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HEADER HYDROLASE 29-APR-19 6OR3
TITLE STRUCTURE OF AN ACYL INTERMEDIATE OF THERMOMYCES LANUGINOSA LIPASE
TITLE 2 WITH PALMITIC ACID IN AN ORTHORHOMBIC CRYSTAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;
SOURCE 3 ORGANISM_TAXID: 5541
KEYWDS PRODUCT COMPLEX, ACYL INTERMEDIATE, DIMER, PALMITIC ACID, LIPID
KEYWDS 2 BINDING PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MCPHERSON
REVDAT 1 20-MAY-20 6OR3 0
JRNL AUTH A.MCPHERSON
JRNL TITL THE STRUCTURE OF THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE IN
JRNL TITL 2 COMPLEX WITH ITS CATALYTIC PRODUCTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 43893
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2291
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3164
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.3490
REMARK 3 BIN FREE R VALUE SET COUNT : 196
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2071
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.10000
REMARK 3 B22 (A**2) : 1.92000
REMARK 3 B33 (A**2) : -5.02000
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): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.250
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2219 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2035 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3029 ; 1.688 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4680 ; 1.501 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 288 ; 6.310 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 111 ;34.281 ;23.784
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 328 ;13.371 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;19.379 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 329 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2598 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 551 ; 0.006 ; 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): 1095 ; 5.044 ; 3.156
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1094 ; 5.031 ; 3.154
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1372 ; 5.700 ; 4.737
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1373 ; 5.701 ; 4.738
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1122 ; 7.167 ; 3.628
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1123 ; 7.168 ; 3.631
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1646 ; 7.599 ; 5.298
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10179 ; 7.039 ;62.849
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10180 ; 7.038 ;62.847
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4248 ; 6.703 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 54 ;54.524 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4313 ;25.706 ; 5.000
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 : 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
REMARK 4
REMARK 4 6OR3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1000241161.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-19
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 6.0 - 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1158
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46198
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 60.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 62.80
REMARK 200 R MERGE (I) : 0.33400
REMARK 200 R SYM (I) : 0.32000
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 38.70
REMARK 200 R MERGE FOR SHELL (I) : 3.60000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.600
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: 1TIB
REMARK 200
REMARK 200 REMARK: ORTHORHOMBIC PRISMS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: USING FILTERED CULTURE MEDIA WITH
