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HEADER HYDROLASE 04-MAY-13 4KJX
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF THREE PHASE PARTITION TREATED
TITLE 2 LIPASE FROM THERMOMYCES LANUGINOSA WITH LAURIC ACID AND P-
TITLE 3 NITROBENZALDEHYDE (PNB) AT 2.1 RESOLUTION
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
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;
SOURCE 3 ORGANISM_TAXID: 5541
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KUMAR,J.MUKHERJEE,M.N.GUPTA,M.SINHA,P.KAUR,S.SHARMA,T.P.SINGH
REVDAT 1 22-MAY-13 4KJX 0
JRNL AUTH M.KUMAR,J.MUKHERJEE,M.N.GUPTA,M.SINHA,P.KAUR,S.SHARMA,
JRNL AUTH 2 T.P.SINGH
JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX OF THREE PHASE PARTITION
JRNL TITL 2 TREATED LIPASE FROM THERMOMYCES LANUGINOSA WITH LAURIC ACID
JRNL TITL 3 AND P-NITROBENZALDEHYDE (PNB) AT 2.1 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 48888
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2634
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3320
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.3760
REMARK 3 BIN FREE R VALUE SET COUNT : 180
REMARK 3 BIN FREE R VALUE : 0.4420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 111
REMARK 3 SOLVENT ATOMS : 269
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 19.23000
REMARK 3 B22 (A**2) : 19.23000
REMARK 3 B33 (A**2) : -38.46000
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): 0.037
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.994
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4349 ; 0.021 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2904 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5903 ; 2.068 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7005 ; 1.108 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 536 ; 7.657 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;37.064 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 622 ;16.965 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;20.632 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 642 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4933 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 934 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 4KJX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079431.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48911
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08600
REMARK 200 FOR THE DATA SET : 35.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.44300
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 4EA6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, O.1M NACL, 1.6M AMMONIUM
REMARK 280 SULPHATE , PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.83067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.66133
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 40.24600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 67.07667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 13.41533
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 81 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 81 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 205 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ASP B 137 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG B 139 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 195 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 205 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG B 205 NE - CZ - NH2 ANGL. DEV. = -3.8 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 CYS A 22 -165.34 -109.34
REMARK 500 ASN A 25 33.99 179.14
REMARK 500 CYS A 41 54.46 -155.09
REMARK 500 LYS A 74 64.04 64.47
REMARK 500 ASP A 102 -25.52 -39.19
REMARK 500 SER A 146 -133.18 71.65
REMARK 500 THR A 199 -112.79 35.43
REMARK 500 PRO A 204 6.69 -63.46
REMARK 500 PHE A 262 -29.96 68.95
REMARK 500 ASN B 25 -164.76 -118.24
REMARK 500 ASN B 26 113.07 61.43
REMARK 500 ASP B 27 8.95 85.52
REMARK 500 CYS B 41 53.36 -147.44
REMARK 500 ASP B 62 67.01 33.15
REMARK 500 ASP B 102 -46.08 -26.26
REMARK 500 CYS B 104 131.33 -174.82
REMARK 500 SER B 146 -129.63 68.81
REMARK 500 ALA B 180 -46.15 87.10
REMARK 500 THR B 199 -114.40 39.43
REMARK 500 PRO B 204 0.04 -67.96
REMARK 500 PHE B 262 -31.61 70.28
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 NAG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XXH B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAO B 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EA6 RELATED DB: PDB
REMARK 900 MODEL PDB
