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HEADER HYDROLASE 28-APR-02 1LLF
TITLE CHOLESTEROL ESTERASE (CANDIDA CYLINDRACEA) CRYSTAL
TITLE 2 STRUCTURE AT 1.4A RESOLUTION
CAVEAT 1LLF CHIRALITY ERROR AT THE CG CENTER OF MET A445,B1445.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CHOLESTEROL ESTERASE;
COMPND 5 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA CYLINDRACEA;
SOURCE 3 ORGANISM_COMMON: YEAST
KEYWDS CANDIDA CYLINDRACEA CHOLESTEROL ESTERASE, STEROL ESTER
KEYWDS 2 ACYLHYDROLASE, CRYSTAL STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.PLETNEV,A.ADDLAGATTA,Z.WAWRZAK,W.DUAX
REVDAT 1 07-JAN-03 1LLF 0
JRNL AUTH V.PLETNEV,A.ADDLAGATTA,Z.WAWRZAK,W.DUAX
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF HOMODIMERIC
JRNL TITL 2 CHOLESTEROL ESTERASE-LIGAND COMPLEX AT 1.4A
JRNL TITL 3 RESOLUTION
JRNL REF ACTA CRYSTALLOGR., SECT.D V. 59 50 2003
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.GHOSH,Z.WAWRZAK,V.Z.PLETNEV,N.LI,R.KAISER,
REMARK 1 AUTH 2 W.PANGBORN,H.JORNVALL,M.ERMAN,W.L.DUAX
REMARK 1 TITL STRUCTURE OF UNCOMPLEXED AND LINOLEATE-BOUND
REMARK 1 TITL 2 CANDIDA CYLINDRACEA CHOLESTEROL ESTERASE
REMARK 1 REF STRUCTURE V. 3 279 1995
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.142
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.142
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 10338
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 196187
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16063
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 352
REMARK 3 SOLVENT ATOMS : 1078
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 ANGLE DISTANCES (A) : 0.026
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.004
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.377
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.063
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.059
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.106
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.036
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : SHELDRICK
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: KONNERT-HENDRICKSON CONJUGATE
REMARK 3 GRADIENT LEAST SQUARES ALGORITHM
REMARK 4
REMARK 4 1LLF COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-2002.
REMARK 100 THE RCSB ID CODE IS RCSB016053.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.30
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 5IDB
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARUSA
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 206525
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.17800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.800
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: PDB ENTRY 1CLE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, POTASSIUM PHOSPHATE,
REMARK 280 DETERGENT THESIT, PH 7.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS B1218 CD2 HIS B1218 NE2 -0.087
REMARK 500 GLN B1402 NE2 GLN B1402 CD -0.069
