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HEADER HYDROLASE 17-DEC-04 1YAJ
TITLE CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE IN
TITLE 2 COMPLEX WITH BENZIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CES1 PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
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, BENZIL, INHIBITION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.FLEMING,S.BENCHARIT,C.C.EDWARDS,J.L.HYATT,C.M.MORTON,
AUTHOR 2 E.L.HOWARD-WILLIAMS,P.M.POTTER,M.R.REDINBO
REVDAT 1 02-AUG-05 1YAJ 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. 3.20 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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2488896.980
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 124749
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) : 0.207
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8767
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 19288
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1392
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49566
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 753
REMARK 3 SOLVENT ATOMS : 474
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 14.78000
REMARK 3 B22 (A**2) : -8.19000
REMARK 3 B33 (A**2) : -6.60000
REMARK 3 B12 (A**2) : 0.91000
REMARK 3 B13 (A**2) : 3.16000
REMARK 3 B23 (A**2) : 2.47000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.50
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) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.66
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.219
REMARK 3 BOND ANGLES (DEGREES) : 3.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.47
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 : 0.37
REMARK 3 BSOL : 40.92
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 : COV.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 : COV.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YAJ 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 RCSB031318.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-2003
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 : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.022
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 124749
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
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 (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.15600
REMARK 200 R SYM (I) : 0.15600
REMARK 200 FOR THE DATA SET : 3.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44600
REMARK 200 R SYM FOR SHELL (I) : 0.44600
REMARK 200 FOR SHELL : 1.800
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 1MX5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
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 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, 2, 3, 4
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 12CHAIN(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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 4
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PRO H 23 O
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 PHE G 303 O PRO G 317 1.84
REMARK 500 OG SER E 221 O HOH 6469 1.90
REMARK 500 OG SER L 221 O HOH 6474 1.91
REMARK 500 O PHE I 303 O PRO I 317 1.96
REMARK 500 OG SER F 221 O2 BEZ F 5023 1.98
REMARK 500 O PHE L 303 O PRO L 317 2.02
REMARK 500 N ALA E 222 O HOH 6472 2.04
REMARK 500 O9 SIA 982 O HOH 6011 2.09
REMARK 500 OG SER B 221 O HOH 6470 2.12
REMARK 500 NZ LYS C 414 O2 BEZ 113 2.12
REMARK 500 O TRP K 138 O HOH 6407 2.19
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 GLY A 181 C GLY A 181 O -0.102
REMARK 500 ASP A 182 CB ASP A 182 CG -0.114
REMARK 500 LEU A 550 CA LEU A 550 C 0.230
REMARK 500 LEU A 550 C LEU A 550 O -0.153
REMARK 500 PRO B 24 CA PRO B 24 C 0.231
REMARK 500 VAL B 77 CA VAL B 77 CB -0.102
REMARK 500 VAL B 77 CB VAL B 77 CG1 0.149
REMARK 500 MET B 145 SD MET B 145 CE 0.089
REMARK 500 TRP B 175 CZ3 TRP B 175 CH2 -0.092
REMARK 500 MET B 326 SD MET B 326 CE 0.099
REMARK 500 LYS C 57 CA LYS C 57 CB 0.134
REMARK 500 LYS C 57 CB LYS C 57 CG 0.112
REMARK 500 LYS C 57 CG LYS C 57 CD 0.089
REMARK 500 LYS C 57 CA LYS C 57 C 0.152
REMARK 500 PRO C 67 CB PRO C 67 CG -0.085
REMARK 500 TRP C 74 CZ3 TRP C 74 CH2 -0.081
REMARK 500 MET C 136 SD MET C 136 CE 0.085
REMARK 500 TRP C 189 CE3 TRP C 189 CZ3 -0.090
REMARK 500 MET D 136 SD MET D 136 CE 0.085
REMARK 500 MET D 326 SD MET D 326 CE 0.103
REMARK 500 LEU D 550 CA LEU D 550 C 0.088
REMARK 500 PRO E 24 CA PRO E 24 C 0.263
REMARK 500 PRO E 23 C PRO E 24 N 0.146
REMARK 500 LEU E 34 CG LEU E 34 CD1 0.086
REMARK 500 LEU E 34 CG LEU E 34 CD2 -0.147
REMARK 500 VAL E 77 CA VAL E 77 CB -0.221
REMARK 500 VAL E 77 CB VAL E 77 CG1 0.337
REMARK 500 MET E 145 SD MET E 145 CE 0.115
REMARK 500 TRP E 383 CZ3 TRP E 383 CH2 -0.096
REMARK 500 LYS F 57 CA LYS F 57 CB 0.163
REMARK 500 LYS F 57 CB LYS F 57 CG 0.291
REMARK 500 LYS F 57 CG LYS F 57 CD -0.095
REMARK 500 LYS F 57 CA LYS F 57 C 0.136
REMARK 500 LYS G 57 CA LYS G 57 CB 0.119
REMARK 500 LYS G 57 CB LYS G 57 CG 0.140
REMARK 500 LYS G 57 CA LYS G 57 C 0.150
REMARK 500 LYS G 57 C LYS G 57 O 0.113
REMARK 500 PRO G 58 CB PRO G 58 CG -0.088
REMARK 500 MET G 86 SD MET G 86 CE 0.093
REMARK 500 GLY G 181 C GLY G 181 O -0.166
