| 5ap9-pdb | HEADER HYDROLASE 15-SEP-15 5AP9
TITLE CONTROLLED LID-OPENING IN THERMOMYCES LANUGINOSUS LIPASE -
TITLE 2 A SWITCH FOR ACTIVITY AND BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 23-291;
COMPND 5 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;
SOURCE 3 ORGANISM_TAXID: 5541;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS HYDROLASE, THERMOMYCES LANUGINOSUS LIPASE, ENGINEERED DISULFIDE
KEYWDS 2 BRIDGE, CONTROLLED BINDING, DUAL SWITCH, CONTROLLED ACTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SKOLD-JORGENSEN,J.VIND,O.V.MOROZ,E.V.BLAGOVA,V.K.BHATIA,A.SVENDSEN,
AUTHOR 2 K.S.WILSON,M.J.BJERRUM
REVDAT 1 28-SEP-16 5AP9 0
JRNL AUTH J.SKOLD-JORGENSEN,J.VIND,O.V.MOROZ,E.V.BLAGOVA,V.K.BHATIA,
JRNL AUTH 2 A.SVENDSEN,K.S.WILSON,M.J.BJERRUM
JRNL TITL CONTROLLED LID-OPENING IN THERMOMYCES LANUGINOSUS LIPASE -
JRNL TITL 2 A SWITCH FOR ACTIVITY AND BINDING
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.84
REMARK 3 NUMBER OF REFLECTIONS : 59391
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) : 0.17272
REMARK 3 R VALUE (WORKING SET) : 0.17152
REMARK 3 FREE R VALUE : 0.19693
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 3061
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) : 1.799
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.846
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4288
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.231
REMARK 3 BIN FREE R VALUE SET COUNT : 220
REMARK 3 BIN FREE R VALUE : 0.251
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4152
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 243
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.267
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.40
REMARK 3 B22 (A**2) : 0.40
REMARK 3 B33 (A**2) : -0.80
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.098
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.243
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4263 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3799 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5828 ; 1.706 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8714 ; 1.497 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 548 ; 6.256 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 205 ;35.360 ;24.049
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 598 ;12.325 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.232 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 636 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5034 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1048 ; 0.007 ; 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): 2164 ; 1.125 ; 1.896
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2163 ; 1.125 ; 1.896
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2717 ; 1.769 ; 2.839
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2098 ; 1.650 ; 2.085
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 : B 1 B 269
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0091 -37.8392 8.3953
REMARK 3 T TENSOR
REMARK 3 T11: 0.1374 T22: 0.0878
REMARK 3 T33: 0.1045 T12: -0.0346
REMARK 3 T13: -0.0423 T23: 0.0753
REMARK 3 L TENSOR
REMARK 3 L11: 2.5193 L22: 1.3971
REMARK 3 L33: 4.3387 L12: -0.1819
REMARK 3 L13: 1.4203 L23: -1.1585
REMARK 3 S TENSOR
REMARK 3 S11: -0.2176 S12: 0.2751 S13: 0.3080
REMARK 3 S21: 0.0361 S22: -0.1011 S23: -0.1907
REMARK 3 S31: -0.3247 S32: 0.5050 S33: 0.3187
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 : A 2 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2111 -2.1499 -8.9800
REMARK 3 T TENSOR
REMARK 3 T11: 0.0967 T22: 0.0173
REMARK 3 T33: 0.0280 T12: 0.0163
REMARK 3 T13: -0.0347 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 2.8609 L22: 1.2943
REMARK 3 L33: 1.3782 L12: 0.9299
REMARK 3 L13: 0.2106 L23: 0.1454
REMARK 3 S TENSOR
REMARK 3 S11: 0.0748 S12: -0.0191 S13: -0.1350
REMARK 3 S21: 0.1165 S22: -0.0405 S23: -0.1390
REMARK 3 S31: 0.0015 S32: -0.0269 S33: -0.0343
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
REMARK 3 RIDING POSITIONS.
REMARK 3 SUBUNIT A IS BETTER ORDERED, THAN SUBUNIT B. DESCRIPTION
REMARK 3 IN THE PAPER WILL REFER TO SUBUNIT A
REMARK 4
REMARK 4 5AP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-SEP-15.
