| content |
HEADER HYDROLASE 01-OCT-02 1MX1
TITLE CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE IN
TITLE 2 COMPLEX WITH TACRINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE I;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: HCEV, ACYL COENZYME A:CHOLESTEROL ACYLTRANSFERASE,
COMPND 5 ACAT, MONOCYTE/MACROPHAGE SERINE ESTERASE, HMSE, SERINE
COMPND 6 ESTERASE 1;
COMPND 7 EC: 3.1.1.1;
COMPND 8 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_CELL_LINE: SF21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS ESTERASE, HYDROLASE, ESTERASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BENCHARIT,C.L.MORTON,J.L.HYATT,P.KUHN,M.K.DANKS,
AUTHOR 2 P.M.POTTER,M.R.REDINBO
REVDAT 1 22-APR-03 1MX1 0
JRNL AUTH S.BENCHARIT,C.L.MORTON,J.L.HYATT,P.KUHN,M.K.DANKS,
JRNL AUTH 2 P.M.POTTER,M.R.REDINBO
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CARBOXYLESTERASE 1
JRNL TITL 2 COMPLEXED WITH THE ALZHEIMER'S DRUG TACRINE: FROM
JRNL TITL 3 BINDING PROMISCUITY TO SELECTIVE INHIBITION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 141078
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) : 0.162
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9914
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 21898
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1650
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 601
REMARK 3 SOLVENT ATOMS : 2117
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.33000
REMARK 3 B22 (A**2) : 2.27000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.75000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.76
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 41.37
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 : THA.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 : THA.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MX1 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-2002.
REMARK 100 THE RCSB ID CODE IS RCSB017266.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-2002
REMARK 200 TEMPERATURE (KELVIN) : 200.0
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) : 1.5418
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141040
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 7.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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) : NULL
REMARK 200 FOR SHELL : NULL
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: NULL
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: PEG3350, GLYCEROL, LITHIUM SULFATE,
REMARK 280 SODIUM CHLORIDE, LITHIUM CHLORIDE, SODIUM CITRATE, PH 5.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 58.51500
REMARK 290 SMTRY3 2 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 6 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 THE AUTHORS HAVE CONFIRMED THAT HUMAN CARBOXYLESTERASE 1
REMARK 300 WILL FORM A TRIMER OR HEXAMER IN SOLUTION BY ATOMIC FORCE
REMARK 300 MICROSCOPY (AFM). THEY FOUND THE RATIO OF
REMARK 300 MONOMER:TRIMER:HEXMER IS ~ 10:44:46. 1MX5 IS A TRIMER AND
REMARK 300 1MX9 IS A HEXAMER. THIS ENTRY CONTAINS A HEXAMER. THE
REMARK 300 AUTHORS FOUND THAT THE TRIMER:HEXMER RATIO IS DEPENDENT
REMARK 300 ON THE TYPE AND AMOUNT OF LIGANDS.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 1019
REMARK 465 PRO A 1020
REMARK 465 LYS A 1554
REMARK 465 ALA A 1555
REMARK 465 VAL A 1556
REMARK 465 GLU A 1557
REMARK 465 LYS A 1558
REMARK 465 PRO A 1559
REMARK 465 PRO A 1560
REMARK 465 GLN A 1561
REMARK 465 THR A 1562
REMARK 465 GLU A 1563
REMARK 465 HIS A 1564
REMARK 465 ILE A 1565
REMARK 465 GLU A 1566
REMARK 465 LEU A 1567
REMARK 465 HIS B 2019
REMARK 465 PRO B 2020
REMARK 465 SER B 2021
REMARK 465 LYS B 2554
REMARK 465 ALA B 2555
REMARK 465 VAL B 2556
REMARK 465 GLU B 2557
REMARK 465 LYS B 2558
REMARK 465 PRO B 2559
REMARK 465 PRO B 2560
REMARK 465 GLN B 2561
REMARK 465 THR B 2562
REMARK 465 GLU B 2563
REMARK 465 HIS B 2564
REMARK 465 ILE B 2565
REMARK 465 GLU B 2566
REMARK 465 LEU B 2567
REMARK 465 HIS C 3019
REMARK 465 PRO C 3020
REMARK 465 SER C 3021
REMARK 465 LYS C 3554
REMARK 465 ALA C 3555
REMARK 465 VAL C 3556
REMARK 465 GLU C 3557
REMARK 465 LYS C 3558
REMARK 465 PRO C 3559
REMARK 465 PRO C 3560
REMARK 465 GLN C 3561
REMARK 465 THR C 3562
REMARK 465 GLU C 3563
REMARK 465 HIS C 3564
REMARK 465 ILE C 3565
REMARK 465 GLU C 3566
REMARK 465 LEU C 3567
REMARK 465 HIS D 4019
REMARK 465 PRO D 4020
REMARK 465 SER D 4021
REMARK 465 LYS D 4554
REMARK 465 ALA D 4555
REMARK 465 VAL D 4556
REMARK 465 GLU D 4557
REMARK 465 LYS D 4558
REMARK 465 PRO D 4559
REMARK 465 PRO D 4560
REMARK 465 GLN D 4561
REMARK 465 THR D 4562
REMARK 465 GLU D 4563
REMARK 465 HIS D 4564
REMARK 465 ILE D 4565
REMARK 465 GLU D 4566
REMARK 465 LEU D 4567
REMARK 465 HIS E 5019
REMARK 465 PRO E 5020
REMARK 465 SER E 5021
REMARK 465 LYS E 5554
REMARK 465 ALA E 5555
REMARK 465 VAL E 5556
REMARK 465 GLU E 5557
REMARK 465 LYS E 5558
REMARK 465 PRO E 5559
REMARK 465 PRO E 5560
REMARK 465 GLN E 5561
REMARK 465 THR E 5562
REMARK 465 GLU E 5563
REMARK 465 HIS E 5564
REMARK 465 ILE E 5565
REMARK 465 GLU E 5566
REMARK 465 LEU E 5567