REMARK 500 ASP G 182 N ASP G 182 CA 0.086
REMARK 500 ASP G 182 CB ASP G 182 CG 0.085
REMARK 500 ARG G 186 CG ARG G 186 CD -0.132
REMARK 500 TRP G 189 CE2 TRP G 189 CZ2 -0.130
REMARK 500 TRP G 189 CE3 TRP G 189 CZ3 -0.154
REMARK 500 MET G 326 SD MET G 326 CE 0.086
REMARK 500 LEU G 550 CA LEU G 550 C 0.344
REMARK 500 LEU G 550 C PHE G 551 N -0.333
REMARK 500 PRO H 24 CA PRO H 24 C 0.097
REMARK 500 PRO H 23 C PRO H 24 N 0.196
REMARK 500 TRP H 74 CZ3 TRP H 74 CH2 -0.083
REMARK 500 VAL H 77 CB VAL H 77 CG1 0.415
REMARK 500 MET H 145 SD MET H 145 CE 0.083
REMARK 500 PRO I 24 CD PRO I 24 N 0.091
REMARK 500 PRO I 24 CA PRO I 24 C 0.246
REMARK 500 LYS I 57 CA LYS I 57 CB 0.093
REMARK 500 LYS I 57 CB LYS I 57 CG 0.218
REMARK 500 LYS I 57 CA LYS I 57 C 0.099
REMARK 500 VAL I 77 CA VAL I 77 CB -0.109
REMARK 500 MET I 145 SD MET I 145 CE 0.123
REMARK 500 MET I 282 SD MET I 282 CE 0.094
REMARK 500 TRP I 383 CG TRP I 383 CD2 0.161
REMARK 500 TRP I 383 CG TRP I 383 CD1 0.135
REMARK 500 TRP I 383 CD1 TRP I 383 NE1 0.094
REMARK 500 TRP I 383 NE1 TRP I 383 CE2 0.142
REMARK 500 TRP I 383 CE2 TRP I 383 CZ2 0.288
REMARK 500 TRP I 383 CE2 TRP I 383 CD2 0.259
REMARK 500 TRP I 383 CD2 TRP I 383 CE3 0.207
REMARK 500 TRP I 383 CE3 TRP I 383 CZ3 0.349
REMARK 500 TRP I 383 CH2 TRP I 383 CZ2 0.087
REMARK 500 LYS J 57 CA LYS J 57 CB 0.132
REMARK 500 LYS J 57 CB LYS J 57 CG 0.166
REMARK 500 LYS J 57 CA LYS J 57 C 0.146
REMARK 500 ARG J 186 CB ARG J 186 CG 0.124
REMARK 500 TRP J 547 CZ3 TRP J 547 CH2 -0.084
REMARK 500 TRP K 74 CZ3 TRP K 74 CH2 -0.102
REMARK 500 MET K 145 SD MET K 145 CE 0.094
REMARK 500 TRP K 175 CZ3 TRP K 175 CH2 -0.084
REMARK 500 LEU K 550 CA LEU K 550 C 0.132
REMARK 500 LEU K 550 C PHE K 551 N 0.178
REMARK 500 PRO L 23 C PRO L 24 N 0.116
REMARK 500 VAL L 77 CB VAL L 77 CG1 0.159
REMARK 500 VAL L 77 CB VAL L 77 CG2 -0.149
REMARK 500 MET L 145 SD MET L 145 CE 0.107
REMARK 500 TRP L 175 CZ3 TRP L 175 CH2 -0.118
REMARK 500 MET L 326 SD MET L 326 CE 0.134
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 A 181 CA - C - N ANGL. DEV. = 11.4 DEGREES
REMARK 500 PHE A 303 N - CA - C ANGL. DEV. = 17.3 DEGREES
REMARK 500 ASN A 510 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU A 550 CA - C - O ANGL. DEV. =-10.3 DEGREES
REMARK 500 LEU A 550 O - C - N ANGL. DEV. = 13.9 DEGREES
REMARK 500 PRO B 24 CB - CA - C ANGL. DEV. =-12.4 DEGREES
REMARK 500 PRO B 24 CA - CB - CG ANGL. DEV. = -8.5 DEGREES
REMARK 500 PRO B 24 N - CA - C ANGL. DEV. =-12.7 DEGREES
REMARK 500 PRO B 24 C - N - CA ANGL. DEV. = -8.8 DEGREES
REMARK 500 LEU B 319 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 LYS C 57 CB - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 LYS C 57 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 LEU C 420 CA - CB - CG ANGL. DEV. = 9.1 DEGREES
REMARK 500 PHE D 303 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 ASN D 510 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 PRO E 24 CB - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 PRO E 24 CA - CB - CG ANGL. DEV. = -8.7 DEGREES
REMARK 500 PRO E 24 N - CA - C ANGL. DEV. =-13.7 DEGREES
REMARK 500 PRO E 24 C - N - CA ANGL. DEV. =-14.2 DEGREES
REMARK 500 SER E 75 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 PHE E 303 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 LYS F 57 CB - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 LYS F 57 CA - CB - CG ANGL. DEV. = 12.6 DEGREES
REMARK 500 LYS F 57 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 ASP F 126 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 GLU F 183 CA - CB - CG ANGL. DEV. = 8.6 DEGREES
REMARK 500 GLU F 448 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 LEU G 34 CA - CB - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 LYS G 57 CB - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 LYS G 57 C - N - CA ANGL. DEV. =-10.6 DEGREES
REMARK 500 GLY G 181 N - CA - C ANGL. DEV. =-18.5 DEGREES
REMARK 500 GLY G 181 CA - C - O ANGL. DEV. =-11.0 DEGREES
REMARK 500 ASP G 182 CB - CG - OD1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 GLY G 181 CA - C - N ANGL. DEV. = 20.3 DEGREES
REMARK 500 GLY G 181 O - C - N ANGL. DEV. = -9.3 DEGREES
REMARK 500 ASP G 182 C - N - CA ANGL. DEV. = -9.0 DEGREES
REMARK 500 PHE G 303 N - CA - C ANGL. DEV. = 17.0 DEGREES
REMARK 500 LEU G 304 CA - CB - CG ANGL. DEV. = 8.3 DEGREES
REMARK 500 LEU G 550 CA - C - O ANGL. DEV. =-27.3 DEGREES
REMARK 500 LEU G 550 O - C - N ANGL. DEV. = 21.6 DEGREES
REMARK 500 PHE G 551 C - N - CA ANGL. DEV. =-12.0 DEGREES
REMARK 500 PRO H 24 C - N - CA ANGL. DEV. =-11.3 DEGREES
REMARK 500 HIS H 30 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 SER H 75 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 VAL H 77 N - CA - CB ANGL. DEV. = -8.8 DEGREES
REMARK 500 PHE H 303 N - CA - C ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU H 304 CA - CB - CG ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU H 319 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 PRO I 24 CA - N - CD ANGL. DEV. = -9.9 DEGREES
REMARK 500 PRO I 24 CB - CA - C ANGL. DEV. =-14.0 DEGREES
REMARK 500 PRO I 24 CA - CB - CG ANGL. DEV. = -9.4 DEGREES
REMARK 500 PRO I 24 N - CA - C ANGL. DEV. =-12.6 DEGREES
REMARK 500 PRO I 24 C - N - CA ANGL. DEV. = -9.9 DEGREES
REMARK 500 LEU I 34 CB - CG - CD2 ANGL. DEV. = -9.3 DEGREES