REMARK 500 MET B1445 SD MET B1445 CG -0.066
REMARK 500 ASN B1501 ND2 ASN B1501 CG -0.065
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 324 CG - CD - NE ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 324 CD - NE - CZ ANGL. DEV. = 20.9 DEGREES
REMARK 500 MET A 445 CG - SD - CE ANGL. DEV. = 13.6 DEGREES
REMARK 500 GLN B1062 CG - CD - NE2 ANGL. DEV. =-12.5 DEGREES
REMARK 500 GLY B1128 C - N - CA ANGL. DEV. = 16.7 DEGREES
REMARK 500 ARG B1419 CG - CD - NE ANGL. DEV. =-14.4 DEGREES
REMARK 500 MET B1445 CG - SD - CE ANGL. DEV. = 16.5 DEGREES
REMARK 500 ASP B1515 C - N - CA ANGL. DEV. = 13.0 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 ILE A 18 -53.98 71.88
REMARK 500 SER A 209 -114.45 58.43
REMARK 500 ILE A 444 -49.39 71.38
REMARK 500 ILE B1018 -53.46 73.36
REMARK 500 SER B1209 -114.71 58.70
REMARK 500 ILE B1444 -47.63 72.43
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CLE RELATED DB: PDB
REMARK 900 1CLE IS THE 2A RESOLUTION STRUCTURE OF THE SAME ENZYME
REMARK 900 COMPLEXED WITH CHOLESTERYL LINOLEATE LIGAND
DBREF 1LLF A 1 534 SWS P32947 LIP3_CANRU 16 549
DBREF 1LLF B 1001 1534 SWS P32947 LIP3_CANRU 16 549
SEQRES 1 A 534 ALA PRO THR ALA LYS LEU ALA ASN GLY ASP THR ILE THR
SEQRES 2 A 534 GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU GLY ILE
SEQRES 3 A 534 PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG PHE LYS
SEQRES 4 A 534 ASP PRO VAL PRO TYR SER GLY SER LEU ASN GLY GLN LYS
SEQRES 5 A 534 PHE THR SER TYR GLY PRO SER CYS MET GLN GLN ASN PRO
SEQRES 6 A 534 GLU GLY THR PHE GLU GLU ASN LEU GLY LYS THR ALA LEU
SEQRES 7 A 534 ASP LEU VAL MET GLN SER LYS VAL PHE GLN ALA VAL LEU
SEQRES 8 A 534 PRO GLN SER GLU ASP CYS LEU THR ILE ASN VAL VAL ARG
SEQRES 9 A 534 PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO VAL MET
SEQRES 10 A 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU ILE GLY SER PRO
SEQRES 11 A 534 THR ILE PHE PRO PRO ALA GLN MET VAL THR LYS SER VAL
SEQRES 12 A 534 LEU MET GLY LYS PRO ILE ILE HIS VAL ALA VAL ASN TYR
SEQRES 13 A 534 ARG VAL ALA SER TRP GLY PHE LEU ALA GLY ASP ASP ILE
SEQRES 14 A 534 LYS ALA GLU GLY SER GLY ASN ALA GLY LEU LYS ASP GLN
SEQRES 15 A 534 ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE ALA GLY
SEQRES 16 A 534 PHE GLY GLY ASP PRO SER LYS VAL THR ILE PHE GLY GLU
SEQRES 17 A 534 SER ALA GLY SER MET SER VAL LEU CYS HIS LEU ILE TRP
SEQRES 18 A 534 ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO LEU PHE
SEQRES 19 A 534 ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL PRO SER
SEQRES 20 A 534 ASP PRO VAL ASP GLY THR TYR GLY ASN GLU ILE TYR ASP
SEQRES 21 A 534 LEU PHE VAL SER SER ALA GLY CYS GLY SER ALA SER ASP
SEQRES 22 A 534 LYS LEU ALA CYS LEU ARG SER ALA SER SER ASP THR LEU
SEQRES 23 A 534 LEU ASP ALA THR ASN ASN THR PRO GLY PHE LEU ALA TYR
SEQRES 24 A 534 SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY
SEQRES 25 A 534 LYS ASN ILE THR ASP ASP MET TYR LYS LEU VAL ARG ASP
SEQRES 26 A 534 GLY LYS TYR ALA SER VAL PRO VAL ILE ILE GLY ASP GLN
