HEADER HYDROLASE/INHIBITOR 08-AUG-17 5Y5E
TITLE CRYSTAL STRUCTURE OF PHOSPHOLIPASE A2 WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROUP IIE SECRETORY PHOSPHOLIPASE A2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 20-142;
COMPND 5 SYNONYM: SPLA2-IIE,PHOSPHATIDYLCHOLINE 2-ACYLHYDROLASE 2E;
COMPND 6 EC: 3.1.1.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLA2G2E;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGAPZAA
KEYWDS MUTANT, HYDROLASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HOU,J.XU,T.XU,J.LIU
REVDAT 2 22-NOV-23 5Y5E 1 REMARK
REVDAT 1 20-JUN-18 5Y5E 0
JRNL AUTH S.HOU,T.XU,J.XU,L.QU,Y.XU,L.CHEN,J.LIU
JRNL TITL STRUCTURAL BASIS FOR FUNCTIONAL SELECTIVITY AND LIGAND
JRNL TITL 2 RECOGNITION REVEALED BY CRYSTAL STRUCTURES OF HUMAN SECRETED
JRNL TITL 3 PHOSPHOLIPASE A2GROUP IIE
JRNL REF SCI REP V. 7 10815 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28883454
JRNL DOI 10.1038/S41598-017-11219-8
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 17182
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 913
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1205
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 951
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.26000
REMARK 3 B33 (A**2) : -0.28000
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): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.341
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1064 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 949 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1445 ; 1.617 ; 2.008
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2195 ; 1.038 ; 3.006
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 126 ; 4.849 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 47 ;35.082 ;22.340
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 168 ;13.503 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;15.790 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 139 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1190 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 259 ; 0.004 ; 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 5Y5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004709.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD RUBY CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.30
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18109
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 18.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.44800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5WZM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2M SODIUM CHLORIDE, 0.1M BIS-TRIS
REMARK 280 PROPANE PH 7.0, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 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 X+1/2,-Y,-Z
REMARK 290 4555 -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 24.36300
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 24.36300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 392 LIES ON A SPECIAL POSITION.
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 ASN A 1
REMARK 465 LEU A 2
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 ASP A 22 41.61 -142.88
REMARK 500 HIS A 33 -164.64 69.61
REMARK 500 SER A 70 -169.59 -118.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 444 DISTANCE = 7.62 ANGSTROMS
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 208 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 26 O
REMARK 620 2 GLY A 28 O 88.2
REMARK 620 3 GLY A 30 O 98.3 89.0
REMARK 620 4 ASP A 47 OD1 115.1 129.5 127.1
REMARK 620 5 ASP A 47 OD2 106.5 164.0 82.8 49.9
REMARK 620 6 7W3 A 202 OAO 143.9 69.9 109.1 65.6 99.9
