| content |
HEADER HYDROLASE 17-DEC-04 1YA8
TITLE CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE IN
TITLE 2 COMPLEX WITH CLEAVAGE PRODUCTS OF MEVASTATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CES1 PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HYDROLASE, CARBOXYLESTERASE, MEVASTATIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.FLEMING,S.BENCHARIT,C.C.EDWARDS,J.L.HYATT,C.L.MORTON,
AUTHOR 2 E.L.HOWARD-WILLIAMS,P.M.POTTER,M.R.REDINBO
REVDAT 1 02-AUG-05 1YA8 0
JRNL AUTH C.D.FLEMING,S.BENCHARIT,C.C.EDWARDS,J.L.HYATT,
JRNL AUTH 2 L.TSURKAN,F.BAI,C.FRAGA,C.L.MORTON,
JRNL AUTH 3 E.L.HOWARD-WILLIAMS,P.M.POTTER,M.R.REDINBO
JRNL TITL STRUCTURAL INSIGHTS INTO DRUG PROCESSING BY HUMAN
JRNL TITL 2 CARBOXYLESTERASE 1: TAMOXIFEN, MEVASTATIN, AND
JRNL TITL 3 INHIBITION BY BENZIL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2421972.330
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 41408
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 SET) : 0.187
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2931
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6311
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 442
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12391
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 207
REMARK 3 SOLVENT ATOMS : 347
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.46000
REMARK 3 B22 (A**2) : 6.85000
REMARK 3 B33 (A**2) : -4.38000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.35
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.88
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.370 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.440 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.880 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 34.32
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : MVP.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : MVP.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YA8 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-2005.
REMARK 100 THE RCSB ID CODE IS RCSB031311.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : 9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41408
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 10.800
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : 0.12800
REMARK 200 FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41500
REMARK 200 R SYM FOR SHELL (I) : 0.41500
REMARK 200 FOR SHELL : 3.700
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 CODE 1MX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM CHLORIDE, LITHIUM
REMARK 280 CHLORIDE, LITHIUM SULFATE, CITRATE, GLYCEROL, PH 5.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-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 SMTRY1 2 -1.000000 0.000000 0.000000 27.88850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.43700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.79450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 101.43700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.88850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.79450
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 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
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 MET A 145 SD MET A 145 CE 0.059
REMARK 500 THR A 252 CA THR A 252 CB 0.044
REMARK 500 GLN A 267 CG GLN A 267 CD 0.043
REMARK 500 GLU A 338 N GLU A 338 CA -0.047
REMARK 500 ARG A 339 CA ARG A 339 C -0.066
REMARK 500 MET B 495 SD MET B 495 CE 0.041
REMARK 500 MET C 326 SD MET C 326 CE 0.080
REMARK 500 GLU C 333 CB GLU C 333 CG 0.040
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 LEU A 34 CA - CB - CG ANGL. DEV. = 7.9 DEGREES
REMARK 500 SER A 75 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 THR A 81 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 115 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASN A 204 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 GLN A 316 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 PRO A 317 C - N - CA ANGL. DEV. = 8.7 DEGREES
REMARK 500 LEU A 318 N - CA - C ANGL. DEV. =-19.9 DEGREES
REMARK 500 GLU A 338 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 339 N - CA - C ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASN A 340 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLN A 528 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ILE B 53 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 SER B 75 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASP B 90 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 LEU B 127 CA - CB - CG ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASN B 204 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 SER B 233 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASN B 506 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 LEU C 34 CA - CB - CG ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLU C 41 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 SER C 75 N - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 GLU C 114 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP C 126 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 PHE C 177 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU C 318 CA - CB - CG ANGL. DEV. = 8.3 DEGREES