REMARK 500 ILE I 53 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 LYS I 57 CB - CA - C ANGL. DEV. = 11.3 DEGREES
REMARK 500 LYS I 57 CB - CG - CD ANGL. DEV. = 12.2 DEGREES
REMARK 500 PHE I 303 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 TRP I 383 CA - CB - CG ANGL. DEV. =-11.6 DEGREES
REMARK 500 TRP I 383 CB - CG - CD2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 TRP I 383 CE2 - CD2 - CE3 ANGL. DEV. = -9.5 DEGREES
REMARK 500 LEU J 34 CA - CB - CG ANGL. DEV. = 8.8 DEGREES
REMARK 500 LYS J 57 CB - CA - C ANGL. DEV. = 11.7 DEGREES
REMARK 500 SER K 75 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 GLY K 181 CA - C - N ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG K 242 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 PHE K 303 N - CA - C ANGL. DEV. = 17.4 DEGREES
REMARK 500 LEU K 550 N - CA - C ANGL. DEV. =-11.8 DEGREES
REMARK 500 PRO L 24 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 VAL L 77 CA - CB - CG2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 PHE L 303 CB - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 PHE L 303 N - CA - C ANGL. DEV. = 18.6 DEGREES
REMARK 500 LEU L 304 CA - CB - CG ANGL. DEV. = 8.3 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 I 221 -118.19 61.51
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: 1YA8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE IN
REMARK 900 COMPLEX WITH CLEAVAGE PRODUCTS OF MEVASTATIN
DBREF 1YAJ A 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ B 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ C 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ D 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ E 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ F 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ G 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ H 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ I 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ J 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ K 21 552 GB 15214585 AAH12418 21 552
DBREF 1YAJ L 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
SEQRES 1 D 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 D 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 D 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 D 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 D 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 D 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 D 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 D 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 D 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 D 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 D 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 D 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 D 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 D 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 D 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 D 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 D 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 D 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 D 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 D 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 D 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 D 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 D 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 D 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 D 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 D 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 D 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 D 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 D 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 D 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 D 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 D 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 D 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 D 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 D 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 D 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 D 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 D 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 D 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 D 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 D 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 E 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 E 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 E 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 E 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 E 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 E 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 E 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 E 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 E 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 E 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 E 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 E 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 E 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 E 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 E 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 E 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 