HEADER LIPID BINDING PROTEIN 31-AUG-17 5OW8
TITLE INDOLE-2 CARBOXAMIDES AS SELECTIVE SECRETED PHOSPHOLIPASE A2 TYPE X
TITLE 2 (SPLA2-X) INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROUP 10 SECRETORY PHOSPHOLIPASE A2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GROUP X SECRETORY PHOSPHOLIPASE A2,SPLA2-X,
COMPND 5 PHOSPHATIDYLCHOLINE 2-ACYLHYDROLASE 10;
COMPND 6 EC: 3.1.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLA2G10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: GOLD;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS INHIBITOR, SECRETED, PHOSPHOLIPASE, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.SANDMARK,R.G.ROTH,L.KNERR,C.BODIN,D.PETTERSEN
REVDAT 2 05-MAY-21 5OW8 1 JRNL REMARK LINK
REVDAT 1 01-AUG-18 5OW8 0
JRNL AUTH L.KNERR,F.GIORDANETTO,P.NORDBERG,D.PETTERSEN,N.SELMI,
JRNL AUTH 2 H.G.BEISEL,H.DE LA MOTTE,T.OLSSON,T.D.J.PERKINS,M.HERSLOF,
JRNL AUTH 3 A.MANSSON,M.DAHLSTROM,I.STARKE,J.BRODDEFALK,G.SAARINEN,
JRNL AUTH 4 F.KLINGEGARD,E.HURT-CAMEJO,B.ROSENGREN,J.BRENGDAHL,F.JANSEN,
JRNL AUTH 5 M.ROHMAN,J.SANDMARK,K.HALLBERG,T.AKERUD,R.G.ROTH,M.AHLQVIST
JRNL TITL DISCOVERY OF A SERIES OF INDOLE-2 CARBOXAMIDES AS SELECTIVE
JRNL TITL 2 SECRETED PHOSPHOLIPASE A2TYPE X (SPLA2-X) INHIBITORS.
JRNL REF ACS MED.CHEM.LETT. V. 9 594 2018
JRNL REFN ISSN 1948-5875
JRNL PMID 30034585
JRNL DOI 10.1021/ACSMEDCHEMLETT.7B00505
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 17095
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 + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 950
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 834
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1888
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 117
REMARK 3 SOLVENT ATOMS : 107
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.216
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.589
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2078 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1849 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2814 ; 1.213 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4289 ; 0.937 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 252 ; 5.202 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;35.173 ;24.889
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 314 ;16.491 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;12.751 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 284 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2320 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 442 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5OW8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6-5.9
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 FR-E+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19430
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 44.083
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 1.05700
REMARK 200 R SYM FOR SHELL (I) : 1.05700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 37-45% PEG400 0.1M BIS-TRIS PH 5.6
REMARK 280 -5.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 13.82600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.47700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.68350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.47700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 13.82600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.68350