REMARK 280 ACTIVE FUNGAL CELLS AS THE STOCK PROTEIN SOLUTION, ABOUT 30 MG/
REMARK 280 ML. SITTING DROP EQUAL AMOUNTS OF THE PROTEIN STOCK AND THE
REMARK 280 RESERVOIR WHICH WAS 20% PEG 335 BUFFERED WITH 0.10 M MES AT PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
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 0.00000
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 SMTRY1 5 1.000000 0.000000 0.000000 34.93250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.63400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 43.37050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.93250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.63400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 43.37050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.93250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.63400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.37050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.93250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.63400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 43.37050
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 69.86500
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 350 BIOMT1 3 -1.000000 0.000000 0.000000 69.86500
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 173.48200
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 173.48200
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 MET A -21
REMARK 465 ARG A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 LEU A -17
REMARK 465 VAL A -16
REMARK 465 LEU A -15
REMARK 465 PHE A -14
REMARK 465 PHE A -13
REMARK 465 VAL A -12
REMARK 465 SER A -11
REMARK 465 ALA A -10
REMARK 465 TRP A -9
REMARK 465 THR A -8
REMARK 465 ALA A -7
REMARK 465 LEU A -6
REMARK 465 ALA A -5
REMARK 465 SER A -4
REMARK 465 PRO A -3
REMARK 465 ILE A -2
REMARK 465 ARG A -1
REMARK 465 ARG A 0
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 HB2 ASN A 33 O HOH A 532 1.55
REMARK 500 HG SER A 83 O2 PLM A 302 1.59
REMARK 500 O HOH A 514 O HOH A 535 2.00
REMARK 500 OG SER A 146 O2 PLM A 302 2.03
REMARK 500 O ASP A 48 O HOH A 401 2.10
REMARK 500 ND2 ASN A 33 C2 NAG A 303 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 A 524 O HOH A 524 4557 0.76
REMARK 500 HG1 PLM A 302 O HOH A 573 4557 0.90
REMARK 500 O HOH A 564 O HOH A 564 3657 1.27
REMARK 500 CG PLM A 302 O HOH A 573 4557 1.43
REMARK 500 O HOH A 567 O HOH A 567 4557 1.86
REMARK 500 O HOH A 558 O HOH A 558 3657 2.17
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 ARG A 84 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 HIS A 215 CA - C - N ANGL. DEV. = -14.4 DEGREES
REMARK 500 HIS A 215 O - C - N ANGL. DEV. = 11.4 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 CYS A 41 59.45 -144.46
REMARK 500 LYS A 74 60.98 61.74
REMARK 500 ARG A 84 -46.37 -144.72
REMARK 500 SER A 146 -128.36 63.85
REMARK 500 THR A 199 -119.41 39.04
REMARK 500 PHE A 262 -37.78 72.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 209 0.12 SIDE CHAIN
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 570 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 571 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A 572 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A 573 DISTANCE = 7.38 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 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 27 OD2
REMARK 620 2 HOH A 408 O 58.3
REMARK 620 3 HOH A 554 O 151.1 99.7
REMARK 620 4 HOH A 423 O 76.8 88.2 84.6
REMARK 620 5 HOH A 541 O 91.5 85.8 106.4 168.3
REMARK 620 N 1 2 3 4
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 303 bound
REMARK 800 to ASN A 33
DBREF 6OR3 A -21 269 UNP O59952 LIP_THELA 1 291
SEQRES 1 A 291 MET ARG SER SER LEU VAL LEU PHE PHE VAL SER ALA TRP