REMARK 500 LEU C 319 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 LEU C 420 CA - CB - CG ANGL. DEV. = 10.0 DEGREES
REMARK 500 LYS C 538 N - CA - C ANGL. DEV. = 8.7 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 SER C 221 -111.32 52.65
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MX1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE IN
REMARK 900 COMPLEX WITH TACRINE
REMARK 900 RELATED ID: 1MX5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE IN
REMARK 900 COMPLEXED WITH HOMATROPINE, A COCAINE ANALOGUE
REMARK 900 RELATED ID: 1MX9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE IN
REMARK 900 COMPLEXED WITH NALOXONE METHIODIDE, A HEROIN ANALOGUE
REMARK 900 RELATED ID: 1YA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE 1 IN
REMARK 900 COMPLEX WITH TAMOXIFEN
REMARK 900 RELATED ID: 1YAH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE COMPLEXED
REMARK 900 TO ETYL ACETATE; A FATTY ACID ETHYL ESTER ANALOGUE
REMARK 900 RELATED ID: 1YAJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE IN
REMARK 900 COMPLEX WITH BENZIL
DBREF 1YA8 A 21 552 GB 15214585 AAH12418 21 552
DBREF 1YA8 B 21 552 GB 15214585 AAH12418 21 552
DBREF 1YA8 C 21 552 GB 15214585 AAH12418 21 552
SEQRES 1 A 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 A 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 A 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 A 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 A 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 A 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 A 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 A 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 A 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 A 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 A 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 A 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 A 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 A 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 A 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 A 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 A 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 A 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 A 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 A 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 A 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 A 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 A 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 A 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 A 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 A 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 A 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 A 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 A 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 A 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 A 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 A 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 A 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 A 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 A 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 A 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 A 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 A 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 A 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 A 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 A 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 B 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 B 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 B 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 B 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 B 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 B 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 B 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 B 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 B 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 B 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 B 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 B 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 B 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 B 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 B 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 B 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 B 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 B 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 B 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 B 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 