E 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 E 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 E 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 E 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 E 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 E 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 E 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 E 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 E 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 E 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 E 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 E 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 E 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 E 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 E 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 E 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 E 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 E 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 E 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 E 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 E 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 E 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 E 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 E 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 E 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 F 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 F 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 F 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 F 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 F 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 F 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 F 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 F 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 F 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 F 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 F 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 F 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 F 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 F 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 F 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 F 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 F 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 F 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 F 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 F 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 F 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 F 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 F 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 F 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 F 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 F 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 F 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 F 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 F 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 F 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 F 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 F 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 F 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 F 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 F 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 F 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 F 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 F 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 F 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 F 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 F 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 G 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 G 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 G 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 G 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 G 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 G 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 G 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 G 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 G 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 G 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 G 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 G 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 G 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 G 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 G 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 G 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 G 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 G 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 G 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 G 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 G 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 G 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 G 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 G 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 G 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 G 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 G 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 G 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 G 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 G 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 G 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 G 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 G 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 G 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 G 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 G 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 G 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 G 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 G 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 G 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 G 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 H 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 H 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 H 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 H 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 H 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 H 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 H 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 H 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 H 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 H 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 H 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 H 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 H 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 H 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 H 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 H 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 H 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 H 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 H 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 H 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 H 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 H 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 H 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 H 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 H 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 H 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 H 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 H 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 H 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 H 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 H 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 H 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 H 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 H 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 H 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 H 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 H 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 H 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 H 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 H 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 H 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 I 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 I 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 I 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 I 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 I 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 I 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 I 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 I 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 I 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 I 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 I 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 I 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 I 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 I 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 I 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 I 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 I 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 I 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 I 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 I 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 I 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 I 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 I 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 I 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 I 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 I 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 I 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 I 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 I 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 I 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 I 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 I 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 I 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 I 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 I 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 I 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 I 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 I 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 I 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 I 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 I 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 J 