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HEADER TRANSFERASE 11-DEC-14 4X93
TITLE CRYSTAL STRUCTURE OF LYSOSOMAL PHOSPHOLIPASE A2 CRYSTALLIZED IN THE
TITLE 2 PRESENCE OF METHYL ARACHIDONYL FLUOROPHOSPHONATE (TETRAGONAL FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROUP XV PHOSPHOLIPASE A2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 34-412;
COMPND 5 SYNONYM: 1-O-ACYLCERAMIDE SYNTHASE,ACS,LCAT-LIKE LYSOPHOSPHOLIPASE,
COMPND 6 LLPL,LYSOPHOSPHOLIPASE 3,LYSOSOMAL PHOSPHOLIPASE A2,LPLA2;
COMPND 7 EC: 2.3.1.-;
COMPND 8 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: PLA2G15, LYPLA3, UNQ341/PRO540;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;
SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022
KEYWDS HYDROLASE, PHOSPHOLIPASE, ESTERASE, ACYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GLUKHOVA,J.J.G.TESMER
REVDAT 1 25-MAR-15 4X93 0
JRNL AUTH A.GLUKHOVA,V.HINKOVSKA-GALCHEVA,R.KELLY,A.ABE,J.A.SHAYMAN,
JRNL AUTH 2 J.J.TESMER
JRNL TITL STRUCTURE AND FUNCTION OF LYSOSOMAL PHOSPHOLIPASE A2 AND
JRNL TITL 2 LECITHIN:CHOLESTEROL ACYLTRANSFERASE.
JRNL REF NAT COMMUN V. 6 6250 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 25727495
JRNL DOI 10.1038/NCOMMS7250
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 42161
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2158
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3054
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6049
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 174
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.67000
REMARK 3 B22 (A**2) : 0.67000
REMARK 3 B33 (A**2) : -1.34000
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): 0.326
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.225
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.175
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.517
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6488 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6054 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8822 ; 1.240 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13916 ; 0.869 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 765 ; 5.914 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 292 ;35.107 ;23.493
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1011 ;12.608 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;11.200 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 966 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7179 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1507 ; 0.003 ; 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): 3051 ; 1.484 ; 3.877
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3050 ; 1.484 ; 3.875
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3813 ; 2.542 ; 5.812
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 4 378 B 4 378 23361 0.070 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 385
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9694 86.6045 65.8475
REMARK 3 T TENSOR
REMARK 3 T11: 0.2837 T22: 0.0702
REMARK 3 T33: 0.0072 T12: 0.0562
REMARK 3 T13: -0.0078 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 1.4662 L22: 1.2504
REMARK 3 L33: 2.1161 L12: 0.4173
REMARK 3 L13: -1.1085 L23: -0.5144
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: -0.0694 S13: -0.0277
REMARK 3 S21: -0.2888 S22: -0.0274 S23: -0.0289
REMARK 3 S31: -0.0410 S32: 0.1720 S33: -0.0165
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 397
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3750 79.1221 21.6907
REMARK 3 T TENSOR
REMARK 3 T11: 0.1884 T22: 0.2236
REMARK 3 T33: 0.1080 T12: -0.0830
REMARK 3 T13: 0.0711 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 1.4174 L22: 1.8129
REMARK 3 L33: 2.3236 L12: 0.0627
REMARK 3 L13: 0.2363 L23: 0.4705
REMARK 3 S TENSOR
REMARK 3 S11: 0.0584 S12: -0.0224 S13: 0.0378
REMARK 3 S21: 0.1609 S22: -0.1614 S23: 0.3851
REMARK 3 S31: 0.0575 S32: -0.6038 S33: 0.1030
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 : WITH TLS ADDED
REMARK 4
REMARK 4 4X93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205258.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44707
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : 0.15900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.70