DBREF 4KJX A 1 269 UNP O59952 LIP_THELA 23 291
DBREF 4KJX B 1 269 UNP O59952 LIP_THELA 23 291
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 ILE 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 ILE 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 ILE 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 ILE PRO ALA HIS LEU TRP
SEQRES 21 B 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
MODRES 4KJX ASN A 33 ASN GLYCOSYLATION SITE
MODRES 4KJX ASN B 33 ASN GLYCOSYLATION SITE
HET NAG A 301 14
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET ACT A 306 4
HET DAO A 307 14
HET NAG B 301 14
HET GOL B 302 6
HET EDO B 303 4
HET GOL B 304 6
HET XXH B 305 11
HET DAO B 306 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETNAM DAO LAURIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM XXH 4-NITROBENZALDEHYDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 GOL 6(C3 H8 O3)
FORMUL 8 ACT C2 H3 O2 1-
FORMUL 9 DAO 2(C12 H24 O2)
FORMUL 12 EDO C2 H6 O2
FORMUL 14 XXH C7 H5 N O3
FORMUL 16 HOH *269(H2 O)
HELIX 1 1 SER A 3 ALA A 20 1 18
HELIX 2 2 CYS A 41 ALA A 47 1 7
HELIX 3 3 SER A 85 ASN A 92 1 8
HELIX 4 4 ASP A 111 HIS A 135 1 25
HELIX 5 5 SER A 146 ARG A 160 1 15
HELIX 6 6 ASN A 178 GLN A 188 1 11
HELIX 7 7 ILE A 202 LEU A 206 5 5
HELIX 8 8 PRO A 208 GLY A 212 5 5
HELIX 9 9 THR A 231 ASN A 233 5 3
HELIX 10 10 ILE A 255 TRP A 260 5 6
HELIX 11 11 SER B 3 GLY B 23 1 21
HELIX 12 12 CYS B 41 LYS B 46 1 6
HELIX 13 13 SER B 85 ASN B 92 1 8
HELIX 14 14 ASP B 111 HIS B 135 1 25
HELIX 15 15 SER B 146 ARG B 160 1 15
HELIX 16 16 ALA B 180 GLN B 188 1 9
HELIX 17 17 ILE B 202 LEU B 206 5 5
HELIX 18 18 PRO B 208 GLY B 212 5 5
HELIX 19 19 THR B 231 ASN B 233 5 3
HELIX 20 20 ILE B 255 TRP B 260 5 6
SHEET 1 A 8 ALA A 49 SER A 58 0
SHEET 2 A 8 VAL A 63 ASP A 70 -1 O LEU A 67 N LEU A 52
SHEET 3 A 8 LEU A 75 PHE A 80 -1 O SER A 79 N PHE A 66
SHEET 4 A 8 ARG A 139 HIS A 145 1 O ARG A 139 N ILE A 76
SHEET 5 A 8 ASP A 167 TYR A 171 1 O ASP A 167 N PHE A 142
SHEET 6 A 8 LEU A 193 HIS A 198 1 O TYR A 194 N VAL A 168
SHEET 7 A 8 GLU A 219 ILE A 222 1 O ILE A 222 N THR A 197
SHEET 8 A 8 ILE A 235 ILE A 238 -1 O ILE A 238 N GLU A 219
SHEET 1 B 2 LEU A 97 GLU A 99 0
SHEET 2 B 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SHEET 1 C 8 ALA B 49 SER B 58 0
SHEET 2 C 8 VAL B 63 ASP B 70 -1 O LEU B 67 N LEU B 52
SHEET 3 C 8 LEU B 75 PHE B 80 -1 O VAL B 77 N ALA B 68
SHEET 4 C 8 ARG B 139 HIS B 145 1 O VAL B 141 N LEU B 78
SHEET 5 C 8 ASP B 167 TYR B 171 1 O ASP B 167 N PHE B 142
SHEET 6 C 8 LEU B 193 HIS B 198 1 O TYR B 194 N VAL B 168
SHEET 7 C 8 GLU B 219 ILE B 222 1 O ILE B 222 N THR B 197
SHEET 8 C 8 ILE B 235 ILE B 238 -1 O ILE B 238 N GLU B 219
SHEET 1 D 2 LEU B 97 GLU B 99 0
SHEET 2 D 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 2.03
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.03
SSBOND 4 CYS B 22 CYS B 268 1555 1555 2.04
SSBOND 5 CYS B 36 CYS B 41 1555 1555 2.01
SSBOND 6 CYS B 104 CYS B 107 1555 1555 2.08
LINK ND2 ASN A 33 C1 NAG A 301 1555 1555 1.44
LINK ND2 ASN B 33 C1 NAG B 301 1555 1555 1.48
CISPEP 1 LEU A 206 PRO A 207 0 -18.23
CISPEP 2 SER A 217 PRO A 218 0 -1.77
CISPEP 3 LEU B 206 PRO B 207 0 -25.14
CISPEP 4 SER B 217 PRO B 218 0 0.22
SITE 1 AC1 2 ASN A 33 ASP A 48
SITE 1 AC2 9 ARG A 160 LEU A 185 THR A 186 GLN A 188
SITE 2 AC2 9 GLY A 191 THR A 192 LEU A 193 HOH A 454
SITE 3 AC2 9 HOH A 491
SITE 1 AC3 5 ARG A 84 SER A 85 ILE A 86 GLU A 87
SITE 2 AC3 5 THR A 267
SITE 1 AC4 4 ASN A 11 PRO A 229 VAL A 230 PHE A 262
SITE 1 AC5 5 ASN A 94 PHE A 95 PHE A 211 HOH A 480
SITE 2 AC5 5 PHE B 95
SITE 1 AC6 4 LEU A 93 ASN A 94 HIS A 110 HOH A 457
SITE 1 AC7 12 ASP A 62 VAL A 63 THR A 64 ARG A 81
SITE 2 AC7 12 GLY A 82 SER A 83 ARG A 84 SER A 85
SITE 3 AC7 12 ASN A 88 TRP A 89 LEU A 147 LEU A 151
SITE 1 AC8 1 ASN B 33
SITE 1 AC9 2 THR B 231 ARG B 232
SITE 1 BC1 6 LEU A 227 GLN B 15 ASN B 39 PHE B 262
SITE 2 BC1 6 HOH B 420 HOH B 427
SITE 1 BC2 2 SER B 58 GLY B 59
SITE 1 BC3 11 SER A 3 ASP A 5 HOH A 468 HOH A 487
SITE 2 BC3 11 ASP B 5 ASN B 8 GLN B 9 LEU B 12
SITE 3 BC3 11 ASN B 73 LEU B 75 ARG B 139
SITE 1 BC4 7 SER B 83 ARG B 84 TRP B 89 ASN B 92
SITE 2 BC4 7 ASN B 94 HIS B 110 LEU B 147
CRYST1 139.997 139.997 80.492 90.00 90.00 120.00 P 61 12
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 0.007143 0.004124 0.000000 0.00000
SCALE2 0.000000 0.008248 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012424 0.00000
TER 2071 LEU A 269
TER 4142 LEU B 269
MASTER 362 0 13 20 20 0 23 6 4520 2 125 42
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