SEQRES 27 A 534 ASN ASP GLU GLY THR ILE PHE GLY LEU SER SER LEU ASN
SEQRES 28 A 534 VAL THR THR ASN ALA GLN ALA ARG ALA TYR PHE LYS GLN
SEQRES 29 A 534 SER PHE ILE HIS ALA SER ASP ALA GLU ILE ASP THR LEU
SEQRES 30 A 534 MET ALA ALA TYR PRO GLN ASP ILE THR GLN GLY SER PRO
SEQRES 31 A 534 PHE ASP THR GLY ILE PHE ASN ALA ILE THR PRO GLN PHE
SEQRES 32 A 534 LYS ARG ILE SER ALA VAL LEU GLY ASP LEU ALA PHE ILE
SEQRES 33 A 534 HIS ALA ARG ARG TYR PHE LEU ASN HIS PHE GLN GLY GLY
SEQRES 34 A 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU
SEQRES 35 A 534 PRO ILE MET GLY THR PHE HIS ALA ASN ASP ILE VAL TRP
SEQRES 36 A 534 GLN ASP TYR LEU LEU GLY SER GLY SER VAL ILE TYR ASN
SEQRES 37 A 534 ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP PRO ASN
SEQRES 38 A 534 THR ALA GLY LEU LEU VAL ASN TRP PRO LYS TYR THR SER
SEQRES 39 A 534 SER SER GLN SER GLY ASN ASN LEU MET MET ILE ASN ALA
SEQRES 40 A 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG THR ALA
SEQRES 41 A 534 GLY TYR ASP ALA LEU MET THR ASN PRO SER SER PHE PHE
SEQRES 42 A 534 VAL
SEQRES 1 B 534 ALA PRO THR ALA LYS LEU ALA ASN GLY ASP THR ILE THR
SEQRES 2 B 534 GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU GLY ILE
SEQRES 3 B 534 PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG PHE LYS
SEQRES 4 B 534 ASP PRO VAL PRO TYR SER GLY SER LEU ASN GLY GLN LYS
SEQRES 5 B 534 PHE THR SER TYR GLY PRO SER CYS MET GLN GLN ASN PRO
SEQRES 6 B 534 GLU GLY THR PHE GLU GLU ASN LEU GLY LYS THR ALA LEU
SEQRES 7 B 534 ASP LEU VAL MET GLN SER LYS VAL PHE GLN ALA VAL LEU
SEQRES 8 B 534 PRO GLN SER GLU ASP CYS LEU THR ILE ASN VAL VAL ARG
SEQRES 9 B 534 PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO VAL MET
SEQRES 10 B 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU ILE GLY SER PRO
SEQRES 11 B 534 THR ILE PHE PRO PRO ALA GLN MET VAL THR LYS SER VAL
SEQRES 12 B 534 LEU MET GLY LYS PRO ILE ILE HIS VAL ALA VAL ASN TYR
SEQRES 13 B 534 ARG VAL ALA SER TRP GLY PHE LEU ALA GLY ASP ASP ILE
SEQRES 14 B 534 LYS ALA GLU GLY SER GLY ASN ALA GLY LEU LYS ASP GLN
SEQRES 15 B 534 ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE ALA GLY
SEQRES 16 B 534 PHE GLY GLY ASP PRO SER LYS VAL THR ILE PHE GLY GLU
SEQRES 17 B 534 SER ALA GLY SER MET SER VAL LEU CYS HIS LEU ILE TRP
SEQRES 18 B 534 ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO LEU PHE
SEQRES 19 B 534 ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL PRO SER
SEQRES 20 B 534 ASP PRO VAL ASP GLY THR TYR GLY ASN GLU ILE TYR ASP
SEQRES 21 B 534 LEU PHE VAL SER SER ALA GLY CYS GLY SER ALA SER ASP
SEQRES 22 B 534 LYS LEU ALA CYS LEU ARG SER ALA SER SER ASP THR LEU
SEQRES 23 B 534 LEU ASP ALA THR ASN ASN THR PRO GLY PHE LEU ALA TYR
SEQRES 24 B 534 SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY
SEQRES 25 B 534 LYS ASN ILE THR ASP ASP MET TYR LYS LEU VAL ARG ASP
SEQRES 26 B 534 GLY LYS TYR ALA SER VAL PRO VAL ILE ILE GLY ASP GLN
SEQRES 27 B 534 ASN ASP GLU GLY THR ILE PHE GLY LEU SER SER LEU ASN