SEQRES 2 A 291 THR ALA LEU ALA SER PRO ILE ARG ARG GLU VAL SER GLN
SEQRES 3 A 291 ASP LEU PHE ASN GLN PHE ASN LEU PHE ALA GLN TYR SER
SEQRES 4 A 291 ALA ALA ALA TYR CYS GLY LYS ASN ASN ASP ALA PRO ALA
SEQRES 5 A 291 GLY THR ASN ILE THR CYS THR GLY ASN ALA CYS PRO GLU
SEQRES 6 A 291 VAL GLU LYS ALA ASP ALA THR PHE LEU TYR SER PHE GLU
SEQRES 7 A 291 ASP SER GLY VAL GLY ASP VAL THR GLY PHE LEU ALA LEU
SEQRES 8 A 291 ASP ASN THR ASN LYS LEU ILE VAL LEU SER PHE ARG GLY
SEQRES 9 A 291 SER ARG SER ILE GLU ASN TRP ILE GLY ASN LEU ASN PHE
SEQRES 10 A 291 ASP LEU LYS GLU ILE ASN ASP ILE CYS SER GLY CYS ARG
SEQRES 11 A 291 GLY HIS ASP GLY PHE THR SER SER TRP ARG SER VAL ALA
SEQRES 12 A 291 ASP THR LEU ARG GLN LYS VAL GLU ASP ALA VAL ARG GLU
SEQRES 13 A 291 HIS PRO ASP TYR ARG VAL VAL PHE THR GLY HIS SER LEU
SEQRES 14 A 291 GLY GLY ALA LEU ALA THR VAL ALA GLY ALA ASP LEU ARG
SEQRES 15 A 291 GLY ASN GLY TYR ASP ILE ASP VAL PHE SER TYR GLY ALA
SEQRES 16 A 291 PRO ARG VAL GLY ASN ARG ALA PHE ALA GLU PHE LEU THR
SEQRES 17 A 291 VAL GLN THR GLY GLY THR LEU TYR ARG ILE THR HIS THR
SEQRES 18 A 291 ASN ASP ILE VAL PRO ARG LEU PRO PRO ARG GLU PHE GLY
SEQRES 19 A 291 TYR SER HIS SER SER PRO GLU TYR TRP ILE LYS SER GLY
SEQRES 20 A 291 THR LEU VAL PRO VAL THR ARG ASN ASP ILE VAL LYS ILE
SEQRES 21 A 291 GLU GLY ILE ASP ALA THR GLY GLY ASN ASN GLN PRO ASN
SEQRES 22 A 291 ILE PRO ASP ILE PRO ALA HIS LEU TRP TYR PHE GLY LEU
SEQRES 23 A 291 ILE GLY THR CYS LEU
HET CA A 301 1
HET PLM A 302 48
HET NAG A 303 27
HETNAM CA CALCIUM ION
HETNAM PLM PALMITIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 CA CA 2+
FORMUL 3 PLM C16 H32 O2
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 HOH *173(H2 O)
HELIX 1 AA1 SER A 3 ALA A 20 1 18
HELIX 2 AA2 TYR A 21 ASN A 26 5 6
HELIX 3 AA3 CYS A 41 ALA A 47 1 7
HELIX 4 AA4 SER A 85 ASN A 94 1 10
HELIX 5 AA5 ASP A 111 HIS A 135 1 25
HELIX 6 AA6 SER A 146 ARG A 160 1 15
HELIX 7 AA7 ASN A 178 GLN A 188 1 11
HELIX 8 AA8 ILE A 202 LEU A 206 5 5
HELIX 9 AA9 PRO A 208 GLY A 212 5 5
HELIX 10 AB1 THR A 231 ASN A 233 5 3
HELIX 11 AB2 ILE A 255 TRP A 260 5 6
SHEET 1 AA1 8 ALA A 49 SER A 58 0
SHEET 2 AA1 8 VAL A 63 ASP A 70 -1 O LEU A 67 N TYR A 53
SHEET 3 AA1 8 LEU A 75 PHE A 80 -1 O SER A 79 N PHE A 66
SHEET 4 AA1 8 ARG A 139 HIS A 145 1 O VAL A 141 N LEU A 78
SHEET 5 AA1 8 ILE A 166 TYR A 171 1 O ASP A 167 N PHE A 142
SHEET 6 AA1 8 LEU A 193 HIS A 198 1 O TYR A 194 N VAL A 168
SHEET 7 AA1 8 GLU A 219 ILE A 222 1 O ILE A 222 N THR A 197
SHEET 8 AA1 8 ILE A 235 ILE A 238 -1 O ILE A 238 N GLU A 219
SHEET 1 AA2 2 LEU A 97 GLU A 99 0
SHEET 2 AA2 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SSBOND 1 CYS A 22 CYS A 268 1555 1555 2.07
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.05
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.08
LINK OD2 ASP A 27 CA CA A 301 1555 1555 2.81
LINK ND2 ASN A 33 C1 NAG A 303 1555 1555 1.44
LINK OG SER A 146 C1 PLM A 302 1555 1555 1.30
LINK CA CA A 301 O HOH A 408 1555 1555 2.46
LINK CA CA A 301 O HOH A 554 1555 1555 2.37
LINK CA CA A 301 O HOH A 423 1555 1555 2.04
LINK CA CA A 301 O HOH A 541 1555 1555 1.91
CISPEP 1 LEU A 206 PRO A 207 0 -14.56
CISPEP 2 SER A 217 PRO A 218 0 0.87
SITE 1 AC1 5 ASP A 27 HOH A 408 HOH A 423 HOH A 541
SITE 2 AC1 5 HOH A 554
SITE 1 AC2 8 SER A 83 TRP A 89 ASN A 92 SER A 146
SITE 2 AC2 8 LEU A 147 PHE A 211 HOH A 440 HOH A 573
SITE 1 AC3 3 ASN A 33 GLU A 45 LYS A 46
CRYST1 69.865 85.268 86.741 90.00 90.00 90.00 I 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014313 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011529 0.00000
TER 4152 LEU A 269
MASTER 445 0 3 11 10 0 5 6 2276 1 90 23
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