REMARK 465 HIS F 6019
REMARK 465 PRO F 6020
REMARK 465 SER F 6021
REMARK 465 LYS F 6554
REMARK 465 ALA F 6555
REMARK 465 VAL F 6556
REMARK 465 GLU F 6557
REMARK 465 LYS F 6558
REMARK 465 PRO F 6559
REMARK 465 PRO F 6560
REMARK 465 GLN F 6561
REMARK 465 THR F 6562
REMARK 465 GLU F 6563
REMARK 465 HIS F 6564
REMARK 465 ILE F 6565
REMARK 465 GLU F 6566
REMARK 465 LEU F 6567
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 O LEU A 1051 O1A SIA A 182 1.74
REMARK 500 O SER B 2082 O1A SIA B 282 2.09
REMARK 500 O LEU B 2051 O1A SIA B 282 2.13
REMARK 500 O ASN E 5079 O10 SIA E 582 2.16
REMARK 500 O GLY B 2052 O2 SIA B 282 2.17
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 A1145 SD MET A1145 CE 0.060
REMARK 500 MET A1282 SD MET A1282 CE -0.066
REMARK 500 MET A1347 SD MET A1347 CE 0.057
REMARK 500 PRO A1367 CB PRO A1367 CG 0.043
REMARK 500 MET A1425 SD MET A1425 CE -0.072
REMARK 500 MET A1446 SD MET A1446 CE 0.042
REMARK 500 ARG C3242 CG ARG C3242 CD -0.038
REMARK 500 LYS C3498 CB LYS C3498 CG -0.034
REMARK 500 MET D4282 SD MET D4282 CE -0.041
REMARK 500 MET D4425 SD MET D4425 CE -0.048
REMARK 500 MET D4497 SD MET D4497 CE 0.038
REMARK 500 MET E5145 SD MET E5145 CE 0.038
REMARK 500 MET E5446 SD MET E5446 CE 0.039
REMARK 500 MET E5497 SD MET E5497 CE 0.043
REMARK 500 MET F6136 SD MET F6136 CE 0.047
REMARK 500 MET F6497 SD MET F6497 CE 0.036
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 GLY A1052 N - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 ASP A1090 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 LEU A1097 CA - CB - CG ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A1126 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 PHE A1177 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASN A1204 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 THR A1252 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 SER A1253 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 ILE A1323 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 GLU A1338 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 LEU A1420 CA - CB - CG ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASN A1506 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 ASN A1508 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 GLN A1528 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 LEU B2034 CA - CB - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP B2090 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 PHE B2177 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASN B2204 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 THR B2252 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 SER B2253 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 LEU B2319 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 LEU B2420 CA - CB - CG ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLY B2484 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 GLN B2528 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 SER C3075 N - CA - C ANGL. DEV. = 11.3 DEGREES
REMARK 500 LEU C3112 CA - CB - CG ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP C3126 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 PHE C3177 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASN C3204 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 THR C3252 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 SER C3253 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 LEU C3319 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 ILE C3323 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 LEU C3420 CA - CB - CG ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU C3448 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 GLY C3484 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASN C3508 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 GLN C3528 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 MET D4086 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 PHE D4101 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP D4126 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 PHE D4177 N - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASN D4204 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 THR D4252 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 SER D4253 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 ALA D4337 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 HIS D4342 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 VAL D4344 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 LEU D4420 CA - CB - CG ANGL. DEV. = 9.1 DEGREES
REMARK 500 GLU D4448 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASN D4506 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 GLN D4528 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 LEU E5034 CA - CB - CG ANGL. DEV. = 8.8 DEGREES