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 J 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 J 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 J 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 J 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 J 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 J 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 J 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 J 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 J 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 J 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 J 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 J 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 J 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 J 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 J 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 J 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 J 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 J 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 J 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 J 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 J 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 J 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 J 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 J 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 J 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 J 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 J 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 J 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 J 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 J 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 J 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 J 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 J 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 J 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 J 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 J 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 J 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 J 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 J 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 J 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 K 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 K 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 K 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 K 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 K 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 K 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 K 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 K 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 K 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 K 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 K 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 K 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 K 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 K 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 K 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 K 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 K 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 K 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 K 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 K 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 K 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 K 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 K 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 K 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 K 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 K 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 K 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 K 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 K 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 K 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 K 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 K 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 K 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 K 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 K 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 K 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 K 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 K 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 K 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 K 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 K 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 L 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 L 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 L 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 L 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 L 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 L 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 L 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 L 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 L 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 L 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 L 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 L 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 L 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 L 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 L 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 L 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 L 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 L 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 L 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 L 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 L 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 L 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 L 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 L 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 L 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 L 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 L 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 L 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 L 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 L 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 L 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 L 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 L 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 L 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 L 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 L 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 L 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 L 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 L 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 L 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 L 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
MODRES 1YAJ ASN A 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN B 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN C 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN D 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN E 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN F 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN G 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN H 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN I 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN J 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN K 79 ASN GLYCOSYLATION SITE
MODRES 1YAJ ASN L 79 ASN GLYCOSYLATION SITE
HET NAG A1179 14
HET SIA 182 21
HET NAG B1279 14
HET SIA 282 21
HET NAG C1379 14
HET SIA 382 21
HET NAG D2179 14
HET SIA 482 21
HET NAG E2279 14
HET SIA 582 21
HET NAG F2379 14
HET SIA 682 21
HET NAG G3179 14
HET SIA 782 21
HET NAG H3279 14
HET SIA 882 21
HET NAG I3379 14
HET SIA 982 21
HET NAG J4179 14
HET SIA 1082 21
HET NAG K4279 14
HET SIA 1182 21
HET NAG L4379 14
HET SIA 1282 21
HET SO4 1184 5
HET SO4 1185 5
HET SO4 1284 5
HET SO4 1285 5
HET SO4 1384 5
HET SO4 1385 5
HET SO4 2184 5
HET SO4 2185 5
HET SO4 2284 5
HET SO4 2285 5
HET SO4 2384 5
HET SO4 2385 5
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 SO4 4184 5
HET SO4 4185 5
HET SO4 4284 5
HET SO4 4285 5
HET SO4 4384 5
HET SO4 4385 5
HET BEZ C5013 8
HET BEZ F5023 8
HET BEZ J5041 8
HET BEZ 11 9
HET BEZ 21 9
HET BEZ 31 9
HET BEZ 32 9
HET BEZ 33 9
HET BEZ 42 9
HET BEZ 43 9
HET BEZ 111 9
HET BEZ 112 9
HET BEZ 121 9
HET BEZ 122 9
HET BEZ 123 9
HET BEZ 131 9
HET BEZ 132 9
HET BEZ 133 9
HET BEZ 141 9
HET BEZ 142 9
HET BEZ 143 9
HET BEZ 12 9
HET BEZ 22 9
HET BEZ 113 9
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SIA O-SIALIC ACID
HETNAM SO4 SULFATE ION
HETNAM BEZ BENZOIC ACID
HETSYN NAG NAG
FORMUL 13 NAG 12(C8 H15 N1 O6)
FORMUL 14 SIA 12(C11 H19 N1 O9)
FORMUL 37 SO4 24(O4 S1 2-)
FORMUL 61 BEZ 24(C7 H6 O2)
FORMUL 85 HOH *474(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 ASP A 203 1 16
HELIX 6 6 ASN A 204 PHE A 208 5 5
HELIX 7 7 SER A 221 SER A 233 1 13
HELIX 8 8 PRO A 234 LYS A 237 5 4
HELIX 9 9 THR A 252 VAL A 256 5 5
HELIX 10 10 VAL A 261 GLY A 273 1 13
HELIX 11 11 THR A 278 LYS A 289 1 12
HELIX 12 12 THR A 290 LYS A 302 1 13
HELIX 13 13 THR A 331 GLN A 336 1 6
HELIX 14 14 TRP A 357 SER A 365 1 8
HELIX 15 15 ASP A 374 LYS A 384 1 11
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 ALA A 440 1 15
HELIX 20 20 GLU A 471 PHE A 476 1 6
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 ALA B 392 GLU B 394 5 3
HELIX 40 40 LEU B 395 GLY B 405 1 11
HELIX 41 41 THR B 410 PHE B 426 1 17
HELIX 42 42 PHE B 426 ALA B 440 1 15
HELIX 43 43 ASP B 470 PHE B 476 1 7
HELIX 44 44 GLY B 477 LEU B 481 5 5
HELIX 45 45 SER B 486 GLY B 507 1 22
HELIX 46 46 LYS B 540 PHE B 551 1 12
HELIX 47 47 LEU C 60 ARG C 64 5 5
HELIX 48 48 ASP C 90 THR C 102 1 13
HELIX 49 49 GLY C 154 GLU C 161 1 8
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 SER C 233 1 13
HELIX 54 54 THR C 252 VAL C 254 5 3
HELIX 55 55 VAL C 261 ALA C 272 1 12
HELIX 56 56 THR C 278 ARG C 287 1 10
HELIX 57 57 THR C 290 LYS C 302 1 13
HELIX 58 58 THR C 331 GLN C 336 1 6
HELIX 59 59 TRP C 357 MET C 364 1 7
HELIX 60 60 PRO C 367 GLY C 371 5 5
HELIX 61 61 ASP C 374 SER C 385 1 12
HELIX 62 62 SER C 385 CYS C 390 1 6
HELIX 63 63 LEU C 395 LEU C 404 1 10
HELIX 64 64 VAL C 411 PHE C 426 1 16
HELIX 65 65 PHE C 426 ASP C 439 1 14
HELIX 66 66 GLU C 471 PHE C 476 1 6
HELIX 67 67 GLY C 477 LEU C 481 5 5
HELIX 68 68 SER C 486 GLY C 507 1 22
HELIX 69 69 LYS C 540 ALA C 552 1 13
HELIX 70 70 LEU D 60 ARG D 64 5 5
HELIX 71 71 ASP D 90 THR D 102 1 13
HELIX 72 72 GLY D 154 ASN D 162 1 9