B 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 B 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 B 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 B 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 B 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 B 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 B 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 B 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 B 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 B 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 B 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 B 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 B 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 B 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 B 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 B 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 B 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 B 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 B 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 B 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 B 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 C 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 C 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 C 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 C 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 C 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 C 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 C 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 C 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 C 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 C 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 C 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 C 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 C 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 C 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 C 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 C 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 C 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 C 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 C 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 C 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 C 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 C 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 C 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 C 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 C 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 C 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 C 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 C 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 C 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 C 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 C 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 C 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 C 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 C 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 C 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 C 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 C 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 C 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 C 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 C 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 C 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
MODRES 1YA8 ASN A 79 ASN GLYCOSYLATION SITE
MODRES 1YA8 ASN B 79 ASN GLYCOSYLATION SITE
MODRES 1YA8 ASN C 79 ASN GLYCOSYLATION SITE
HET NAG A1179 14
HET SIA 1182 21
HET NAG B1279 14
HET SIA 1282 21
HET NAG C1379 14
HET SIA 1382 21
HET SO4 3184 5
HET SO4 3185 5
HET SO4 3284 5
HET SO4 3285 5
HET SO4 3384 5
HET SO4 3385 5
HET MVB 2011 22
HET MVB 2031 22
HET SMB 4001 7
HET SMB 4002 7
HET SMB 4003 7
HET SMB 4004 7
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SIA O-SIALIC ACID
HETNAM SO4 SULFATE ION
HETNAM MVB (1S,7S,8S,8AR)-1,2,3,7,8,8A-HEXAHYDRO-7-METHYL-8-[2-
HETNAM 2 MVB [(2R,4R)-TETRAHYDRO-4-HY DROXY-6-OXO-2H-PYRAN-2-
HETNAM 3 MVB YL]ETHYL]-1-NAPHTHALENOL
HETNAM SMB 2-METHYLBUTANOIC ACID
HETSYN NAG NAG
FORMUL 4 NAG 3(C8 H15 N1 O6)
FORMUL 5 SIA 3(C11 H19 N1 O9)
FORMUL 10 SO4 6(O4 S1 2-)
FORMUL 16 MVB 2(C18 H26 O4)
FORMUL 18 SMB 4(C5 H10 O2)
FORMUL 22 HOH *347(H2 O1)
HELIX 1 1 LEU A 60 ARG A 64 5 5
HELIX 2 2 ASP A 90 THR A 102 1 13
HELIX 3 3 GLY A 154 ASN A 162 1 9
HELIX 4 4 LEU A 172 PHE A 178 1 7
HELIX 5 5 ASN A 188 ILE A 205 1 18
HELIX 6 6 ALA A 206 PHE A 208 5 3
HELIX 7 7 SER A 221 SER A 233 1 13
HELIX 8 8 THR A 252 VAL A 256 5 5
HELIX 9 9 VAL A 261 ALA A 272 1 12
HELIX 10 10 THR A 278 ARG A 287 1 10
HELIX 11 11 THR A 290 LYS A 302 1 13
HELIX 12 12 ASP A 311 SER A 315 5 5
HELIX 13 13 THR A 331 ALA A 337 1 7
HELIX 14 14 TRP A 357 SER A 365 1 8
HELIX 15 15 ASP A 374 SER A 385 1 12
HELIX 16 16 SER A 385 CYS A 390 1 6
HELIX 17 17 LEU A 395 GLY A 405 1 11