REMARK 500 MET E5086 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 PHE E5101 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 PHE E5177 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASN E5204 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 THR E5252 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 SER E5253 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU E5319 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 GLN E5372 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 GLY E5405 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 LEU E5420 CA - CB - CG ANGL. DEV. = 8.7 DEGREES
REMARK 500 SER F6075 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 PHE F6101 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 ASP F6126 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 GLU F6183 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASN F6204 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 THR F6252 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 SER F6253 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 LEU F6319 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 ILE F6323 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 LEU F6420 CA - CB - CG ANGL. DEV. = 7.9 DEGREES
REMARK 500 GLU F6448 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASN F6506 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
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 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHOR'S SEQUENCE HAS NO GLN 362
REMARK 999 (CALLED HCEV IN: KROETZ DL, MCBRIDE OW,
REMARK 999 GONZALEZ FJ.GLYCOSYLATION-DEPENDENT
REMARK 999 ACTIVITY OF BACULOVIRUS-EXPRESSED HUMAN
REMARK 999 LIVER CARBOXYLESTERASES: CDNA CLONING
REMARK 999 AND CHARACTERIZATION OF TWO HIGHLY
REMARK 999 SIMILAR ENZYME FORMS. BIOCHEMISTRY
REMARK 999 1993 NOV 2;32(43):11606-17)
DBREF 1MX1 A 1019 1567 SWS P23141 EST1_HUMAN 19 567
DBREF 1MX1 B 2019 2567 SWS P23141 EST1_HUMAN 19 567
DBREF 1MX1 C 3019 3567 SWS P23141 EST1_HUMAN 19 567
DBREF 1MX1 D 4019 4567 SWS P23141 EST1_HUMAN 19 567
DBREF 1MX1 E 5019 5567 SWS P23141 EST1_HUMAN 19 567
DBREF 1MX1 F 6019 6567 SWS P23141 EST1_HUMAN 19 567
SEQADV 1MX1 A SWS P23141 GLN 362 DELETION
SEQADV 1MX1 B SWS P23141 GLN 362 DELETION
SEQADV 1MX1 C SWS P23141 GLN 362 DELETION
SEQADV 1MX1 D SWS P23141 GLN 362 DELETION
SEQADV 1MX1 E SWS P23141 GLN 362 DELETION
SEQADV 1MX1 F SWS P23141 GLN 362 DELETION
SEQRES 1 A 548 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 A 548 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 A 548 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 A 548 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 A 548 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 A 548 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 A 548 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 A 548 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 A 548 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 A 548 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 A 548 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 A 548 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 A 548 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 A 548 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 A 548 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 A 548 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 A 548 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 A 548 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 A 548 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 A 548 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 A 548 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 A 548 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 A 548 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 A 548 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 A 548 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 A 548 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 A 548 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 A 548 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 A 548 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 A 548 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 A 548 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 A 548 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 A 548 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 A 548 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 A 548 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 A 548 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 A 548 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 A 548 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 A 548 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 A 548 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 A 548 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 A 548 LYS LYS ALA VAL GLU LYS PRO PRO GLN THR GLU HIS ILE
SEQRES 43 A 548 GLU LEU