REMARK 200 R MERGE FOR SHELL (I) : 0.85500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: 4X90
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5, 30% PEG MME 550,
REMARK 280 50 MM MGCL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 182.92400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.41000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.41000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 274.38600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.41000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.41000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 91.46200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.41000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.41000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 274.38600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.41000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.41000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 91.46200
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 182.92400
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 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 GLY A 0
REMARK 465 ALA A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLY B 0
REMARK 465 ALA B 1
REMARK 465 GLY B 2
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 OD1 ASN B 212 N ASN B 213 1.60
REMARK 500 O ARG B 214 CG1 ILE B 215 1.61
REMARK 500 ND2 ASN A 256 O5 NAG A 403 1.95
REMARK 500 O ASN B 212 N ARG B 214 1.98
REMARK 500 ND2 ASN B 365 O5 NAG B 404 2.04
REMARK 500 O1S EPE B 405 O HOH B 546 2.12
REMARK 500 ND2 ASN B 240 O5 NAG B 402 2.12
REMARK 500 N VAL B 52 O HOH B 501 2.13
REMARK 500 ND2 ASN A 240 O5 NAG A 402 2.15
REMARK 500 ND2 ASN B 66 O5 NAG B 401 2.16
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 PRO B 51 N - CA - C ANGL. DEV. = 22.8 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 ASP A 23 70.55 -151.65
REMARK 500 VAL A 52 -15.76 -49.23
REMARK 500 ILE A 53 -3.89 -144.96
REMARK 500 TYR A 104 -79.51 -125.39
REMARK 500 GLU A 121 -92.61 -113.03
REMARK 500 SER A 165 -130.03 56.79
REMARK 500 THR A 329 -54.73 -127.73
REMARK 500 ASP B 23 70.28 -151.96
REMARK 500 TYR B 104 -80.31 -125.48
REMARK 500 GLU B 121 -90.99 -111.61
REMARK 500 SER B 165 -130.67 56.89
REMARK 500 ASN B 212 -79.57 -102.89
REMARK 500 ASN B 213 -25.69 42.86
REMARK 500 ILE B 215 85.64 155.92
REMARK 500 THR B 329 -54.58 -127.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PE8 B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound
REMARK 800 to ASN A 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 402 bound
REMARK 800 to ASN A 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 403 bound
REMARK 800 to ASN A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 404 bound
REMARK 800 to ASN A 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 401 bound
REMARK 800 to ASN B 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 402 bound
REMARK 800 to ASN B 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 403 bound
REMARK 800 to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 404 bound
REMARK 800 to ASN B 365
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X90 RELATED DB: PDB
REMARK 900 RELATED ID: 4X91 RELATED DB: PDB
REMARK 900 RELATED ID: 4X92 RELATED DB: PDB
REMARK 900 RELATED ID: 4X94 RELATED DB: PDB
REMARK 900 RELATED ID: 4X95 RELATED DB: PDB
REMARK 900 RELATED ID: 4X96 RELATED DB: PDB
REMARK 900 RELATED ID: 4X97 RELATED DB: PDB
DBREF 4X93 A 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 4X93 B 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
SEQADV 4X93 GLY A 0 UNP Q8NCC3 CLONING ARTIFACT
SEQADV 4X93 GLY B 0 UNP Q8NCC3 CLONING ARTIFACT
SEQRES 1 A 380 GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY
SEQRES 2 A 380 ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO
SEQRES 3 A 380 THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER
SEQRES 4 A 380 TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 5 A 380 VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL
SEQRES 6 A 380 TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY
SEQRES 7 A 380 VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER
SEQRES 8 A 380 LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER
SEQRES 9 A 380 TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY
SEQRES 10 A 380 TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP
SEQRES 11 A 380 TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU
SEQRES 12 A 380 ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR
SEQRES 13 A 380 GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN
SEQRES 14 A 380 MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA
SEQRES 15 A 380 TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY
SEQRES 16 A 380 ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU
SEQRES 17 A 380 ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO
SEQRES 18 A 380 LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR
SEQRES 19 A 380 SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU
SEQRES 20 A 380 LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU
SEQRES 21 A 380 ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU
SEQRES 22 A 380 ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL
SEQRES 23 A 380 GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU
SEQRES 24 A 380 TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR
SEQRES 25 A 380 GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY
SEQRES 26 A 380 ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN
SEQRES 27 A 380 CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU
SEQRES 28 A 380 LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU
SEQRES 29 A 380 ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU
SEQRES 30 A 380 LEU GLY PRO
SEQRES 1 B 380 GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY
SEQRES 2 B 380 ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO
SEQRES 3 B 380 THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER
SEQRES 4 B 380 TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 5 B 380 VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL
SEQRES 6 B 380 TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY
SEQRES 7 B 380 VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER
SEQRES 8 B 380 LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER
SEQRES 9 B 380 TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY
SEQRES 10 B 380 TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP
SEQRES 11 B 380 TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU
SEQRES 12 B 380 ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR
SEQRES 13 B 380 GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN
SEQRES 14 B 380 MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA
SEQRES 15 B 380 TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY
SEQRES 16 B 380 ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU
SEQRES 17 B 380 ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO
SEQRES 18 B 380 LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR
SEQRES 19 B 380 SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU
SEQRES 20 B 380 LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU
SEQRES 21 B 380 ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU
SEQRES 22 B 380 ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL
SEQRES 23 B 380 GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU
SEQRES 24 B 380 TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR
SEQRES 25 B 380 GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY
SEQRES 26 B 380 ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN
SEQRES 27 B 380 CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU
SEQRES 28 B 380 LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU
SEQRES 29 B 380 ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU
SEQRES 30 B 380 LEU GLY PRO
HET NAG A 401 14
HET NAG A 402 14
HET NAG A 403 14
HET NAG A 404 14
HET EPE A 405 15
HET NAG B 401 14
HET NAG B 402 14
HET NAG B 403 14
HET NAG B 404 14
HET EPE B 405 15
HET PEG B 406 7
HET PE8 B 407 25
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL
HETSYN EPE HEPES
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 7 EPE 2(C8 H18 N2 O4 S)
FORMUL 13 PEG C4 H10 O3
FORMUL 14 PE8 C16 H34 O9
FORMUL 15 HOH *91(H2 O)
HELIX 1 AA1 ASN A 45 LEU A 49 5 5
HELIX 2 AA2 LEU A 50 ARG A 62 1 13
HELIX 3 AA3 THR A 88 PHE A 93 1 6
HELIX 4 AA4 SER A 99 SER A 103 5 5
HELIX 5 AA5 PHE A 105 TRP A 115 1 11
HELIX 6 AA6 ALA A 133 GLU A 136 5 4
HELIX 7 AA7 ASN A 137 GLY A 156 1 20
