAL A 81 HIS A 86 1 O ILE A 84 N VAL A 14
SHEET 4 A 6 VAL A 104 ILE A 110 1 O ILE A 110 N GLY A 85
SHEET 5 A 6 SER 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 VAL A 11 VAL A 14 1 N VAL A 11 O TYR A 45
SHEET 3 B 6 VAL A 81 HIS A 86 1 O ILE A 84 N VAL A 14
SHEET 4 B 6 VAL A 104 ILE A 110 1 O ILE A 110 N GLY A 85
SHEET 5 B 6 SER A 202 GLY A 211 1 O TYR A 207 N VAL A 107
SHEET 6 B 6 GLN A 275 TYR A 281 1 O ILE A 277 N SER A 208
SHEET 1 C 2 LYS A 22 PHE A 23 0
SHEET 2 C 2 VAL A 27 ASP A 28 -1 O VAL A 27 N PHE A 23
SHEET 1 D 2 ILE A 214 PRO A 216 0
SHEET 2 D 2 ALA A 226 ASP A 228 -1 O THR A 227 N GLN A 215
SHEET 1 E 6 VAL B 44 VAL B 46 0
SHEET 2 E 6 VAL B 11 VAL B 14 1 N VAL B 11 O TYR B 45
SHEET 3 E 6 VAL B 81 HIS B 86 1 O ILE B 84 N VAL B 14
SHEET 4 E 6 VAL B 104 ILE B 110 1 O THR B 108 N GLY B 85
SHEET 5 E 6 SER B 202 GLY B 211 1 O LEU B 205 N VAL B 107
SHEET 6 E 6 THR B 196 VAL B 199 -1 N GLU B 197 O HIS B 204
SHEET 1 F 6 VAL B 44 VAL B 46 0
SHEET 2 F 6 VAL B 11 VAL B 14 1 N VAL B 11 O TYR B 45
SHEET 3 F 6 VAL B 81 HIS B 86 1 O ILE B 84 N VAL B 14
SHEET 4 F 6 VAL B 104 ILE B 110 1 O THR B 108 N GLY B 85
SHEET 5 F 6 SER B 202 GLY B 211 1 O LEU B 205 N VAL B 107
SHEET 6 F 6 GLN B 275 TYR B 281 1 O ILE B 277 N SER B 208
SHEET 1 G 2 LYS B 22 PHE B 23 0
SHEET 2 G 2 VAL B 27 ASP B 28 -1 O VAL B 27 N PHE B 23
SHEET 1 H 2 ILE B 214 THR B 217 0
SHEET 2 H 2 GLY B 225 ASP B 228 -1 O THR B 227 N GLN B 215
SSBOND 1 CYS A 190 CYS A 269
SSBOND 2 CYS B 190 CYS B 269
CISPEP 1 GLN A 291 LEU A 292 0 -0.13
CISPEP 2 GLN B 291 LEU B 292 0 -0.27
CRYST1 183.000 75.700 116.600 90.00 117.60 90.00 C 1 2 1 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 0.005464 0.000000 0.002857 0.00000
SCALE2 0.000000 0.013210 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009678 0.00000
TER 2304 VAL A 319
TER 4297 GLY D 332
TER 6590 VAL B 319
TER 8614 GLY E 330
MASTER 552 0 12 53 32 0 0 6 9463 4 18 102
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