SEQRES 1 B 548 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 B 548 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 B 548 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 B 548 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 B 548 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 B 548 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 B 548 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 B 548 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 B 548 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 B 548 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 B 548 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 B 548 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 B 548 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 B 548 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 B 548 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 B 548 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 B 548 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 B 548 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 B 548 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 B 548 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 B 548 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 B 548 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 B 548 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 B 548 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 B 548 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 B 548 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 B 548 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 B 548 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 B 548 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 B 548 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 B 548 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 B 548 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 B 548 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 B 548 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 B 548 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 B 548 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 B 548 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 B 548 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 B 548 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 B 548 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 B 548 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 B 548 LYS LYS ALA VAL GLU LYS PRO PRO GLN THR GLU HIS ILE
SEQRES 43 B 548 GLU LEU
SEQRES 1 C 548 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 C 548 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 C 548 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 C 548 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 C 548 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 C 548 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 C 548 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 C 548 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 C 548 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 C 548 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 C 548 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 C 548 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 C 548 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 C 548 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 C 548 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 C 548 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 C 548 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 C 548 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 C 548 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 C 548 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 C 548 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 C 548 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 C 548 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 C 548 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 C 548 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 C 548 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 C 548 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 C 548 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 C 548 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 C 548 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 C 548 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 C 548 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 C 548 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 C 548 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 C 548 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 C 548 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 C 548 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 C 548 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 C 548 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 C 548 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 C 548 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 C 548 LYS LYS ALA VAL GLU LYS PRO PRO GLN THR GLU HIS ILE
SEQRES 43 C 548 GLU LEU