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 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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 26 O
REMARK 620 2 GLY A 28 O 89.7
REMARK 620 3 GLY A 30 O 93.1 79.9
REMARK 620 4 ASP A 47 OD1 103.8 150.9 124.1
REMARK 620 5 ASP A 47 OD2 92.4 156.5 76.6 50.2
REMARK 620 6 DMS A 203 O 174.0 84.4 85.3 81.8 92.8
REMARK 620 7 AYN A 206 O11 79.9 75.2 154.1 81.8 128.2 99.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 26 O
REMARK 620 2 GLY B 28 O 94.0
REMARK 620 3 GLY B 30 O 92.5 82.5
REMARK 620 4 ASP B 47 OD1 103.4 147.1 123.7
REMARK 620 5 ASP B 47 OD2 89.9 159.0 76.8 50.2
REMARK 620 6 DMS B 202 O 175.0 81.9 89.6 79.1 95.0
REMARK 620 7 AYN B 206 O11 80.1 74.1 154.8 81.5 126.9 96.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AYN A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AYN B 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 209
DBREF 5OW8 A 1 123 UNP O15496 PA2GX_HUMAN 43 165
DBREF 5OW8 B 1 123 UNP O15496 PA2GX_HUMAN 43 165
SEQRES 1 A 123 GLY ILE LEU GLU LEU ALA GLY THR VAL GLY CYS VAL GLY
SEQRES 2 A 123 PRO ARG THR PRO ILE ALA TYR MET LYS TYR GLY CYS PHE
SEQRES 3 A 123 CYS GLY LEU GLY GLY HIS GLY GLN PRO ARG ASP ALA ILE
SEQRES 4 A 123 ASP TRP CYS CYS HIS GLY HIS ASP CYS CYS TYR THR ARG
SEQRES 5 A 123 ALA GLU GLU ALA GLY CYS SER PRO LYS THR GLU ARG TYR
SEQRES 6 A 123 SER TRP GLN CYS VAL ASN GLN SER VAL LEU CYS GLY PRO
SEQRES 7 A 123 ALA GLU ASN LYS CYS GLN GLU LEU LEU CYS LYS CYS ASP
SEQRES 8 A 123 GLN GLU ILE ALA ASN CYS LEU ALA GLN THR GLU TYR ASN
SEQRES 9 A 123 LEU LYS TYR LEU PHE TYR PRO GLN PHE LEU CYS GLU PRO
SEQRES 10 A 123 ASP SER PRO LYS CYS ASP
SEQRES 1 B 123 GLY ILE LEU GLU LEU ALA GLY THR VAL GLY CYS VAL GLY
SEQRES 2 B 123 PRO ARG THR PRO ILE ALA TYR MET LYS TYR GLY CYS PHE
SEQRES 3 B 123 CYS GLY LEU GLY GLY HIS GLY GLN PRO ARG ASP ALA ILE
SEQRES 4 B 123 ASP TRP CYS CYS HIS GLY HIS ASP CYS CYS TYR THR ARG
SEQRES 5 B 123 ALA GLU GLU ALA GLY CYS SER PRO LYS THR GLU ARG TYR
SEQRES 6 B 123 SER TRP GLN CYS VAL ASN GLN SER VAL LEU CYS GLY PRO
SEQRES 7 B 123 ALA GLU ASN LYS CYS GLN GLU LEU LEU CYS LYS CYS ASP
SEQRES 8 B 123 GLN GLU ILE ALA ASN CYS LEU ALA GLN THR GLU TYR ASN
SEQRES 9 B 123 LEU LYS TYR LEU PHE TYR PRO GLN PHE LEU CYS GLU PRO
SEQRES 10 B 123 ASP SER PRO LYS CYS ASP
HET CA A 201 1
HET DMS A 202 4
HET DMS A 203 4
HET DMS A 204 4
HET DMS A 205 4
HET AYN A 206 22
HET PEG A 207 7
HET PEG A 208 7
HET PEG A 209 7
HET PEG A 210 7
HET CL A 211 1
HET CL A 212 1
HET CA B 201 1
HET DMS B 202 4
HET DMS B 203 4
HET DMS B 204 4
HET DMS B 205 4
HET AYN B 206 22
HET PEG B 207 7
HET CL B 208 1
HET CL B 209 1
HETNAM CA CALCIUM ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM AYN 1-[3-(TRIFLUOROMETHYL)PHENYL]INDOLE-2-CARBOXAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 DMS 8(C2 H6 O S)
FORMUL 8 AYN 2(C16 H11 F3 N2 O)
FORMUL 9 PEG 5(C4 H10 O3)
FORMUL 13 CL 4(CL 1-)
FORMUL 24 HOH *107(H2 O)
HELIX 1 AA1 GLY A 1 GLY A 13 1 13
HELIX 2 AA2 THR A 16 MET A 21 5 6
HELIX 3 AA3 ASP A 37 ALA A 56 1 20
HELIX 4 AA4 ASN A 81 GLN A 100 1 20
HELIX 5 AA5 ASN A 104 LEU A 108 5 5
HELIX 6 AA6 PRO A 111 CYS A 115 5 5
HELIX 7 AA7 ILE B 2 GLY B 13 1 12
HELIX 8 AA8 THR B 16 MET B 21 5 6
HELIX 9 AA9 ASP B 37 ALA B 56 1 20
HELIX 10 AB1 ASN B 81 GLN B 100 1 20
