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HEADER HYDROLASE 14-FEB-19 6QPR
TITLE RHIZOMUCOR MIEHEI LIPASE PROPEPTIDE COMPLEX, SER95/ILE96 DELETION
TITLE 2 MUTANT
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, DELETION
KEYWDS 2 MUTANT, FUNGAL, 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 6QPR 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. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 55606
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) : 0.128
REMARK 3 R VALUE (WORKING SET) : 0.126
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2945
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) : 3007
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2428
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 256
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.34000
REMARK 3 B22 (A**2) : -0.18000
REMARK 3 B33 (A**2) : 0.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.78000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.056
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.055
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.160
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): 2538 ; 0.017 ; 0.015
REMARK 3 BOND LENGTHS OTHERS (A): 2185 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3481 ; 1.985 ; 1.783
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5135 ; 0.664 ; 1.739
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 324 ; 7.027 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 99 ;34.287 ;21.818
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 342 ;11.035 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;18.019 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 352 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2866 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 468 ; 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): 1290 ; 3.135 ; 1.463
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1291 ; 3.134 ; 1.463
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1616 ; 3.768 ; 2.210
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1617 ; 3.767 ; 2.210
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1248 ; 4.199 ; 1.761
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1249 ; 4.197 ; 1.761
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1866 ; 4.633 ; 2.523
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2787 ; 4.663 ;18.745
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2749 ; 4.585 ;18.468
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4723 ; 4.667 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 181 ;25.070 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4728 ;18.208 ; 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 6QPR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1292100624.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55606
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 30.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.8000
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 (%) : 67.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
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: MOLREP
REMARK 200 STARTING MODEL: 6QPP
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: 4M NA FORMATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING 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 49.34800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.68700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.34800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.68700
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: 320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 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 91
REMARK 465 VAL A 92
REMARK 465 VAL A 93
REMARK 465 GLN A 94
REMARK 465 ALA A 95
REMARK 465 MET A 96
REMARK 465 ASP A 97
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 SER A 51 CB OG
REMARK 470 ARG A 124 CZ NH1 NH2
REMARK 470 LYS A 231 CE NZ