SEQRES 1 D 548 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 D 548 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 D 548 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 D 548 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 D 548 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 D 548 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 D 548 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 D 548 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 D 548 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 D 548 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 D 548 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 D 548 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 D 548 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 D 548 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 D 548 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 D 548 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 D 548 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 D 548 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 D 548 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 D 548 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 D 548 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 D 548 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 D 548 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 D 548 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 D 548 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 D 548 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 D 548 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 D 548 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 D 548 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 D 548 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 D 548 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 D 548 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 D 548 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 D 548 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 D 548 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 D 548 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 D 548 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 D 548 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 D 548 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 D 548 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 D 548 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 D 548 LYS LYS ALA VAL GLU LYS PRO PRO GLN THR GLU HIS ILE
SEQRES 43 D 548 GLU LEU
SEQRES 1 E 548 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 E 548 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 E 548 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 E 548 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 E 548 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 E 548 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 E 548 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 E 548 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 E 548 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 E 548 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 E 548 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 E 548 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 E 548 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 E 548 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 E 548 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 E 548 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 E 548 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 E 548 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 E 548 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 E 548 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 E 548 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 E 548 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 E 548 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 E 548 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 E 548 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 E 548 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 E 548 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 E 548 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 E 548 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 E 548 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 E 548 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 E 548 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 E 548 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 E 548 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 E 548 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 E 548 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 E 548 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 E 548 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 E 548 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 E 548 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 E 548 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 E 548 LYS LYS ALA VAL GLU LYS PRO PRO GLN THR GLU HIS ILE
SEQRES 43 E 548 GLU LEU