HELIX 11 AB2 ASN B 104 LEU B 108 5 5
HELIX 12 AB3 PRO B 111 CYS B 115 5 5
SHEET 1 AA1 2 TRP A 67 CYS A 69 0
SHEET 2 AA1 2 VAL A 74 CYS A 76 -1 O LEU A 75 N GLN A 68
SHEET 1 AA2 2 TRP B 67 CYS B 69 0
SHEET 2 AA2 2 VAL B 74 CYS B 76 -1 O LEU B 75 N GLN B 68
SSBOND 1 CYS A 11 CYS A 69 1555 1555 2.03
SSBOND 2 CYS A 25 CYS A 115 1555 1555 2.02
SSBOND 3 CYS A 27 CYS A 43 1555 1555 2.03
SSBOND 4 CYS A 42 CYS A 97 1555 1555 2.02
SSBOND 5 CYS A 48 CYS A 122 1555 1555 2.03
SSBOND 6 CYS A 49 CYS A 90 1555 1555 2.03
SSBOND 7 CYS A 58 CYS A 83 1555 1555 2.04
SSBOND 8 CYS A 76 CYS A 88 1555 1555 2.03
SSBOND 9 CYS B 11 CYS B 69 1555 1555 2.03
SSBOND 10 CYS B 25 CYS B 115 1555 1555 2.03
SSBOND 11 CYS B 27 CYS B 43 1555 1555 2.04
SSBOND 12 CYS B 42 CYS B 97 1555 1555 2.04
SSBOND 13 CYS B 48 CYS B 122 1555 1555 2.03
SSBOND 14 CYS B 49 CYS B 90 1555 1555 2.03
SSBOND 15 CYS B 58 CYS B 83 1555 1555 2.04
SSBOND 16 CYS B 76 CYS B 88 1555 1555 2.02
LINK O PHE A 26 CA CA A 201 1555 1555 2.31
LINK O GLY A 28 CA CA A 201 1555 1555 2.30
LINK O GLY A 30 CA CA A 201 1555 1555 2.36
LINK OD1 ASP A 47 CA CA A 201 1555 1555 2.58
LINK OD2 ASP A 47 CA CA A 201 1555 1555 2.55
LINK CA CA A 201 O DMS A 203 1555 1555 2.42
LINK CA CA A 201 O11 AYN A 206 1555 1555 2.48
LINK O PHE B 26 CA CA B 201 1555 1555 2.28
LINK O GLY B 28 CA CA B 201 1555 1555 2.29
LINK O GLY B 30 CA CA B 201 1555 1555 2.34
LINK OD1 ASP B 47 CA CA B 201 1555 1555 2.60
LINK OD2 ASP B 47 CA CA B 201 1555 1555 2.53
LINK CA CA B 201 O DMS B 202 1555 1555 2.33
LINK CA CA B 201 O11 AYN B 206 1555 1555 2.51
CISPEP 1 GLY A 77 PRO A 78 0 -0.97
CISPEP 2 GLY B 13 PRO B 14 0 8.65
CISPEP 3 GLY B 77 PRO B 78 0 -0.40
SITE 1 AC1 6 PHE A 26 GLY A 28 GLY A 30 ASP A 47
SITE 2 AC1 6 DMS A 203 AYN A 206
SITE 1 AC2 4 LEU A 75 CYS A 76 GLN A 92 ALA B 79
SITE 1 AC3 6 GLY A 28 GLY A 30 ASP A 47 TYR A 50
SITE 2 AC3 6 CA A 201 AYN A 206
SITE 1 AC4 6 GLY A 24 CYS A 25 CYS A 27 GLY A 28
SITE 2 AC4 6 GLY A 30 GLY A 31
SITE 1 AC5 5 LYS A 61 VAL A 74 GLN A 92 ASN A 96
SITE 2 AC5 5 HOH A 308
SITE 1 AC6 15 ILE A 2 LEU A 5 PRO A 17 TYR A 20
SITE 2 AC6 15 PHE A 26 GLY A 28 LEU A 29 CYS A 43
SITE 3 AC6 15 HIS A 46 ASP A 47 TYR A 50 LYS A 61
SITE 4 AC6 15 ILE A 94 CA A 201 DMS A 203
SITE 1 AC7 5 SER A 66 GLU A 80 GLN B 68 VAL B 70
SITE 2 AC7 5 LEU B 75
SITE 1 AC8 2 THR A 16 LEU B 108
SITE 1 AC9 1 ARG A 15
SITE 1 AD1 2 TRP A 67 GLN B 34
SITE 1 AD2 1 THR A 16
SITE 1 AD3 2 LYS A 61 GLN A 100
SITE 1 AD4 6 PHE B 26 GLY B 28 GLY B 30 ASP B 47
SITE 2 AD4 6 DMS B 202 AYN B 206
SITE 1 AD5 6 GLY B 28 GLY B 30 ASP B 47 TYR B 50
SITE 2 AD5 6 CA B 201 AYN B 206
SITE 1 AD6 5 PRO A 78 ALA A 79 LEU B 75 CYS B 76
SITE 2 AD6 5 GLN B 92
SITE 1 AD7 5 GLY B 24 CYS B 27 LEU B 29 GLY B 30
SITE 2 AD7 5 GLN B 112
SITE 1 AD8 6 ILE B 2 VAL B 12 LEU B 29 GLN B 72
SITE 2 AD8 6 AYN B 206 HOH B 305
SITE 1 AD9 14 ILE B 2 PRO B 17 TYR B 20 PHE B 26
SITE 2 AD9 14 GLY B 28 LEU B 29 CYS B 43 HIS B 46
SITE 3 AD9 14 ASP B 47 TYR B 50 ILE B 94 CA B 201
SITE 4 AD9 14 DMS B 202 DMS B 205
SITE 1 AE1 4 GLN A 68 VAL A 70 SER B 66 GLU B 80
SITE 1 AE2 1 TRP B 67
CRYST1 27.652 85.367 102.954 90.00 90.00 90.00 P 21 21 21 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 0.036164 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011714 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009713 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