HELIX 8 AA8 MET A 166 ARG A 177 1 12
HELIX 9 AA9 PRO A 179 TYR A 186 1 8
HELIX 10 AB1 LYS A 202 GLY A 210 1 9
HELIX 11 AB2 GLY A 219 ALA A 230 1 12
HELIX 12 AB3 ALA A 230 LEU A 236 1 7
HELIX 13 AB4 ASP A 261 ILE A 269 1 9
HELIX 14 AB5 GLU A 272 GLU A 282 1 11
HELIX 15 AB6 ASN A 331 SER A 334 5 4
HELIX 16 AB7 ALA A 335 GLN A 342 1 8
HELIX 17 AB8 ILE A 360 ALA A 364 5 5
HELIX 18 AB9 ASN A 365 GLY A 378 1 14
HELIX 19 AC1 ASN B 45 LEU B 50 5 6
HELIX 20 AC2 VAL B 52 ARG B 62 1 11
HELIX 21 AC3 THR B 88 PHE B 93 1 6
HELIX 22 AC4 SER B 99 SER B 103 5 5
HELIX 23 AC5 PHE B 105 TRP B 115 1 11
HELIX 24 AC6 ALA B 133 GLU B 136 5 4
HELIX 25 AC7 ASN B 137 GLY B 156 1 20
HELIX 26 AC8 MET B 166 ARG B 177 1 12
HELIX 27 AC9 PRO B 179 TYR B 186 1 8
HELIX 28 AD1 ALA B 201 GLY B 210 1 10
HELIX 29 AD2 GLY B 219 ALA B 230 1 12
HELIX 30 AD3 ALA B 230 LEU B 236 1 7
HELIX 31 AD4 ASP B 261 ILE B 269 1 9
HELIX 32 AD5 GLU B 272 GLU B 282 1 11
HELIX 33 AD6 ASN B 331 SER B 334 5 4
HELIX 34 AD7 ALA B 335 GLN B 342 1 8
HELIX 35 AD8 ILE B 360 ALA B 364 5 5
HELIX 36 AD9 ASN B 365 GLY B 378 1 14
SHEET 1 AA1 6 VAL A 123 GLY A 125 0
SHEET 2 AA1 6 VAL A 7 VAL A 10 1 N LEU A 9 O ARG A 124
SHEET 3 AA1 6 VAL A 159 HIS A 164 1 O VAL A 162 N VAL A 8
SHEET 4 AA1 6 ILE A 187 LEU A 193 1 O VAL A 191 N LEU A 161
SHEET 5 AA1 6 LEU A 295 THR A 301 1 O HIS A 296 N SER A 192
SHEET 6 AA1 6 VAL A 349 PRO A 355 1 O LEU A 350 N LEU A 295
SHEET 1 AA2 3 PHE A 40 TRP A 43 0
SHEET 2 AA2 3 LEU A 18 LEU A 22 -1 N ALA A 20 O PHE A 40
SHEET 3 AA2 3 VAL A 78 ARG A 81 -1 O ARG A 81 N GLU A 19
SHEET 1 AA3 2 VAL A 64 ASN A 66 0
SHEET 2 AA3 2 ALA A 71 GLN A 73 -1 O GLN A 73 N VAL A 64
SHEET 1 AA4 4 ASN A 256 TYR A 257 0
SHEET 2 AA4 4 VAL A 250 GLN A 251 -1 N VAL A 250 O TYR A 257
SHEET 3 AA4 4 THR A 305 TYR A 310 1 O PHE A 309 N GLN A 251
SHEET 4 AA4 4 LYS A 320 GLY A 324 -1 O CYS A 322 N ASP A 307
SHEET 1 AA5 6 VAL B 123 GLY B 125 0
SHEET 2 AA5 6 VAL B 7 VAL B 10 1 N LEU B 9 O ARG B 124
SHEET 3 AA5 6 VAL B 159 HIS B 164 1 O VAL B 162 N VAL B 8
SHEET 4 AA5 6 ILE B 187 LEU B 193 1 O VAL B 191 N LEU B 161
SHEET 5 AA5 6 LEU B 295 THR B 301 1 O HIS B 296 N SER B 192
SHEET 6 AA5 6 VAL B 349 PRO B 355 1 O LEU B 350 N LEU B 295
SHEET 1 AA6 3 PHE B 40 TRP B 43 0
SHEET 2 AA6 3 LEU B 18 LEU B 22 -1 N ALA B 20 O PHE B 40
SHEET 3 AA6 3 VAL B 78 ARG B 81 -1 O ARG B 81 N GLU B 19
SHEET 1 AA7 2 VAL B 64 ASN B 66 0
SHEET 2 AA7 2 ALA B 71 GLN B 73 -1 O GLN B 73 N VAL B 64
SHEET 1 AA8 4 ASN B 256 TYR B 257 0
SHEET 2 AA8 4 VAL B 250 GLN B 251 -1 N VAL B 250 O TYR B 257
SHEET 3 AA8 4 THR B 305 TYR B 310 1 O PHE B 309 N GLN B 251
SHEET 4 AA8 4 LYS B 320 GLY B 324 -1 O CYS B 322 N ASP B 307
SSBOND 1 CYS A 32 CYS A 56 1555 1555 2.05
SSBOND 2 CYS B 32 CYS B 56 1555 1555 2.07
LINK ND2 ASN A 66 C1 NAG A 401 1555 1555 1.43
LINK ND2 ASN A 240 C1 NAG A 402 1555 1555 1.43
LINK ND2 ASN A 256 C1 NAG A 403 1555 1555 1.44
LINK ND2 ASN A 365 C1 NAG A 404 1555 1555 1.43
LINK ND2 ASN B 66 C1 NAG B 401 1555 1555 1.43
LINK ND2 ASN B 240 C1 NAG B 402 1555 1555 1.43
LINK ND2 ASN B 256 C1 NAG B 403 1555 1555 1.44
LINK ND2 ASN B 365 C1 NAG B 404 1555 1555 1.44
CISPEP 1 TRP A 43 LEU A 44 0 -1.74
CISPEP 2 PHE A 314 PRO A 315 0 5.94
CISPEP 3 TRP B 43 LEU B 44 0 -2.07
CISPEP 4 PHE B 314 PRO B 315 0 2.00
SITE 1 AC1 9 CYS A 32 SER A 33 PHE A 40 ASN A 60
SITE 2 AC1 9 HOH A 527 HOH A 537 HOH A 538 TYR B 30
SITE 3 AC1 9 HOH B 502
SITE 1 AC2 6 SER B 33 LEU B 48 CYS B 56 ASN B 60
SITE 2 AC2 6 HOH B 541 HOH B 546
SITE 1 AC3 3 SER B 165 VAL B 200 HOH B 538
SITE 1 AC4 3 GLY B 302 PRO B 304 GLY B 324
SITE 1 AC5 3 ASN A 66 SER A 69 GLN A 73
SITE 1 AC6 2 ASN A 240 GLU A 282
SITE 1 AC7 4 VAL A 248 GLN A 251 ASN A 256 GLN B 251
SITE 1 AC8 4 PRO A 355 GLU A 361 ASN A 365 THR A 367
SITE 1 AC9 2 ASN B 66 GLN B 73
SITE 1 AD1 2 ASN B 240 GLU B 282
SITE 1 AD2 5 THR A 254 ILE A 255 ASN A 256 GLN B 251
SITE 2 AD2 5 ASN B 256
SITE 1 AD3 4 PRO B 355 GLU B 361 ASN B 365 THR B 367
CRYST1 86.820 86.820 365.848 90.00 90.00 90.00 P 43 21 2 16
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 0.011518 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011518 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002733 0.00000
TER 3026 PRO A 379
TER 6125 PRO B 379
MASTER 445 0 12 36 30 0 16 6 6314 2 186 60
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