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HEADER HYDROLASE 14-FEB-19 6QPP
TITLE RHIZOMUCOR MIEHEI LIPASE PROPEPTIDE COMPLEX, NATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOMUCOR MIEHEI;
SOURCE 3 ORGANISM_TAXID: 4839;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS LIPASE, PROPEPTIDE, INTRAMOLECULAR CHAPERONE, INHIBITION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.V.MOROZ,E.BLAGOVA,V.REISER,R.SAIKIA,S.DALAL,C.I.JORGENSEN,
AUTHOR 2 L.BAUNSGAARD,B.ANDERSEN,A.SVENDSEN,K.S.WILSON
REVDAT 1 13-MAR-19 6QPP 0
JRNL AUTH O.V.MOROZ,E.BLAGOVA,V.REISER,R.SAIKIA,S.DALAL,C.I.JORGENSEN,
JRNL AUTH 2 L.BAUNSGAARD,B.ANDERSEN,A.SVENDSEN,K.S.WILSON
JRNL TITL NOVEL INHIBITORY FUNCTION OF THE RHIZOMUCOR MIEHEI LIPASE
JRNL TITL 2 PROPEPTIDE AND 3D STRUCTURES OF ITS COMPLEXES WITH THE
JRNL TITL 3 ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 52758
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2735
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3896
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.1560
REMARK 3 BIN FREE R VALUE SET COUNT : 203
REMARK 3 BIN FREE R VALUE : 0.2270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2384
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.91000
REMARK 3 B22 (A**2) : -0.91000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.227
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2465 ; 0.017 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 2138 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3376 ; 1.850 ; 1.672
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5011 ; 1.184 ; 1.638
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 308 ; 6.824 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;30.217 ;22.478
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 360 ;10.763 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;16.692 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 343 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2760 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 454 ; 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): 1241 ; 2.268 ; 1.214
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1240 ; 2.224 ; 1.213
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1546 ; 2.765 ; 1.830
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1547 ; 2.770 ; 1.831
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1224 ; 3.100 ; 1.477
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1224 ; 3.099 ; 1.477
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1831 ; 3.762 ; 2.128
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2721 ; 3.595 ;15.212
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2710 ; 3.582 ;15.143
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4603 ; 4.044 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 111 ;20.975 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4585 ;11.257 ; 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 : 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
REMARK 4
REMARK 4 6QPP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1292100620.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55513
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 50.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.800
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: 3TGL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8K, SODIUM CACODYLATE, AMMONIUM