SEQRES 28 B 534 VAL THR THR ASN ALA GLN ALA ARG ALA TYR PHE LYS GLN
SEQRES 29 B 534 SER PHE ILE HIS ALA SER ASP ALA GLU ILE ASP THR LEU
SEQRES 30 B 534 MET ALA ALA TYR PRO GLN ASP ILE THR GLN GLY SER PRO
SEQRES 31 B 534 PHE ASP THR GLY ILE PHE ASN ALA ILE THR PRO GLN PHE
SEQRES 32 B 534 LYS ARG ILE SER ALA VAL LEU GLY ASP LEU ALA PHE ILE
SEQRES 33 B 534 HIS ALA ARG ARG TYR PHE LEU ASN HIS PHE GLN GLY GLY
SEQRES 34 B 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU
SEQRES 35 B 534 PRO ILE MET GLY THR PHE HIS ALA ASN ASP ILE VAL TRP
SEQRES 36 B 534 GLN ASP TYR LEU LEU GLY SER GLY SER VAL ILE TYR ASN
SEQRES 37 B 534 ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP PRO ASN
SEQRES 38 B 534 THR ALA GLY LEU LEU VAL ASN TRP PRO LYS TYR THR SER
SEQRES 39 B 534 SER SER GLN SER GLY ASN ASN LEU MET MET ILE ASN ALA
SEQRES 40 B 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG THR ALA
SEQRES 41 B 534 GLY TYR ASP ALA LEU MET THR ASN PRO SER SER PHE PHE
SEQRES 42 B 534 VAL
MODRES 1LLF ASN A 314 ASN GLYCOSYLATION SITE
MODRES 1LLF ASN A 351 ASN GLYCOSYLATION SITE
MODRES 1LLF ASN B 1314 ASN GLYCOSYLATION SITE
MODRES 1LLF ASN B 1351 ASN GLYCOSYLATION SITE
HET NAG C 535 27
HET NAG C 536 28
HET NAG D 537 27
HET NAG D 538 28
HET NAG E1535 27
HET NAG E1536 28
HET NAG F1537 27
HET NAG F1538 28
HET F23 800 66
HET F23 1800 66
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM F23 TRICOSANOIC ACID
HETSYN NAG NAG
FORMUL 3 NAG 8(C8 H15 N1 O6)
FORMUL 7 F23 2(C23 H46 O2)
FORMUL 9 HOH *1078(H2 O1)
HELIX 1 1 VAL A 33 ARG A 37 5 5
HELIX 2 2 ASN A 72 SER A 84 1 13
HELIX 3 3 SER A 84 LEU A 91 1 8
HELIX 4 4 SER A 129 PHE A 133 5 5
HELIX 5 5 PRO A 135 MET A 145 1 11
HELIX 6 6 VAL A 158 LEU A 164 1 7
HELIX 7 7 GLY A 166 GLY A 173 1 8
HELIX 8 8 ASN A 176 ILE A 193 1 18
HELIX 9 9 ALA A 194 PHE A 196 5 3
HELIX 10 10 SER A 209 TRP A 221 1 13
HELIX 11 11 ASN A 222 ASP A 225 5 4
HELIX 12 12 GLY A 252 ALA A 266 1 15
HELIX 13 13 ASP A 273 ALA A 281 1 9
HELIX 14 14 SER A 282 ASN A 292 1 11
HELIX 15 15 ASP A 318 ASP A 325 1 8
HELIX 16 16 GLY A 342 LEU A 347 1 6
HELIX 17 17 SER A 348 LEU A 350 5 3
HELIX 18 18 THR A 354 PHE A 366 1 13
HELIX 19 19 SER A 370 TYR A 381 1 12
HELIX 20 20 ASP A 384 GLY A 388 5 5
HELIX 21 21 GLN A 402 PHE A 415 1 14
HELIX 22 22 PHE A 415 PHE A 426 1 12
HELIX 23 23 ALA A 450 TYR A 458 1 9
HELIX 24 24 GLY A 463 ASN A 468 1 6
HELIX 25 25 ASN A 468 LEU A 478 1 11
HELIX 26 26 ASP A 479 GLY A 484 5 6
HELIX 27 27 ARG A 518 THR A 527 1 10
HELIX 28 28 ASN A 528 PHE A 533 5 6
HELIX 29 29 VAL B 1033 ARG B 1037 5 5
HELIX 30 30 ASN B 1072 SER B 1084 1 13
HELIX 31 31 SER B 1084 LEU B 1091 1 8
HELIX 32 32 SER B 1129 PHE B 1133 5 5
HELIX 33 33 PRO B 1135 MET B 1145 1 11
HELIX 34 34 VAL B 1158 LEU B 1164 1 7
HELIX 35 35 GLY B 1166 GLY B 1173 1 8
HELIX 36 36 ASN B 1176 ILE B 1193 1 18
HELIX 37 37 ALA B 1194 PHE B 1196 5 3
HELIX 38 38 SER B 1209 TRP B 1221 1 13
HELIX 39 39 ASN B 1222 ASP B 1225 5 4
HELIX 40 40 GLY B 1252 ALA B 1266 1 15
