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HEADER HYDROLASE 14-JUN-12 4FLF
TITLE STRUCTURE OF THREE PHASE PARTITION TREATED LIPASE FROM THERMOMYCES
TITLE 2 LANUGINOSA AT 2.15A RESOLUTION.
CAVEAT 4FLF NAG B 301 HAS WRONG GEOMETRY.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
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 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KUMAR,J.MUKHERJEE,M.SINHA,P.KAUR,M.N.GUPTA,S.SHARMA,T.P.SINGH
REVDAT 1 11-JUL-12 4FLF 0
JRNL AUTH M.KUMAR,J.MUKHERJEE,M.SINHA,P.KAUR,M.N.GUPTA,S.SHARMA,
JRNL AUTH 2 T.P.SINGH
JRNL TITL STRUCTURE OF THREE PHASE PARTITION TREATED LIPASE FROM
JRNL TITL 2 THERMOMYCES LANUGINOSA AT 2.15A RESOLUTION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 46024
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2442
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3274
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.4300
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.4950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4142
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 79
REMARK 3 SOLVENT ATOMS : 288
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.97000
REMARK 3 B22 (A**2) : 1.97000
REMARK 3 B33 (A**2) : -2.96000
REMARK 3 B12 (A**2) : 0.99000
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): 0.198
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.151
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.074
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4321 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5876 ; 2.018 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 536 ; 7.735 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;36.903 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 622 ;18.179 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;22.536 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 636 ; 0.145 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3385 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2658 ; 1.200 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4270 ; 2.088 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1663 ; 2.944 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1606 ; 4.554 ; 4.500
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 : 1.40
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 4FLF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073045.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 : 46024
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08600
REMARK 200 FOR THE DATA SET : 33.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41300
REMARK 200 FOR SHELL : 2.170
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, 0.1M 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 26.83433
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 53.66867
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 40.25150
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 67.08583
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 13.41717
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: 1180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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: 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 25 112.92 155.46
REMARK 500 ASP A 27 42.67 -140.58
REMARK 500 CYS A 41 58.74 -155.51
REMARK 500 ASP A 57 12.38 59.97
REMARK 500 ASN A 92 35.92 -95.83
REMARK 500 SER A 146 -131.49 71.76
REMARK 500 THR A 199 -112.53 38.78
REMARK 500 GLU A 210 0.22 -67.50
REMARK 500 ASP A 254 131.40 -171.27
REMARK 500 ALA A 257 9.35 -61.61
REMARK 500 PHE A 262 -30.54 66.74
REMARK 500 ASN B 25 -169.22 -115.95
REMARK 500 ASN B 26 125.74 58.24
REMARK 500 ASP B 27 12.94 80.72
REMARK 500 CYS B 41 57.88 -147.51
REMARK 500 ILE B 100 66.96 -152.13
REMARK 500 SER B 146 -137.11 64.54
REMARK 500 GLN B 188 132.88 -34.21
REMARK 500 THR B 199 -112.83 39.63
REMARK 500 ASP B 242 30.16 38.95
REMARK 500 PHE B 262 -26.22 64.94
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 GOL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XXH 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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EA6 RELATED DB: PDB
DBREF 4FLF A 1 269 UNP O59952 LIP_THELA 23 291
DBREF 4FLF 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 4FLF ASN B 33 ASN GLYCOSYLATION SITE
MODRES 4FLF ASN A 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 GOL A 306 6
HET XXH A 307 11
HET NAG B 301 14
HET GOL B 302 6
HET EDO B 303 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM GOL GLYCEROL
HETNAM XXH 4-NITROBENZALDEHYDE
HETNAM EDO 1,2-ETHANEDIOL
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 9 XXH C7 H5 N O3
FORMUL 12 EDO C2 H6 O2
FORMUL 13 HOH *288(H2 O)
HELIX 1 1 SER A 3 GLY A 23 1 21
HELIX 2 2 CYS A 41 LYS A 46 1 6
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 LEU A 259 5 5
HELIX 11 11 SER B 3 GLY B 23 1 21
HELIX 12 12 CYS B 41 ALA B 47 1 7
HELIX 13 13 SER B 85 ASN B 92 1 8
HELIX 14 14 GLY B 112 HIS B 135 1 24
HELIX 15 15 SER B 146 ARG B 160 1 15
HELIX 16 16 ASN B 178 GLN B 188 1 11
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 ASP B 254 LEU B 259 1 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 VAL A 141 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 SER A 170
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 THR B 143 N LEU B 78
SHEET 5 C 8 ILE B 166 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 VAL B 236 ILE B 238 -1 O VAL B 236 N TRP B 221
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 2.04
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.04
SSBOND 3 CYS A 104 CYS A 107 1555 1555 2.00
SSBOND 4 CYS B 22 CYS B 268 1555 1555 2.03
SSBOND 5 CYS B 36 CYS B 41 1555 1555 2.00
SSBOND 6 CYS B 104 CYS B 107 1555 1555 2.10
LINK ND2 ASN B 33 C1 NAG B 301 1555 1555 1.48
LINK ND2 ASN A 33 C1 NAG A 301 1555 1555 1.48
CISPEP 1 LEU A 206 PRO A 207 0 -6.90
CISPEP 2 SER A 217 PRO A 218 0 -2.82
CISPEP 3 LEU B 206 PRO B 207 0 -13.64
CISPEP 4 SER B 217 PRO B 218 0 1.44
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 469
SITE 3 AC2 9 HOH A 522
SITE 1 AC3 6 ARG A 84 SER A 85 ILE A 86 GLU A 87
SITE 2 AC3 6 GLY A 266 THR A 267
SITE 1 AC4 3 ASN A 11 VAL A 230 PHE A 262
SITE 1 AC5 2 GLY A 225 VAL A 228
SITE 1 AC6 5 LEU A 93 PHE A 95 PHE A 211 HOH A 476
SITE 2 AC6 5 PHE B 95
SITE 1 AC7 9 SER A 3 ASP A 5 ASP B 5 ASN B 8
SITE 2 AC7 9 GLN B 9 ASN B 73 ARG B 139 HOH B 494
SITE 3 AC7 9 HOH B 496
SITE 1 AC8 2 ASN B 33 ASP B 48
SITE 1 AC9 3 GLN B 4 THR B 231 ARG B 232
SITE 1 BC1 4 GLN B 15 ASN B 39 HOH B 489 HOH B 504
CRYST1 139.996 139.996 80.503 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 0.012422 0.00000
TER 2072 LEU A 269
TER 4144 LEU B 269
MASTER 323 0 10 19 20 0 16 6 4509 2 93 42
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