REMARK 280 SULPHATE, PH 6.5, VAPOR DIFFUSION, SITTING 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 X+1/2,Y+1/2,Z
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 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 49.02000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.51000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.02000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.51000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 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 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 1
REMARK 465 VAL A 2
REMARK 465 LEU A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 ARG A 6
REMARK 465 ALA A 7
REMARK 465 ASN A 8
REMARK 465 TYR A 9
REMARK 465 LEU A 10
REMARK 465 GLY A 11
REMARK 465 PHE A 12
REMARK 465 LEU A 13
REMARK 465 ILE A 14
REMARK 465 VAL A 15
REMARK 465 PHE A 16
REMARK 465 PHE A 17
REMARK 465 THR A 18
REMARK 465 ALA A 19
REMARK 465 PHE A 20
REMARK 465 LEU A 21
REMARK 465 VAL A 22
REMARK 465 GLU A 23
REMARK 465 ALA A 24
REMARK 465 VAL A 25
REMARK 465 PRO A 26
REMARK 465 ILE A 27
REMARK 465 LYS A 28
REMARK 465 ARG A 29
REMARK 465 GLN A 30
REMARK 465 SER A 31
REMARK 465 ASN A 32
REMARK 465 SER A 33
REMARK 465 THR A 34
REMARK 465 VAL A 35
REMARK 465 ASP A 36
REMARK 465 SER A 50
REMARK 465 SER A 51
REMARK 465 SER A 52
REMARK 465 PRO A 53
REMARK 465 SER A 54
REMARK 465 ASP A 88
REMARK 465 SER A 89
REMARK 465 VAL A 90
REMARK 465 VAL A 91
REMARK 465 GLN A 92
REMARK 465 ALA A 93
REMARK 465 MET A 94
REMARK 465 SER A 95
REMARK 465 ILE A 96
REMARK 465 ASP A 97
REMARK 465 GLY A 98
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 ILE A 135 CD1
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 GLU A 256 CD OE1 OE2
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 747 O HOH A 747 2555 1.65
REMARK 500 NH2 ARG A 180 O HOH A 747 2555 2.00
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 99 N GLY A 99 CA 0.145
REMARK 500 SER A 353 CB SER A 353 OG -0.086
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 290 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 296 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 296 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 CYS A 329 CB - CA - C ANGL. DEV. = 7.6 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 ASN A 82 33.38 -147.94
REMARK 500 SER A 238 -131.13 66.43
REMARK 500 ASN A 262 14.95 -145.23
REMARK 500 GLU A 295 -124.87 50.34
REMARK 500 CYS A 338 -124.21 -109.18
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 124 0.11 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 756 DISTANCE = 6.05 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 82
DBREF 6QPP A 1 363 UNP P19515 LIP_RHIMI 1 363
SEQRES 1 A 363 MET VAL LEU LYS GLN ARG ALA ASN TYR LEU GLY PHE LEU
SEQRES 2 A 363 ILE VAL PHE PHE THR ALA PHE LEU VAL GLU ALA VAL PRO
SEQRES 3 A 363 ILE LYS ARG GLN SER ASN SER THR VAL ASP SER LEU PRO
SEQRES 4 A 363 PRO LEU ILE PRO SER ARG THR SER ALA PRO SER SER SER
SEQRES 5 A 363 PRO SER THR THR ASP PRO GLU ALA PRO ALA MET SER ARG
SEQRES 6 A 363 ASN GLY PRO LEU PRO SER ASP VAL GLU THR LYS TYR GLY
SEQRES 7 A 363 MET ALA LEU ASN ALA THR SER TYR PRO ASP SER VAL VAL
SEQRES 8 A 363 GLN ALA MET SER ILE ASP GLY GLY ILE ARG ALA ALA THR
SEQRES 9 A 363 SER GLN GLU ILE ASN GLU LEU THR TYR TYR THR THR LEU
SEQRES 10 A 363 SER ALA ASN SER TYR CYS ARG THR VAL ILE PRO GLY ALA