SEQRES 1 F 548 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 F 548 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 F 548 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 F 548 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 F 548 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 F 548 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 F 548 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 F 548 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 F 548 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 F 548 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 F 548 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 F 548 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 F 548 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 F 548 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 F 548 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 F 548 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 F 548 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 F 548 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 F 548 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 F 548 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 F 548 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 F 548 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 F 548 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 F 548 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 F 548 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 F 548 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 F 548 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 F 548 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 F 548 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 F 548 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 F 548 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 F 548 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 F 548 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 F 548 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 F 548 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 F 548 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 F 548 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 F 548 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 F 548 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 F 548 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 F 548 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 F 548 LYS LYS ALA VAL GLU LYS PRO PRO GLN THR GLU HIS ILE
SEQRES 43 F 548 GLU LEU
MODRES 1MX1 ASN A 1079 ASN GLYCOSYLATION SITE
MODRES 1MX1 ASN B 2079 ASN GLYCOSYLATION SITE
MODRES 1MX1 ASN C 3079 ASN GLYCOSYLATION SITE
MODRES 1MX1 ASN D 4079 ASN GLYCOSYLATION SITE
MODRES 1MX1 ASN E 5079 ASN GLYCOSYLATION SITE
MODRES 1MX1 ASN F 6079 ASN GLYCOSYLATION SITE
HET NAG A 179 14
HET SIA A 182 21
HET NAG B 279 14
HET SIA B 282 21
HET NAG C 379 14
HET NAG C 380 14
HET NAG D 479 14
HET SIA D 482 21
HET NAG E 579 14
HET SIA E 582 21
HET NAG F 679 14
HET NAG F 680 14
HET THA 1 60
HET THA 2 60
HET THA 3 75
HET THA 4 75
HET THA 5 75
HET THA 6 60
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SIA O-SIALIC ACID
HETNAM THA TACRINE
HETSYN NAG NAG
FORMUL 7 NAG 8(C8 H15 N1 O6)
FORMUL 8 SIA 4(C11 H19 N1 O9)
FORMUL 18 THA 6(C13 H14 N2)
FORMUL 24 HOH *2117(H2 O1)
HELIX 1 1 LEU A 1060 ARG A 1064 5 5
HELIX 2 2 ASP A 1090 THR A 1102 1 13
HELIX 3 3 GLY A 1154 ASN A 1162 1 9
HELIX 4 4 LEU A 1172 PHE A 1178 1 7
HELIX 5 5 ASN A 1188 ILE A 1205 1 18
HELIX 6 6 ALA A 1206 PHE A 1208 5 3
HELIX 7 7 SER A 1221 LEU A 1232 1 12
HELIX 8 8 SER A 1233 LYS A 1237 5 5
HELIX 9 9 THR A 1252 VAL A 1254 5 3
HELIX 10 10 VAL A 1261 ALA A 1272 1 12
HELIX 11 11 THR A 1278 LYS A 1289 1 12
HELIX 12 12 THR A 1290 LYS A 1302 1 13
HELIX 13 13 ASP A 1311 SER A 1315 5 5
HELIX 14 14 THR A 1331 GLU A 1338 1 8
HELIX 15 15 TRP A 1357 MET A 1364 1 7
HELIX 16 16 ASP A 1374 SER A 1385 1 12
HELIX 17 17 SER A 1385 CYS A 1390 1 6
HELIX 18 18 LEU A 1395 GLY A 1405 1 11
HELIX 19 19 ASP A 1409 PHE A 1426 1 18
HELIX 20 20 PHE A 1426 ASP A 1439 1 14
HELIX 21 21 GLU A 1471 PHE A 1476 1 6
HELIX 22 22 GLY A 1477 LEU A 1481 5 5
HELIX 23 23 SER A 1486 GLY A 1507 1 22
HELIX 24 24 LYS A 1540 PHE A 1551 1 12
HELIX 25 25 LEU B 2060 ARG B 2064 5 5
HELIX 26 26 ASP B 2090 THR B 2102 1 13
HELIX 27 27 ALA B 2148 TYR B 2152 5 5
HELIX 28 28 GLY B 2154 ASN B 2162 1 9
HELIX 29 29 LEU B 2172 PHE B 2178 1 7
HELIX 30 30 ASN B 2188 ILE B 2205 1 18
HELIX 31 31 ALA B 2206 PHE B 2208 5 3
HELIX 32 32 SER B 2221 SER B 2233 1 13
HELIX 33 33 PRO B 2234 LYS B 2237 5 4
HELIX 34 34 THR B 2252 VAL B 2254 5 3
HELIX 35 35 VAL B 2261 GLY B 2273 1 13
HELIX 36 36 THR B 2278 LYS B 2289 1 12
HELIX 37 37 THR B 2290 LYS B 2302 1 13
HELIX 38 38 ASP B 2311 SER B 2315 5 5
HELIX 39 39 THR B 2331 GLU B 2338 1 8
HELIX 40 40 TRP B 2357 MET B 2364 1 7
HELIX 41 41 ASP B 2374 SER B 2385 1 12
HELIX 42 42 SER B 2385 CYS B 2390 1 6
HELIX 43 43 LEU B 2395 GLY B 2405 1 11
HELIX 44 44 ASP B 2409 PHE B 2426 1 18
HELIX 45 45 PHE B 2426 ALA B 2440 1 15
HELIX 46 46 GLU B 2471 PHE B 2476 1 6
HELIX 47 47 GLY B 2477 LEU B 2481 5 5
HELIX 48 48 SER B 2486 GLY B 2507 1 22
HELIX 49 49 LYS B 2540 ALA B 2552 1 13
HELIX 50 50 LEU C 3060 ARG C 3064 5 5
HELIX 51 51 ASP C 3090 THR C 3102 1 13
HELIX 52 52 GLY C 3154 ASN C 3162 1 9
HELIX 53 53 LEU C 3172 PHE C 3178 1 7
HELIX 54 54 ASN C 3188 ILE C 3205 1 18
HELIX 55 55 ALA C 3206 PHE C 3208 5 3