REMARK 100 THE PDBE ID CODE IS EBI-65054.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
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 : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59391
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 50.02
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.1
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 12.8
REMARK 200 R MERGE FOR SHELL (I) : 0.87
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.00
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: PDB ENTRY 1DT3
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 % PEG400, 0.2 M LITHIUM
REMARK 280 SULFATE, 0.1 M NA-ACETATE PH 4.5, SITTING DROP, VAPOUR
REMARK 280 DIFFUSION
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 80.22750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 45.23900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.23900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 120.34125
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.23900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 45.23900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.11375
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.23900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.23900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 120.34125
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 45.23900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.23900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.11375
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 80.22750
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2047 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY B 23
REMARK 465 LYS B 24
REMARK 465 ASN B 25
REMARK 465 ASN B 26
REMARK 465 ASP B 27
REMARK 465 ALA B 28
REMARK 465 PRO B 29
REMARK 465 ALA B 30
REMARK 465 GLY B 31
REMARK 465 THR B 32
REMARK 465 ASN B 33
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 74 CE NZ
REMARK 480 ARG A 84 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 98 CD CE NZ
REMARK 480 ARG A 118 CD NE CZ NH1 NH2
REMARK 480 LYS A 223 CE NZ
REMARK 480 LEU A 269 CG CD1 CD2
REMARK 480 LYS B 46 CD CE NZ
REMARK 480 ASN B 71 CG OD1 ND2
REMARK 480 LYS B 74 CG CD CE NZ
REMARK 480 ARG B 84 CG CD NE CZ NH1 NH2
REMARK 480 ASN B 94 CG OD1 ND2
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 CG2A THR A 114 NH2 ARG A 118 2.03
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 LYS A 98 CG LYS A 98 CD -0.286
REMARK 500 ARG A 118 CG ARG A 118 CD 0.165
REMARK 500 LYS A 223 CD LYS A 223 CE -0.181
REMARK 500 LYS B 74 CB LYS B 74 CG -0.236
REMARK 500 ARG B 84 CB ARG B 84 CG 0.311
REMARK 500 ASN B 94 CB A ASN B 94 CG A -0.401
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 LYS A 74 CG - CD - CE ANGL. DEV. = 18.6 DEGREES
REMARK 500 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 LYS A 98 CB - CG - CD ANGL. DEV. = 28.5 DEGREES
REMARK 500 ASP A 167 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 209 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LYS B 74 CA - CB - CG ANGL. DEV. = 22.5 DEGREES
REMARK 500 CYS B 86 N - CA - CB ANGL. DEV. = -15.0 DEGREES
REMARK 500 ASN B 94 CA - CB - CG ANGL. DEV. = 26.4 DEGREES
REMARK 500 ASN B 94 CB - CG - OD1 ANGL. DEV. = -15.2 DEGREES
REMARK 500 ASP B 167 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 175 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 179 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG B 179 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG B 209 NE - CZ - NH2 ANGL. DEV. = -3.1 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 54.43 -148.66
REMARK 500 SER A 146 -131.39 60.04
REMARK 500 THR A 199 -114.85 34.62
REMARK 500 PHE A 262 -46.33 75.92
REMARK 500 CYS B 41 54.27 -150.20
REMARK 500 ASN B 94 37.26 -97.99
REMARK 500 SER B 146 -133.26 60.14
REMARK 500 THR B 199 -118.77 35.23
REMARK 500 PHE B 262 -47.27 77.21
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 GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 300 BOUND TO ASN A 33
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 MUTATIONS I86C, I255C
DBREF 5AP9 A 1 269 UNP O59952 LIP_THELA 23 291
DBREF 5AP9 B 1 269 UNP O59952 LIP_THELA 23 291
SEQADV 5AP9 CYS A 86 UNP O59952 ILE 108 ENGINEERED MUTATION
SEQADV 5AP9 CYS A 255 UNP O59952 ILE 277 ENGINEERED MUTATION
SEQADV 5AP9 CYS B 86 UNP O59952 ILE 108 ENGINEERED MUTATION
SEQADV 5AP9 CYS B 255 UNP O59952 ILE 277 ENGINEERED MUTATION
SEQRES 1 A 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 A 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 A 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 A 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 A 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 A 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 A 269 SER PHE ARG GLY SER ARG SER CYS GLU ASN TRP ILE GLY
SEQRES 8 A 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 A 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 A 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 A 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 A 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 A 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 A 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 A 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 A 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 A 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 A 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 A 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 A 269 ASN GLN PRO ASN ILE PRO ASP CYS PRO ALA HIS LEU TRP