SEQRES 11 A 363 THR TRP ASP CYS ILE HIS CYS ASP ALA THR GLU ASP LEU
SEQRES 12 A 363 LYS ILE ILE LYS THR TRP SER THR LEU ILE TYR ASP THR
SEQRES 13 A 363 ASN ALA MET VAL ALA ARG GLY ASP SER GLU LYS THR ILE
SEQRES 14 A 363 TYR ILE VAL PHE ARG GLY SER SER SER ILE ARG ASN TRP
SEQRES 15 A 363 ILE ALA ASP LEU THR PHE VAL PRO VAL SER TYR PRO PRO
SEQRES 16 A 363 VAL SER GLY THR LYS VAL HIS LYS GLY PHE LEU ASP SER
SEQRES 17 A 363 TYR GLY GLU VAL GLN ASN GLU LEU VAL ALA THR VAL LEU
SEQRES 18 A 363 ASP GLN PHE LYS GLN TYR PRO SER TYR LYS VAL ALA VAL
SEQRES 19 A 363 THR GLY HIS SER LEU GLY GLY ALA THR ALA LEU LEU CYS
SEQRES 20 A 363 ALA LEU ASP LEU TYR GLN ARG GLU GLU GLY LEU SER SER
SEQRES 21 A 363 SER ASN LEU PHE LEU TYR THR GLN GLY GLN PRO ARG VAL
SEQRES 22 A 363 GLY ASP PRO ALA PHE ALA ASN TYR VAL VAL SER THR GLY
SEQRES 23 A 363 ILE PRO TYR ARG ARG THR VAL ASN GLU ARG ASP ILE VAL
SEQRES 24 A 363 PRO HIS LEU PRO PRO ALA ALA PHE GLY PHE LEU HIS ALA
SEQRES 25 A 363 GLY GLU GLU TYR TRP ILE THR ASP ASN SER PRO GLU THR
SEQRES 26 A 363 VAL GLN VAL CYS THR SER ASP LEU GLU THR SER ASP CYS
SEQRES 27 A 363 SER ASN SER ILE VAL PRO PHE THR SER VAL LEU ASP HIS
SEQRES 28 A 363 LEU SER TYR PHE GLY ILE ASN THR GLY LEU CYS THR
HET NAG A 501 14
HET EDO A 502 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *156(H2 O)
HELIX 1 AA1 ILE A 42 THR A 46 5 5
HELIX 2 AA2 GLU A 59 ASN A 66 1 8
HELIX 3 AA3 THR A 104 SER A 121 1 18
HELIX 4 AA4 HIS A 136 GLU A 141 5 6
HELIX 5 AA5 SER A 178 LEU A 186 1 9
HELIX 6 AA6 LYS A 203 TYR A 227 1 25
HELIX 7 AA7 SER A 238 GLU A 255 1 18
HELIX 8 AA8 ASP A 275 THR A 285 1 11
HELIX 9 AA9 ILE A 298 LEU A 302 5 5
HELIX 10 AB1 PRO A 304 GLY A 308 5 5
HELIX 11 AB2 CYS A 338 VAL A 343 5 6
HELIX 12 AB3 VAL A 348 HIS A 351 5 4
SHEET 1 AA1 2 THR A 75 LYS A 76 0
SHEET 2 AA1 2 MET A 79 ALA A 80 -1 O MET A 79 N LYS A 76
SHEET 1 AA2 9 ILE A 100 ALA A 102 0
SHEET 2 AA2 9 THR A 325 CYS A 329 -1 O VAL A 328 N ARG A 101
SHEET 3 AA2 9 GLU A 314 ASP A 320 -1 N TRP A 317 O GLN A 327
SHEET 4 AA2 9 TYR A 289 ASN A 294 1 N VAL A 293 O ILE A 318
SHEET 5 AA2 9 LEU A 263 GLN A 268 1 N THR A 267 O THR A 292
SHEET 6 AA2 9 LYS A 231 HIS A 237 1 N VAL A 234 O TYR A 266
SHEET 7 AA2 9 THR A 168 PHE A 173 1 N ILE A 169 O LYS A 231
SHEET 8 AA2 9 ASN A 157 GLY A 163 -1 N GLY A 163 O THR A 168
SHEET 9 AA2 9 LYS A 144 SER A 150 -1 N LYS A 144 O ARG A 162
SHEET 1 AA3 2 PRO A 190 SER A 192 0
SHEET 2 AA3 2 LYS A 200 HIS A 202 -1 O VAL A 201 N VAL A 191
SHEET 1 AA4 2 SER A 353 TYR A 354 0
SHEET 2 AA4 2 ILE A 357 ASN A 358 -1 O ILE A 357 N TYR A 354
SSBOND 1 CYS A 123 CYS A 362 1555 1555 2.06
SSBOND 2 CYS A 134 CYS A 137 1555 1555 2.13
SSBOND 3 CYS A 329 CYS A 338 1555 1555 2.06
LINK ND2 ASN A 82 C1 NAG A 501 1555 1555 1.42
CISPEP 1 ILE A 127 PRO A 128 0 15.08
CISPEP 2 LEU A 302 PRO A 303 0 -21.02
CISPEP 3 SER A 322 PRO A 323 0 -5.10
CISPEP 4 VAL A 343 PRO A 344 0 2.37
SITE 1 AC1 6 SER A 44 ARG A 45 THR A 46 SER A 47
SITE 2 AC1 6 TYR A 252 SER A 284
SITE 1 AC2 4 ASP A 72 ASN A 82 ARG A 124 HOH A 645
CRYST1 98.040 61.020 62.650 90.00 111.97 90.00 C 1 2 1 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 0.010200 0.000000 0.004115 0.00000
SCALE2 0.000000 0.016388 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017212 0.00000
TER 2385 THR A 363
MASTER 429 0 2 12 15 0 3 6 2558 1 25 28
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