HELIX 56 56 SER C 3221 SER C 3233 1 13
HELIX 57 57 PRO C 3234 LYS C 3237 5 4
HELIX 58 58 THR C 3252 VAL C 3254 5 3
HELIX 59 59 VAL C 3261 ALA C 3272 1 12
HELIX 60 60 THR C 3278 LYS C 3289 1 12
HELIX 61 61 THR C 3290 LYS C 3302 1 13
HELIX 62 62 ASP C 3311 SER C 3315 5 5
HELIX 63 63 THR C 3331 GLU C 3338 1 8
HELIX 64 64 TRP C 3357 MET C 3364 1 7
HELIX 65 65 ASP C 3374 SER C 3385 1 12
HELIX 66 66 SER C 3385 CYS C 3390 1 6
HELIX 67 67 ALA C 3392 GLU C 3394 5 3
HELIX 68 68 LEU C 3395 GLY C 3405 1 11
HELIX 69 69 ASP C 3409 PHE C 3426 1 18
HELIX 70 70 PHE C 3426 ALA C 3440 1 15
HELIX 71 71 GLU C 3471 PHE C 3476 1 6
HELIX 72 72 GLY C 3477 LEU C 3481 5 5
HELIX 73 73 SER C 3486 GLY C 3507 1 22
HELIX 74 74 LYS C 3540 LYS C 3553 1 14
HELIX 75 75 LEU D 4060 ARG D 4064 5 5
HELIX 76 76 ASP D 4090 THR D 4102 1 13
HELIX 77 77 GLY D 4154 ASN D 4162 1 9
HELIX 78 78 LEU D 4172 PHE D 4178 1 7
HELIX 79 79 ASN D 4188 ILE D 4205 1 18
HELIX 80 80 ALA D 4206 PHE D 4208 5 3
HELIX 81 81 SER D 4221 LEU D 4232 1 12
HELIX 82 82 SER D 4233 LYS D 4237 5 5
HELIX 83 83 VAL D 4261 ALA D 4272 1 12
HELIX 84 84 THR D 4278 LYS D 4289 1 12
HELIX 85 85 THR D 4290 LYS D 4302 1 13
HELIX 86 86 ASP D 4311 SER D 4315 5 5
HELIX 87 87 THR D 4331 GLU D 4338 1 8
HELIX 88 88 TRP D 4357 MET D 4364 1 7
HELIX 89 89 ASP D 4374 SER D 4385 1 12
HELIX 90 90 SER D 4385 CYS D 4390 1 6
HELIX 91 91 LEU D 4395 GLY D 4405 1 11
HELIX 92 92 ASP D 4409 PHE D 4426 1 18
HELIX 93 93 PHE D 4426 ALA D 4440 1 15
HELIX 94 94 GLU D 4471 PHE D 4476 1 6
HELIX 95 95 GLY D 4477 LEU D 4481 5 5
HELIX 96 96 SER D 4486 GLY D 4507 1 22
HELIX 97 97 LYS D 4540 ALA D 4552 1 13
HELIX 98 98 LEU E 5060 ARG E 5064 5 5
HELIX 99 99 ASP E 5090 THR E 5102 1 13
HELIX 100 100 GLY E 5154 ASN E 5162 1 9
HELIX 101 101 LEU E 5172 PHE E 5178 1 7
HELIX 102 102 ASN E 5188 ILE E 5205 1 18
HELIX 103 103 ALA E 5206 PHE E 5208 5 3
HELIX 104 104 SER E 5221 LEU E 5232 1 12
HELIX 105 105 SER E 5233 LYS E 5237 5 5
HELIX 106 106 THR E 5252 VAL E 5256 5 5
HELIX 107 107 VAL E 5261 GLY E 5273 1 13
HELIX 108 108 THR E 5278 LYS E 5289 1 12
HELIX 109 109 THR E 5290 LYS E 5302 1 13
HELIX 110 110 ASP E 5311 SER E 5315 5 5
HELIX 111 111 THR E 5331 GLU E 5338 1 8
HELIX 112 112 TRP E 5357 MET E 5364 1 7
HELIX 113 113 ASP E 5374 SER E 5385 1 12
HELIX 114 114 SER E 5385 CYS E 5390 1 6
HELIX 115 115 LEU E 5395 GLY E 5405 1 11
HELIX 116 116 ASP E 5409 PHE E 5426 1 18
HELIX 117 117 PHE E 5426 ASP E 5439 1 14
HELIX 118 118 GLU E 5471 PHE E 5476 1 6
HELIX 119 119 GLY E 5477 LEU E 5481 5 5
HELIX 120 120 SER E 5486 GLY E 5507 1 22
HELIX 121 121 LYS E 5540 LYS E 5553 1 14
HELIX 122 122 LEU F 6060 ARG F 6064 5 5
HELIX 123 123 ASP F 6090 THR F 6102 1 13
HELIX 124 124 GLY F 6154 ASN F 6162 1 9
HELIX 125 125 LEU F 6172 PHE F 6178 1 7
HELIX 126 126 ASN F 6188 ILE F 6205 1 18
HELIX 127 127 ALA F 6206 PHE F 6208 5 3
HELIX 128 128 SER F 6221 SER F 6233 1 13
HELIX 129 129 THR F 6252 VAL F 6254 5 3
HELIX 130 130 VAL F 6261 ALA F 6272 1 12
HELIX 131 131 THR F 6278 LYS F 6289 1 12
HELIX 132 132 THR F 6290 LYS F 6302 1 13
HELIX 133 133 ASP F 6311 SER F 6315 5 5
HELIX 134 134 THR F 6331 GLU F 6338 1 8
HELIX 135 135 TRP F 6357 MET F 6364 1 7
HELIX 136 136 ASP F 6374 SER F 6385 1 12
HELIX 137 137 SER F 6385 CYS F 6390 1 6
HELIX 138 138 ALA F 6392 GLU F 6394 5 3
HELIX 139 139 LEU F 6395 GLY F 6405 1 11
HELIX 140 140 ASP F 6409 PHE F 6426 1 18
HELIX 141 141 PHE F 6426 ALA F 6440 1 15
HELIX 142 142 GLU F 6471 PHE F 6476 1 6
HELIX 143 143 GLY F 6477 LEU F 6481 5 5
HELIX 144 144 SER F 6486 GLY F 6507 1 22
HELIX 145 145 LYS F 6540 LYS F 6553 1 14
SHEET 1 A 3 VAL A1025 THR A1028 0
SHEET 2 A 3 GLY A1031 LEU A1034 -1 O VAL A1033 N VAL A1026
SHEET 3 A 3 VAL A1077 ASN A1079 1 O LYS A1078 N LYS A1032
SHEET 1 B11 LYS A1036 VAL A1038 0
SHEET 2 B11 VAL A1047 PRO A1054 -1 O ILE A1049 N LYS A1036
SHEET 3 B11 TYR A1118 THR A1123 -1 O ILE A1121 N PHE A1050
SHEET 4 B11 VAL A1164 ILE A1168 -1 O VAL A1165 N TYR A1122
SHEET 5 B11 LEU A1133 ILE A1139 1 N TRP A1138 O VAL A1166
SHEET 6 B11 GLY A1210 GLU A1220 1 O THR A1216 N VAL A1135
SHEET 7 B11 ARG A1242 GLU A1246 1 O GLU A1246 N GLY A1219
SHEET 8 B11 TYR A1346 ASN A1351 1 O MET A1347 N ALA A1243
SHEET 9 B11 THR A1444 GLN A1450 1 O TYR A1445 N VAL A1348
SHEET 10 B11 GLY A1525 GLY A1530 1 O ILE A1529 N GLN A1450
SHEET 11 B11 GLN A1534 GLN A1537 -1 O ALA A1536 N TYR A1526
SHEET 1 C 2 MET A1086 CYS A1087 0
SHEET 2 C 2 LEU A1112 SER A1113 1 O SER A1113 N MET A1086
SHEET 1 D 2 VAL A1256 LYS A1257 0
SHEET 2 D 2 THR A1321 VAL A1322 1 O THR A1321 N LYS A1257
SHEET 1 E 3 VAL B2025 THR B2028 0
SHEET 2 E 3 GLY B2031 LEU B2034 -1 O VAL B2033 N VAL B2026
SHEET 3 E 3 VAL B2077 ASN B2079 1 O LYS B2078 N LEU B2034
SHEET 1 F11 LYS B2036 VAL B2038 0
SHEET 2 F11 VAL B2047 PRO B2054 -1 O ILE B2049 N LYS B2036
SHEET 3 F11 TYR B2118 THR B2123 -1 O ILE B2121 N PHE B2050
SHEET 4 F11 VAL B2164 ILE B2168 -1 O THR B2167 N ASN B2120
SHEET 5 F11 LEU B2133 ILE B2139 1 N TRP B2138 O VAL B2166
SHEET 6 F11 GLY B2210 GLU B2220 1 O THR B2216 N VAL B2135
SHEET 7 F11 ARG B2242 GLU B2246 1 O GLU B2246 N GLY B2219
SHEET 8 F11 TYR B2346 ASN B2351 1 O MET B2347 N ALA B2243