HELIX 41 41 ASP B 1273 ALA B 1281 1 9
HELIX 42 42 SER B 1282 ASN B 1292 1 11
HELIX 43 43 ASP B 1318 ASP B 1325 1 8
HELIX 44 44 GLY B 1342 LEU B 1347 1 6
HELIX 45 45 SER B 1348 LEU B 1350 5 3
HELIX 46 46 THR B 1354 PHE B 1366 1 13
HELIX 47 47 SER B 1370 TYR B 1381 1 12
HELIX 48 48 ASP B 1384 GLY B 1388 5 5
HELIX 49 49 GLN B 1402 PHE B 1415 1 14
HELIX 50 50 PHE B 1415 PHE B 1426 1 12
HELIX 51 51 ALA B 1450 TYR B 1458 1 9
HELIX 52 52 GLY B 1463 ASN B 1468 1 6
HELIX 53 53 ASN B 1468 LEU B 1478 1 11
HELIX 54 54 ASP B 1479 GLY B 1484 5 6
HELIX 55 55 ARG B 1518 THR B 1527 1 10
HELIX 56 56 ASN B 1528 PHE B 1533 5 6
SHEET 1 A 2 THR A 3 LYS A 5 0
SHEET 2 A 2 THR A 11 THR A 13 -1 O ILE A 12 N ALA A 4
SHEET 1 B11 LEU A 15 ASN A 16 0
SHEET 2 B11 GLU A 21 PRO A 27 -1 O ALA A 22 N LEU A 15
SHEET 3 B11 THR A 99 ARG A 104 -1 O VAL A 102 N PHE A 23
SHEET 4 B11 ILE A 150 VAL A 154 -1 O HIS A 151 N VAL A 103
SHEET 5 B11 LEU A 114 ILE A 120 1 N MET A 117 O ILE A 150
SHEET 6 B11 GLY A 198 GLU A 208 1 O THR A 204 N VAL A 116
SHEET 7 B11 ALA A 236 GLN A 240 1 O GLN A 240 N GLY A 207
SHEET 8 B11 VAL A 333 GLN A 338 1 O ILE A 334 N MET A 239
SHEET 9 B11 LYS A 431 SER A 436 1 O SER A 436 N ASP A 337
SHEET 10 B11 LEU A 502 ASN A 506 1 O MET A 503 N LEU A 435
SHEET 11 B11 GLY A 509 GLY A 513 -1 O TYR A 511 N MET A 504
SHEET 1 C 2 THR A 227 TYR A 228 0
SHEET 2 C 2 LYS A 231 PRO A 232 -1 O LYS A 231 N TYR A 228
SHEET 1 D 2 THR B1003 LYS B1005 0
SHEET 2 D 2 THR B1011 THR B1013 -1 O ILE B1012 N ALA B1004
SHEET 1 E11 LEU B1015 ASN B1016 0
SHEET 2 E11 GLU B1021 PRO B1027 -1 O ALA B1022 N LEU B1015
SHEET 3 E11 THR B1099 ARG B1104 -1 O VAL B1102 N PHE B1023
SHEET 4 E11 ILE B1150 VAL B1154 -1 O HIS B1151 N VAL B1103
SHEET 5 E11 LEU B1114 ILE B1120 1 N MET B1117 O ILE B1150
SHEET 6 E11 GLY B1198 GLU B1208 1 O THR B1204 N VAL B1116
SHEET 7 E11 ALA B1236 GLN B1240 1 O GLN B1240 N GLY B1207
SHEET 8 E11 VAL B1333 GLN B1338 1 O ILE B1334 N MET B1239
SHEET 9 E11 LYS B1431 SER B1436 1 O SER B1436 N ASP B1337
SHEET 10 E11 LEU B1502 ASN B1506 1 O MET B1503 N LEU B1435
SHEET 11 E11 GLY B1509 GLY B1513 -1 O TYR B1511 N MET B1504
SHEET 1 F 2 THR B1227 TYR B1228 0
SHEET 2 F 2 LYS B1231 PRO B1232 -1 O LYS B1231 N TYR B1228
SSBOND 1 CYS A 60 CYS A 97
SSBOND 2 CYS A 268 CYS A 277
SSBOND 3 CYS B 1060 CYS B 1097
SSBOND 4 CYS B 1268 CYS B 1277
LINK ND2 ASN A 314 C1 NAG C 535
LINK ND2 ASN A 351 C1 NAG D 537
LINK ND2 ASN B1314 C1 NAG E1535
LINK ND2 ASN B1351 C1 NAG F1537
LINK O4 NAG C 535 C1 NAG C 536
LINK O4 NAG D 537 C1 NAG D 538
LINK O4 NAG E1535 C1 NAG E1536
LINK O4 NAG F1537 C1 NAG F1538
CISPEP 1 SER A 389 PRO A 390 0 5.99
CISPEP 2 SER B 1389 PRO B 1390 0 6.08
CRYST1 58.461 58.477 89.515 92.71 97.48 109.38 P 1 2
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 0.017105 0.006017 0.002841 0.00000
SCALE2 0.000000 0.018128 0.001762 0.00000
SCALE3 0.000000 0.000000 0.011320 0.00000
MASTER 238 0 10 56 30 0 0 617493 2 364 84
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