REMARK 620 7 7W3 A 202 OAT 76.6 65.6 154.1 76.7 123.1 68.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 210 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 81 OG1
REMARK 620 2 HOH A 421 O 115.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7W3 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B3P A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 210
DBREF 5Y5E A 1 123 UNP Q9NZK7 PA2GE_HUMAN 20 142
SEQADV 5Y5E GLY A 21 UNP Q9NZK7 ASN 40 ENGINEERED MUTATION
SEQRES 1 A 123 ASN LEU VAL GLN PHE GLY VAL MET ILE GLU LYS MET THR
SEQRES 2 A 123 GLY LYS SER ALA LEU GLN TYR GLY ASP TYR GLY CYS TYR
SEQRES 3 A 123 CYS GLY ILE GLY GLY SER HIS TRP PRO VAL ASP GLN THR
SEQRES 4 A 123 ASP TRP CYS CYS HIS ALA HIS ASP CYS CYS TYR GLY ARG
SEQRES 5 A 123 LEU GLU LYS LEU GLY CYS GLU PRO LYS LEU GLU LYS TYR
SEQRES 6 A 123 LEU PHE SER VAL SER GLU ARG GLY ILE PHE CYS ALA GLY
SEQRES 7 A 123 ARG THR THR CYS GLN ARG LEU THR CYS GLU CYS ASP LYS
SEQRES 8 A 123 ARG ALA ALA LEU CYS PHE ARG ARG ASN LEU GLY THR TYR
SEQRES 9 A 123 ASN ARG LYS TYR ALA HIS TYR PRO ASN LYS LEU CYS THR
SEQRES 10 A 123 GLY PRO THR PRO PRO CYS
HET GOL A 201 6
HET 7W3 A 202 31
HET CL A 203 1
HET CL A 204 1
HET CL A 205 1
HET CL A 206 1
HET CL A 207 1
HET CA A 208 1
HET B3P A 209 19
HET NA A 210 1
HETNAM GOL GLYCEROL
HETNAM 7W3 2-[2-METHYL-3-OXAMOYL-1-[[2-(TRIFLUOROMETHYL)
HETNAM 2 7W3 PHENYL]METHYL]INDOL-4-YL]OXYETHANOIC ACID
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-
HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 7W3 C21 H17 F3 N2 O5
FORMUL 4 CL 5(CL 1-)
FORMUL 9 CA CA 2+
FORMUL 10 B3P C11 H26 N2 O6
FORMUL 11 NA NA 1+
FORMUL 12 HOH *144(H2 O)
HELIX 1 AA1 VAL A 3 GLY A 14 1 12
HELIX 2 AA2 SER A 16 TYR A 20 5 5
HELIX 3 AA3 ASP A 37 LEU A 56 1 20
HELIX 4 AA4 THR A 80 ASN A 100 1 21
HELIX 5 AA5 LEU A 101 TYR A 104 5 4
HELIX 6 AA6 ASN A 105 ALA A 109 5 5
HELIX 7 AA7 PRO A 112 CYS A 116 5 5
SHEET 1 AA1 2 LEU A 66 SER A 70 0
SHEET 2 AA1 2 GLY A 73 ALA A 77 -1 O PHE A 75 N SER A 68
SSBOND 1 CYS A 25 CYS A 116 1555 1555 2.02
SSBOND 2 CYS A 27 CYS A 43 1555 1555 2.02
SSBOND 3 CYS A 42 CYS A 96 1555 1555 2.05
SSBOND 4 CYS A 48 CYS A 123 1555 1555 2.03
SSBOND 5 CYS A 49 CYS A 89 1555 1555 2.03
SSBOND 6 CYS A 58 CYS A 82 1555 1555 2.01
SSBOND 7 CYS A 76 CYS A 87 1555 1555 2.01
LINK O TYR A 26 CA CA A 208 1555 1555 2.19
LINK O GLY A 28 CA CA A 208 1555 1555 2.30
LINK O GLY A 30 CA CA A 208 1555 1555 2.33
LINK OD1 ASP A 47 CA CA A 208 1555 1555 2.71
LINK OD2 ASP A 47 CA CA A 208 1555 1555 2.44
LINK OG1 THR A 81 NA NA A 210 1555 1555 2.85
LINK OAO 7W3 A 202 CA CA A 208 1555 1555 2.74
LINK OAT 7W3 A 202 CA CA A 208 1555 1555 2.64
LINK NA NA A 210 O HOH A 421 1555 4555 2.77
SITE 1 AC1 6 CYS A 49 ARG A 52 LEU A 53 GLU A 88
SITE 2 AC1 6 ARG A 92 HOH A 369
SITE 1 AC2 17 PHE A 5 GLY A 6 ALA A 17 LEU A 18
SITE 2 AC2 17 GLY A 21 TYR A 26 CYS A 27 GLY A 28
SITE 3 AC2 17 ILE A 29 GLY A 30 CYS A 43 HIS A 46
SITE 4 AC2 17 ASP A 47 LYS A 61 CA A 208 HOH A 329
SITE 5 AC2 17 HOH A 332
SITE 1 AC3 2 ASP A 37 GLN A 38
SITE 1 AC4 3 ARG A 106 HOH A 403 HOH A 417
SITE 1 AC5 2 SER A 68 VAL A 69
SITE 1 AC6 5 ALA A 45 CYS A 49 ARG A 52 ARG A 92
SITE 2 AC6 5 HOH A 436
SITE 1 AC7 3 GLY A 73 ILE A 74 LYS A 91
SITE 1 AC8 5 TYR A 26 GLY A 28 GLY A 30 ASP A 47
SITE 2 AC8 5 7W3 A 202
SITE 1 AC9 3 GLN A 4 LEU A 66 PHE A 67
SITE 1 AD1 3 THR A 81 CYS A 82 HOH A 421
CRYST1 48.726 61.063 63.356 90.00 90.00 90.00 P 21 2 2 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 0.020523 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016377 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015784 0.00000
(ATOM LINES ARE NOT SHOWN.)
END