SHEET 9 F11 THR B2444 GLN B2450 1 O TYR B2445 N VAL B2348
SHEET 10 F11 GLY B2525 GLY B2530 1 O ILE B2529 N GLN B2450
SHEET 11 F11 GLN B2534 GLN B2537 -1 O ALA B2536 N TYR B2526
SHEET 1 G 2 MET B2086 CYS B2087 0
SHEET 2 G 2 LEU B2112 SER B2113 1 O SER B2113 N MET B2086
SHEET 1 H 2 VAL B2256 LYS B2257 0
SHEET 2 H 2 THR B2321 VAL B2322 1 O THR B2321 N LYS B2257
SHEET 1 I 3 VAL C3025 THR C3028 0
SHEET 2 I 3 GLY C3031 LEU C3034 -1 O VAL C3033 N VAL C3026
SHEET 3 I 3 VAL C3077 ASN C3079 1 O LYS C3078 N LYS C3032
SHEET 1 J11 LYS C3036 VAL C3038 0
SHEET 2 J11 VAL C3047 PRO C3054 -1 O ILE C3049 N LYS C3036
SHEET 3 J11 TYR C3118 THR C3123 -1 O ILE C3121 N PHE C3050
SHEET 4 J11 VAL C3164 ILE C3168 -1 O VAL C3165 N TYR C3122
SHEET 5 J11 LEU C3133 ILE C3139 1 N TRP C3138 O VAL C3166
SHEET 6 J11 GLY C3210 GLU C3220 1 O THR C3216 N VAL C3137
SHEET 7 J11 ARG C3242 GLU C3246 1 O GLU C3246 N GLY C3219
SHEET 8 J11 TYR C3346 ASN C3351 1 O MET C3347 N ALA C3243
SHEET 9 J11 THR C3444 GLN C3450 1 O TYR C3445 N VAL C3348
SHEET 10 J11 GLY C3525 GLY C3530 1 O ILE C3529 N GLN C3450
SHEET 11 J11 GLN C3534 GLN C3537 -1 O GLN C3534 N GLN C3528
SHEET 1 K 2 MET C3086 CYS C3087 0
SHEET 2 K 2 LEU C3112 SER C3113 1 O SER C3113 N MET C3086
SHEET 1 L 2 VAL C3256 LYS C3257 0
SHEET 2 L 2 THR C3321 VAL C3322 1 O THR C3321 N LYS C3257
SHEET 1 M 3 VAL D4025 ASP D4027 0
SHEET 2 M 3 LYS D4032 LEU D4034 -1 O VAL D4033 N VAL D4026
SHEET 3 M 3 VAL D4077 ASN D4079 1 O LYS D4078 N LEU D4034
SHEET 1 N11 LYS D4036 LEU D4040 0
SHEET 2 N11 PHE D4043 PRO D4054 -1 O ILE D4049 N LYS D4036
SHEET 3 N11 TYR D4118 THR D4123 -1 O THR D4123 N ALA D4048
SHEET 4 N11 VAL D4164 ILE D4168 -1 O VAL D4165 N TYR D4122
SHEET 5 N11 LEU D4133 ILE D4139 1 N TRP D4138 O VAL D4166
SHEET 6 N11 GLY D4210 GLU D4220 1 O THR D4216 N VAL D4135
SHEET 7 N11 ARG D4242 GLU D4246 1 O GLU D4246 N GLY D4219
SHEET 8 N11 TYR D4346 ASN D4351 1 O MET D4347 N SER D4245
SHEET 9 N11 THR D4444 PHE D4449 1 O PHE D4449 N ILE D4350
SHEET 10 N11 GLY D4525 ILE D4529 1 O ILE D4529 N GLU D4448
SHEET 11 N11 GLN D4534 GLN D4537 -1 O ALA D4536 N TYR D4526
SHEET 1 O 2 MET D4086 CYS D4087 0
SHEET 2 O 2 LEU D4112 SER D4113 1 O SER D4113 N MET D4086
SHEET 1 P 2 VAL D4256 LYS D4257 0
SHEET 2 P 2 THR D4321 VAL D4322 1 O THR D4321 N LYS D4257
SHEET 1 Q 3 VAL E5025 THR E5028 0
SHEET 2 Q 3 GLY E5031 LEU E5034 -1 O VAL E5033 N VAL E5026
SHEET 3 Q 3 VAL E5077 ASN E5079 1 O LYS E5078 N LYS E5032
SHEET 1 R11 LYS E5036 VAL E5038 0
SHEET 2 R11 VAL E5047 PRO E5054 -1 O ILE E5049 N LYS E5036
SHEET 3 R11 TYR E5118 THR E5123 -1 O THR E5123 N ALA E5048
SHEET 4 R11 VAL E5164 ILE E5168 -1 O VAL E5165 N TYR E5122
SHEET 5 R11 LEU E5133 ILE E5139 1 N TRP E5138 O VAL E5166
SHEET 6 R11 GLY E5210 GLU E5220 1 O THR E5216 N VAL E5135
SHEET 7 R11 ARG E5242 GLU E5246 1 O GLU E5246 N GLY E5219
SHEET 8 R11 TYR E5346 ASN E5351 1 O MET E5347 N ALA E5243
SHEET 9 R11 THR E5444 PHE E5449 1 O TYR E5445 N VAL E5348
SHEET 10 R11 GLY E5525 ILE E5529 1 O LEU E5527 N GLU E5448
SHEET 11 R11 GLN E5534 GLN E5537 -1 O ALA E5536 N TYR E5526
SHEET 1 S 2 MET E5086 CYS E5087 0
SHEET 2 S 2 LEU E5112 SER E5113 1 O SER E5113 N MET E5086
SHEET 1 T 3 VAL F6025 THR F6028 0
SHEET 2 T 3 GLY F6031 LEU F6034 -1 O VAL F6033 N VAL F6026
SHEET 3 T 3 VAL F6077 ASN F6079 1 O LYS F6078 N LEU F6034
SHEET 1 U11 LYS F6036 VAL F6038 0
SHEET 2 U11 VAL F6047 PRO F6054 -1 O ILE F6049 N LYS F6036
SHEET 3 U11 TYR F6118 THR F6123 -1 O THR F6123 N ALA F6048
SHEET 4 U11 VAL F6164 ILE F6168 -1 O VAL F6165 N TYR F6122
SHEET 5 U11 LEU F6133 ILE F6139 1 N TRP F6138 O VAL F6166
SHEET 6 U11 GLY F6210 GLU F6220 1 O THR F6216 N VAL F6135
SHEET 7 U11 ARG F6242 GLU F6246 1 O GLU F6246 N GLY F6219
SHEET 8 U11 TYR F6346 ASN F6351 1 O MET F6347 N ALA F6243
SHEET 9 U11 THR F6444 PHE F6449 1 O TYR F6445 N VAL F6348
SHEET 10 U11 GLY F6525 ILE F6529 1 O ILE F6529 N GLU F6448
SHEET 11 U11 GLN F6534 GLN F6537 -1 O GLN F6534 N GLN F6528
SHEET 1 V 2 MET F6086 CYS F6087 0
SHEET 2 V 2 LEU F6112 SER F6113 1 O SER F6113 N MET F6086
SHEET 1 W 2 VAL F6256 LYS F6257 0
SHEET 2 W 2 THR F6321 VAL F6322 1 O THR F6321 N LYS F6257
SSBOND 1 CYS A 1087 CYS A 1116
SSBOND 2 CYS A 1274 CYS A 1285
SSBOND 3 CYS B 2087 CYS B 2116
SSBOND 4 CYS B 2274 CYS B 2285
SSBOND 5 CYS C 3087 CYS C 3116
SSBOND 6 CYS C 3274 CYS C 3285
SSBOND 7 CYS D 4087 CYS D 4116
SSBOND 8 CYS D 4274 CYS D 4285
SSBOND 9 CYS E 5087 CYS E 5116
SSBOND 10 CYS E 5274 CYS E 5285
SSBOND 11 CYS F 6087 CYS F 6116
SSBOND 12 CYS F 6274 CYS F 6285
LINK ND2 ASN A1079 C1 NAG A 179
LINK ND2 ASN B2079 C1 NAG B 279
LINK ND2 ASN C3079 C1 NAG C 379
LINK ND2 ASN D4079 C1 NAG D 479
LINK ND2 ASN E5079 C1 NAG E 579
LINK ND2 ASN F6079 C1 NAG F 679
LINK O4 NAG C 379 C1 NAG C 380
CRYST1 90.021 117.030 176.010 90.00 95.69 90.00 P 1 21 1 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 0.011109 0.000000 0.001107 0.00000
SCALE2 0.000000 0.008545 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005710 0.00000
TER 4131 LYS A1553
TER 8256 LYS B2553
TER 12381 LYS C3553
TER 16506 LYS D4553
TER 20631 LYS E5553
TER 24756 LYS F6553
MASTER 476 0 18 145 106 0 0 627468 6 631 258
END |