HELIX 18 18 ASP A 409 PHE A 426 1 18
HELIX 19 19 PHE A 426 GLY A 441 1 16
HELIX 20 20 ASP A 470 PHE A 476 1 7
HELIX 21 21 GLY A 477 LEU A 481 5 5
HELIX 22 22 SER A 486 GLY A 507 1 22
HELIX 23 23 LYS A 540 PHE A 551 1 12
HELIX 24 24 LEU B 60 ARG B 64 5 5
HELIX 25 25 ASP B 90 THR B 102 1 13
HELIX 26 26 GLY B 154 ASN B 162 1 9
HELIX 27 27 LEU B 172 PHE B 178 1 7
HELIX 28 28 ASN B 188 ILE B 205 1 18
HELIX 29 29 ALA B 206 PHE B 208 5 3
HELIX 30 30 SER B 221 SER B 233 1 13
HELIX 31 31 THR B 252 VAL B 256 5 5
HELIX 32 32 VAL B 261 GLY B 273 1 13
HELIX 33 33 THR B 278 LYS B 289 1 12
HELIX 34 34 THR B 290 MET B 301 1 12
HELIX 35 35 THR B 331 GLN B 336 1 6
HELIX 36 36 TRP B 357 SER B 365 1 8
HELIX 37 37 ASP B 374 SER B 385 1 12
HELIX 38 38 SER B 385 CYS B 390 1 6
HELIX 39 39 LEU B 395 GLY B 405 1 11
HELIX 40 40 ASP B 409 PHE B 426 1 18
HELIX 41 41 PHE B 426 ALA B 440 1 15
HELIX 42 42 GLU B 471 PHE B 476 1 6
HELIX 43 43 GLY B 477 LEU B 481 5 5
HELIX 44 44 SER B 486 GLY B 507 1 22
HELIX 45 45 LYS B 540 ALA B 552 1 13
HELIX 46 46 LEU C 60 ARG C 64 5 5
HELIX 47 47 ASP C 90 THR C 102 1 13
HELIX 48 48 ALA C 148 TYR C 152 5 5
HELIX 49 49 GLY C 154 ASN C 162 1 9
HELIX 50 50 LEU C 172 PHE C 178 1 7
HELIX 51 51 ASN C 188 ILE C 205 1 18
HELIX 52 52 ALA C 206 PHE C 208 5 3
HELIX 53 53 SER C 221 VAL C 231 1 11
HELIX 54 54 THR C 252 VAL C 256 5 5
HELIX 55 55 VAL C 261 ALA C 272 1 12
HELIX 56 56 THR C 278 LYS C 289 1 12
HELIX 57 57 THR C 290 LYS C 302 1 13
HELIX 58 58 THR C 331 ALA C 337 1 7
HELIX 59 59 TRP C 357 MET C 364 1 7
HELIX 60 60 ASP C 374 SER C 385 1 12
HELIX 61 61 SER C 385 CYS C 390 1 6
HELIX 62 62 LEU C 395 LEU C 404 1 10
HELIX 63 63 ASP C 409 PHE C 426 1 18
HELIX 64 64 PHE C 426 ALA C 440 1 15
HELIX 65 65 GLU C 471 PHE C 476 1 6
HELIX 66 66 GLY C 477 LEU C 481 5 5
HELIX 67 67 SER C 486 GLY C 507 1 22
HELIX 68 68 LYS C 540 ALA C 552 1 13
SHEET 1 A 3 VAL A 25 ASP A 27 0
SHEET 2 A 3 LYS A 32 LEU A 34 -1 O VAL A 33 N VAL A 26
SHEET 3 A 3 VAL A 77 ASN A 79 1 O LYS A 78 N LYS A 32
SHEET 1 B11 LYS A 36 LEU A 40 0
SHEET 2 B11 PHE A 43 PRO A 54 -1 O ILE A 49 N LYS A 36
SHEET 3 B11 TYR A 118 THR A 123 -1 O ILE A 121 N PHE A 50
SHEET 4 B11 VAL A 164 ILE A 168 -1 O VAL A 165 N TYR A 122
SHEET 5 B11 LEU A 133 ILE A 139 1 N TRP A 138 O VAL A 166
SHEET 6 B11 GLY A 210 GLU A 220 1 O THR A 216 N VAL A 135
SHEET 7 B11 ARG A 242 GLU A 246 1 O GLU A 246 N GLY A 219
SHEET 8 B11 TYR A 346 ASN A 351 1 O MET A 347 N SER A 245
SHEET 9 B11 THR A 444 PHE A 449 1 O TYR A 445 N VAL A 348
SHEET 10 B11 GLY A 525 ILE A 529 1 O ILE A 529 N GLU A 448
SHEET 11 B11 GLN A 534 GLN A 537 -1 O GLN A 534 N GLN A 528
SHEET 1 C 2 MET A 86 CYS A 87 0
SHEET 2 C 2 LEU A 112 SER A 113 1 O SER A 113 N MET A 86
SHEET 1 D 3 VAL B 25 THR B 28 0
SHEET 2 D 3 GLY B 31 LEU B 34 -1 O VAL B 33 N VAL B 26
SHEET 3 D 3 VAL B 77 ASN B 79 1 O LYS B 78 N LEU B 34
SHEET 1 E11 LYS B 36 VAL B 38 0
SHEET 2 E11 VAL B 47 PRO B 54 -1 O VAL B 47 N VAL B 38
SHEET 3 E11 TYR B 118 THR B 123 -1 O THR B 123 N ALA B 48
SHEET 4 E11 VAL B 164 ILE B 168 -1 O THR B 167 N ASN B 120
SHEET 5 E11 LEU B 133 ILE B 139 1 N TRP B 138 O VAL B 166
SHEET 6 E11 GLY B 210 GLU B 220 1 O THR B 216 N VAL B 135
SHEET 7 E11 ARG B 242 GLU B 246 1 O ILE B 244 N ILE B 217
SHEET 8 E11 TYR B 346 ASN B 351 1 O MET B 347 N ALA B 243
SHEET 9 E11 THR B 444 PHE B 449 1 O TYR B 445 N VAL B 348
SHEET 10 E11 GLY B 525 ILE B 529 1 O LEU B 527 N GLU B 448
SHEET 11 E11 GLN B 534 GLN B 537 -1 O ALA B 536 N TYR B 526
SHEET 1 F 2 MET B 86 CYS B 87 0
SHEET 2 F 2 LEU B 112 SER B 113 1 O SER B 113 N MET B 86
SHEET 1 G 3 VAL C 25 THR C 28 0
SHEET 2 G 3 GLY C 31 LEU C 34 -1 O GLY C 31 N THR C 28
SHEET 3 G 3 VAL C 77 ASN C 79 1 O LYS C 78 N LYS C 32
SHEET 1 H11 LYS C 36 VAL C 38 0
SHEET 2 H11 VAL C 47 PRO C 54 -1 O ILE C 49 N LYS C 36
SHEET 3 H11 TYR C 118 THR C 123 -1 O ILE C 121 N PHE C 50
SHEET 4 H11 VAL C 164 ILE C 168 -1 O THR C 167 N ASN C 120
SHEET 5 H11 LEU C 133 ILE C 139 1 N TRP C 138 O VAL C 166
SHEET 6 H11 GLY C 210 GLU C 220 1 O THR C 216 N VAL C 135
SHEET 7 H11 ARG C 242 GLU C 246 1 O ILE C 244 N ILE C 217
SHEET 8 H11 TYR C 346 ASN C 351 1 O MET C 347 N ALA C 243
SHEET 9 H11 THR C 444 GLN C 450 1 O TYR C 445 N VAL C 348
SHEET 10 H11 GLY C 525 GLY C 530 1 O ILE C 529 N GLN C 450
SHEET 11 H11 GLN C 534 GLN C 537 -1 O GLN C 534 N GLN C 528
SHEET 1 I 2 MET C 86 CYS C 87 0
SHEET 2 I 2 LEU C 112 SER C 113 1 O SER C 113 N MET C 86
SSBOND 1 CYS A 87 CYS A 116
SSBOND 2 CYS A 274 CYS A 285
SSBOND 3 CYS B 87 CYS B 116
SSBOND 4 CYS B 274 CYS B 285
SSBOND 5 CYS C 87 CYS C 116
SSBOND 6 CYS C 274 CYS C 285
LINK ND2 ASN A 79 C1 NAG A1179
LINK ND2 ASN B 79 C1 NAG B1279
LINK ND2 ASN C 79 C1 NAG C1379
CRYST1 55.777 181.589 202.874 90.00 90.00 90.00 P 21 21 21 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 0.017929 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004929 0.00000
TER 4131 LYS A 553
TER 8262 LYS B 553
TER 12394 LYS C 553
MASTER 318 0 18 68 48 0 0 612945 3 222 123
END |