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 CB CYS A 329 O HOH A 686 2.09
REMARK 500 CG2 THR A 55 O HOH A 780 2.13
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 657 O HOH A 749 4555 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 ASP A 138 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 272 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 350 CB - CG - OD2 ANGL. DEV. = -5.5 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 34.80 -144.16
REMARK 500 TRP A 132 59.99 -97.91
REMARK 500 TRP A 132 54.91 -97.91
REMARK 500 ASP A 133 64.10 -108.09
REMARK 500 SER A 238 -133.23 64.41
REMARK 500 SER A 259 -169.69 -160.47
REMARK 500 ASN A 262 15.92 -141.22
REMARK 500 GLU A 295 -120.36 48.39
REMARK 500 CYS A 338 -124.66 -112.15
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 180 0.10 SIDE CHAIN
REMARK 500 TYR A 354 0.07 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 856 DISTANCE = 5.85 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
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 6QPR A 1 363 UNP P19515 LIP_RHIMI 1 363
SEQADV 6QPR A UNP P19515 SER 95 DELETION
SEQADV 6QPR A UNP P19515 ILE 96 DELETION
SEQRES 1 A 361 MET VAL LEU LYS GLN ARG ALA ASN TYR LEU GLY PHE LEU
SEQRES 2 A 361 ILE VAL PHE PHE THR ALA PHE LEU VAL GLU ALA VAL PRO
SEQRES 3 A 361 ILE LYS ARG GLN SER ASN SER THR VAL ASP SER LEU PRO
SEQRES 4 A 361 PRO LEU ILE PRO SER ARG THR SER ALA PRO SER SER SER
SEQRES 5 A 361 PRO SER THR THR ASP PRO GLU ALA PRO ALA MET SER ARG
SEQRES 6 A 361 ASN GLY PRO LEU PRO SER ASP VAL GLU THR LYS TYR GLY
SEQRES 7 A 361 MET ALA LEU ASN ALA THR SER TYR PRO ASP SER VAL VAL
SEQRES 8 A 361 GLN ALA MET ASP GLY GLY ILE ARG ALA ALA THR SER GLN
SEQRES 9 A 361 GLU ILE ASN GLU LEU THR TYR TYR THR THR LEU SER ALA
SEQRES 10 A 361 ASN SER TYR CYS ARG THR VAL ILE PRO GLY ALA THR TRP
SEQRES 11 A 361 ASP CYS ILE HIS CYS ASP ALA THR GLU ASP LEU LYS ILE
SEQRES 12 A 361 ILE LYS THR TRP SER THR LEU ILE TYR ASP THR ASN ALA
SEQRES 13 A 361 MET VAL ALA ARG GLY ASP SER GLU LYS THR ILE TYR ILE
SEQRES 14 A 361 VAL PHE ARG GLY SER SER SER ILE ARG ASN TRP ILE ALA
SEQRES 15 A 361 ASP LEU THR PHE VAL PRO VAL SER TYR PRO PRO VAL SER
SEQRES 16 A 361 GLY THR LYS VAL HIS LYS GLY PHE LEU ASP SER TYR GLY
SEQRES 17 A 361 GLU VAL GLN ASN GLU LEU VAL ALA THR VAL LEU ASP GLN
SEQRES 18 A 361 PHE LYS GLN TYR PRO SER TYR LYS VAL ALA VAL THR GLY
SEQRES 19 A 361 HIS SER LEU GLY GLY ALA THR ALA LEU LEU CYS ALA LEU
SEQRES 20 A 361 ASP LEU TYR GLN ARG GLU GLU GLY LEU SER SER SER ASN
SEQRES 21 A 361 LEU PHE LEU TYR THR GLN GLY GLN PRO ARG VAL GLY ASP
SEQRES 22 A 361 PRO ALA PHE ALA ASN TYR VAL VAL SER THR GLY ILE PRO
SEQRES 23 A 361 TYR ARG ARG THR VAL ASN GLU ARG ASP ILE VAL PRO HIS
SEQRES 24 A 361 LEU PRO PRO ALA ALA PHE GLY PHE LEU HIS ALA GLY GLU
SEQRES 25 A 361 GLU TYR TRP ILE THR ASP ASN SER PRO GLU THR VAL GLN
SEQRES 26 A 361 VAL CYS THR SER ASP LEU GLU THR SER ASP CYS SER ASN
SEQRES 27 A 361 SER ILE VAL PRO PHE THR SER VAL LEU ASP HIS LEU SER
SEQRES 28 A 361 TYR PHE GLY ILE ASN THR GLY LEU CYS THR
HET NAG A 501 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 HOH *256(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 ILE A 342 5 5
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 ARG A 291 O GLU A 314
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 2.04
SSBOND 2 CYS A 134 CYS A 137 1555 1555 2.01
SSBOND 3 CYS A 329 CYS A 338 1555 1555 2.09
LINK ND2 ASN A 82 C1 NAG A 501 1555 1555 1.44
CISPEP 1 GLY A 67 PRO A 68 0 -16.56
CISPEP 2 ILE A 127 PRO A 128 0 9.02
CISPEP 3 LEU A 302 PRO A 303 0 -21.33
CISPEP 4 SER A 322 PRO A 323 0 -4.08
CISPEP 5 VAL A 343 PRO A 344 0 1.06
SITE 1 AC1 4 ASP A 72 ASN A 82 ARG A 124 HOH A 676
CRYST1 98.696 61.374 62.814 90.00 111.85 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 0.010132 0.000000 0.004063 0.00000
SCALE2 0.000000 0.016294 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017152 0.00000
TER 2455 THR A 363
MASTER 413 0 1 12 15 0 1 6 2698 1 21 28
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