SEQRES 21 A 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 B 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 B 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 B 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 B 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 B 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 B 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 B 269 SER PHE ARG GLY SER ARG SER CYS GLU ASN TRP ILE GLY
SEQRES 8 B 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 B 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 B 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 B 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 B 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 B 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 B 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 B 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 B 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 B 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 B 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 B 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 B 269 ASN GLN PRO ASN ILE PRO ASP CYS PRO ALA HIS LEU TRP
SEQRES 21 B 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
HET NAG A 300 14
HET GOL A 401 6
HET PEG A 601 7
HET GOL B 401 6
HET SO4 B 501 5
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN GOL GLYCERIN
FORMUL 2 SO4 O4 S 2-
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 PEG C4 H10 O3
FORMUL 5 NAG C8 H15 N O6
FORMUL 6 HOH *243(H2 O)
HELIX 1 1 SER A 3 ALA A 20 1 18
HELIX 2 2 TYR A 21 ASN A 26 5 6
HELIX 3 3 CYS A 41 LYS A 46 1 6
HELIX 4 4 ASN A 88 LEU A 93 1 6
HELIX 5 5 ASP A 111 HIS A 135 1 25
HELIX 6 6 SER A 146 ARG A 160 1 15
HELIX 7 7 ASN A 178 GLN A 188 1 11
HELIX 8 8 ILE A 202 LEU A 206 5 5
HELIX 9 9 PRO A 208 GLY A 212 5 5
HELIX 10 10 THR A 231 ASN A 233 5 3
HELIX 11 11 CYS A 255 LEU A 259 5 5
HELIX 12 12 SER B 3 ALA B 20 1 18
HELIX 13 13 CYS B 36 ALA B 40 5 5
HELIX 14 14 CYS B 41 LYS B 46 1 6
HELIX 15 15 GLU B 87 ASN B 92 1 6
HELIX 16 16 ASP B 111 HIS B 135 1 25
HELIX 17 17 SER B 146 ARG B 160 1 15
HELIX 18 18 ASN B 178 GLN B 188 1 11
HELIX 19 19 ILE B 202 LEU B 206 5 5
HELIX 20 20 PRO B 208 GLY B 212 5 5
HELIX 21 21 THR B 231 ASN B 233 5 3
HELIX 22 22 CYS B 255 LEU B 259 5 5
SHEET 1 AA 8 ALA A 49 SER A 58 0
SHEET 2 AA 8 VAL A 63 ASP A 70 -1 O VAL A 63 N SER A 58
SHEET 3 AA 8 LEU A 75 PHE A 80 -1 O LEU A 75 N ASP A 70
SHEET 4 AA 8 ARG A 139 HIS A 145 1 O ARG A 139 N ILE A 76
SHEET 5 AA 8 ILE A 166 TYR A 171 1 O ASP A 167 N PHE A 142
SHEET 6 AA 8 LEU A 193 HIS A 198 1 O TYR A 194 N SER A 170
SHEET 7 AA 8 GLU A 219 ILE A 222 1 O TYR A 220 N THR A 197
SHEET 8 AA 8 ILE A 235 ILE A 238 -1 O VAL A 236 N TRP A 221
SHEET 1 AB 2 LEU A 97 GLU A 99 0
SHEET 2 AB 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SHEET 1 BA 8 ALA B 49 SER B 58 0
SHEET 2 BA 8 VAL B 63 ASP B 70 -1 O VAL B 63 N SER B 58
SHEET 3 BA 8 LEU B 75 PHE B 80 -1 O LEU B 75 N ASP B 70
SHEET 4 BA 8 ARG B 139 HIS B 145 1 O ARG B 139 N ILE B 76
SHEET 5 BA 8 ILE B 166 TYR B 171 1 O ASP B 167 N PHE B 142
SHEET 6 BA 8 LEU B 193 HIS B 198 1 O TYR B 194 N SER B 170
SHEET 7 BA 8 GLU B 219 ILE B 222 1 O TYR B 220 N THR B 197
SHEET 8 BA 8 ILE B 235 ILE B 238 -1 O VAL B 236 N TRP B 221
SHEET 1 BB 2 LEU B 97 GLU B 99 0
SHEET 2 BB 2 ARG B 108 HIS B 110 -1 O GLY B 109 N LYS B 98
SSBOND 1 CYS A 22 CYS A 268 1555 1555 2.06
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.05
SSBOND 3 CYS A 86 CYS A 255 1555 1555 2.03
SSBOND 4 CYS A 104 CYS A 107 1555 1555 2.09
SSBOND 5 CYS B 22 CYS B 268 1555 1555 2.03
SSBOND 6 CYS B 36 CYS B 41 1555 1555 2.06
SSBOND 7 CYS B 86 CYS B 255 1555 1555 2.01
SSBOND 8 CYS B 104 CYS B 107 1555 1555 2.10
LINK ND2 ASN A 33 C1 NAG A 300 1555 1555 1.44
CISPEP 1 LEU A 206 PRO A 207 0 -21.95
CISPEP 2 SER A 217 PRO A 218 0 -1.09
CISPEP 3 LEU B 206 PRO B 207 0 -18.60
CISPEP 4 SER B 217 PRO B 218 0 4.34
SITE 1 AC1 9 ARG A 160 LEU A 185 THR A 186 GLN A 188
SITE 2 AC1 9 GLY A 191 THR A 192 LEU A 193 HOH A2102
SITE 3 AC1 9 HOH A2149
SITE 1 AC2 5 ASP A 27 ALA A 28 SER A 54 GLN A 126
SITE 2 AC2 5 LYS A 127
SITE 1 AC3 8 ARG B 160 LEU B 185 THR B 186 GLN B 188
SITE 2 AC3 8 GLY B 191 THR B 192 LEU B 193 HOH B2094
SITE 1 AC4 7 PRO A 208 ARG A 209 GLU A 210 GLU B 210
SITE 2 AC4 7 HOH B2062 HOH B2066 HOH B2087
SITE 1 AC5 11 ASN A 33 HOH A2023 HOH A2037 HOH A2148
SITE 2 AC5 11 ARG B 118 ASP B 122 ARG B 125 ASP B 158
SITE 3 AC5 11 HOH B2024 HOH B2034 HOH B2038
CRYST1 90.478 90.478 160.455 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 0.011052 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011052 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006232 0.00000
TER 2108 LEU A 269
TER 4154 LEU B 269
MASTER 454 0 5 22 20 0 12 6 4433 2 59 42
END
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