HELIX 73 73 LEU D 172 PHE D 178 1 7
HELIX 74 74 ASN D 188 ASP D 203 1 16
HELIX 75 75 ASN D 204 PHE D 208 5 5
HELIX 76 76 SER D 221 LEU D 232 1 12
HELIX 77 77 SER D 233 LYS D 237 5 5
HELIX 78 78 VAL D 261 GLY D 273 1 13
HELIX 79 79 THR D 278 GLN D 288 1 11
HELIX 80 80 THR D 290 LYS D 302 1 13
HELIX 81 81 ASP D 311 SER D 315 5 5
HELIX 82 82 THR D 331 ALA D 337 1 7
HELIX 83 83 TRP D 357 SER D 365 1 8
HELIX 84 84 LYS D 376 LYS D 384 1 9
HELIX 85 85 SER D 385 CYS D 390 1 6
HELIX 86 86 LEU D 395 GLY D 405 1 11
HELIX 87 87 ASP D 409 PHE D 426 1 18
HELIX 88 88 PHE D 426 ASP D 439 1 14
HELIX 89 89 ASP D 470 PHE D 476 1 7
HELIX 90 90 GLY D 477 LEU D 481 5 5
HELIX 91 91 SER D 486 GLY D 507 1 22
HELIX 92 92 LYS D 540 ALA D 552 1 13
HELIX 93 93 LEU E 60 ARG E 64 5 5
HELIX 94 94 ASP E 90 THR E 102 1 13
HELIX 95 95 GLY E 154 ASN E 162 1 9
HELIX 96 96 GLY E 173 PHE E 178 1 6
HELIX 97 97 ASN E 188 ILE E 205 1 18
HELIX 98 98 ALA E 206 PHE E 208 5 3
HELIX 99 99 SER E 221 SER E 233 1 13
HELIX 100 100 THR E 252 VAL E 256 5 5
HELIX 101 101 VAL E 261 ALA E 272 1 12
HELIX 102 102 THR E 278 LYS E 289 1 12
HELIX 103 103 THR E 290 MET E 301 1 12
HELIX 104 104 THR E 331 ALA E 337 1 7
HELIX 105 105 TRP E 357 SER E 365 1 8
HELIX 106 106 ASP E 374 SER E 385 1 12
HELIX 107 107 SER E 385 CYS E 390 1 6
HELIX 108 108 LEU E 395 TYR E 403 1 9
HELIX 109 109 VAL E 411 PHE E 426 1 16
HELIX 110 110 PHE E 426 ALA E 442 1 17
HELIX 111 111 GLU E 471 PHE E 476 1 6
HELIX 112 112 GLY E 477 LEU E 481 5 5
HELIX 113 113 SER E 486 GLY E 507 1 22
HELIX 114 114 LYS E 540 PHE E 551 1 12
HELIX 115 115 LEU F 60 ARG F 64 5 5
HELIX 116 116 ASP F 90 THR F 102 1 13
HELIX 117 117 ALA F 148 TYR F 152 5 5
HELIX 118 118 GLY F 154 GLU F 161 1 8
HELIX 119 119 LEU F 172 PHE F 178 1 7
HELIX 120 120 ASN F 188 ILE F 205 1 18
HELIX 121 121 ALA F 206 PHE F 208 5 3
HELIX 122 122 SER F 221 LEU F 232 1 12
HELIX 123 123 THR F 252 VAL F 256 5 5
HELIX 124 124 VAL F 261 ALA F 272 1 12
HELIX 125 125 THR F 278 ARG F 287 1 10
HELIX 126 126 THR F 290 LYS F 302 1 13
HELIX 127 127 THR F 331 GLN F 336 1 6
HELIX 128 128 TRP F 357 MET F 364 1 7
HELIX 129 129 ASP F 374 SER F 385 1 12
HELIX 130 130 SER F 385 CYS F 390 1 6
HELIX 131 131 LEU F 395 GLY F 405 1 11
HELIX 132 132 VAL F 411 PHE F 426 1 16
HELIX 133 133 PHE F 426 ALA F 440 1 15
HELIX 134 134 GLU F 471 PHE F 476 1 6
HELIX 135 135 GLY F 477 LEU F 481 5 5
HELIX 136 136 SER F 486 GLY F 507 1 22
HELIX 137 137 LYS F 540 PHE F 551 1 12
HELIX 138 138 LEU G 60 ARG G 64 5 5
HELIX 139 139 ASP G 90 THR G 102 1 13
HELIX 140 140 ALA G 148 TYR G 152 5 5
HELIX 141 141 GLY G 154 GLU G 161 1 8
HELIX 142 142 LEU G 172 PHE G 178 1 7
HELIX 143 143 ASN G 188 ILE G 205 1 18
HELIX 144 144 ALA G 206 PHE G 208 5 3
HELIX 145 145 SER G 221 SER G 233 1 13
HELIX 146 146 PRO G 234 LYS G 237 5 4
HELIX 147 147 THR G 252 VAL G 256 5 5
HELIX 148 148 VAL G 261 ALA G 272 1 12
HELIX 149 149 THR G 278 LYS G 289 1 12
HELIX 150 150 THR G 290 LYS G 302 1 13
HELIX 151 151 THR G 331 GLN G 336 1 6
HELIX 152 152 TRP G 357 MET G 364 1 7
HELIX 153 153 ASP G 374 SER G 385 1 12
HELIX 154 154 SER G 385 CYS G 390 1 6
HELIX 155 155 ALA G 392 GLU G 394 5 3
HELIX 156 156 LEU G 395 LEU G 404 1 10
HELIX 157 157 VAL G 411 PHE G 426 1 16
HELIX 158 158 PHE G 426 ASP G 439 1 14
HELIX 159 159 GLU G 471 PHE G 476 1 6
HELIX 160 160 GLY G 477 LEU G 481 5 5
HELIX 161 161 SER G 486 GLY G 507 1 22
HELIX 162 162 LYS G 540 ALA G 552 1 13
HELIX 163 163 LEU H 60 ARG H 64 5 5
HELIX 164 164 ASP H 90 THR H 102 1 13
HELIX 165 165 ALA H 148 TYR H 152 5 5
HELIX 166 166 GLY H 154 ASN H 162 1 9
HELIX 167 167 LEU H 172 PHE H 178 1 7
HELIX 168 168 ASN H 188 ILE H 205 1 18
HELIX 169 169 ALA H 206 PHE H 208 5 3
HELIX 170 170 SER H 221 SER H 233 1 13
HELIX 171 171 THR H 252 VAL H 256 5 5
HELIX 172 172 VAL H 261 GLY H 273 1 13
HELIX 173 173 THR H 278 ARG H 287 1 10
HELIX 174 174 THR H 290 LYS H 302 1 13
HELIX 175 175 THR H 331 GLU H 338 1 8
HELIX 176 176 TRP H 357 SER H 365 1 8
HELIX 177 177 ASP H 374 LYS H 384 1 11
HELIX 178 178 SER H 385 CYS H 390 1 6
HELIX 179 179 ALA H 392 GLU H 394 5 3
HELIX 180 180 LEU H 395 GLY H 405 1 11
HELIX 181 181 ASP H 409 PHE H 426 1 18
HELIX 182 182 PHE H 426 ALA H 440 1 15
HELIX 183 183 ASP H 470 PHE H 476 1 7
HELIX 184 184 GLY H 477 LEU H 481 5 5
HELIX 185 185 SER H 486 GLY H 507 1 22
HELIX 186 186 LYS H 540 ALA H 552 1 13
HELIX 187 187 LEU I 60 ARG I 64 5 5
HELIX 188 188 ASP I 90 THR I 102 1 13
HELIX 189 189 ALA I 148 TYR I 152 5 5
HELIX 190 190 GLY I 154 ASN I 162 1 9
HELIX 191 191 GLY I 173 PHE I 178 1 6
HELIX 192 192 ASN I 188 ILE I 205 1 18
HELIX 193 193 ALA I 206 PHE I 208 5 3
HELIX 194 194 SER I 221 SER I 233 1 13
HELIX 195 195 THR I 252 VAL I 256 5 5
HELIX 196 196 VAL I 261 GLY I 273 1 13
HELIX 197 197 THR I 278 GLN I 288 1 11
HELIX 198 198 THR I 290 MET I 301 1 12
HELIX 199 199 ASP I 311 SER I 315 5 5
HELIX 200 200 THR I 331 ALA I 337 1 7
HELIX 201 201 TRP I 357 SER I 365 1 8
HELIX 202 202 ASP I 374 SER I 385 1 12
HELIX 203 203 SER I 385 CYS I 390 1 6
HELIX 204 204 LEU I 395 GLY I 405 1 11
HELIX 205 205 ASP I 409 PHE I 426 1 18
HELIX 206 206 PHE I 426 ALA I 440 1 15
HELIX 207 207 GLU I 471 PHE I 476 1 6
HELIX 208 208 GLY I 477 LEU I 481 5 5
HELIX 209 209 SER I 486 GLY I 507 1 22
HELIX 210 210 LYS I 540 PHE I 551 1 12
HELIX 211 211 LEU J 60 ARG J 64 5 5
HELIX 212 212 ASP J 90 THR J 102 1 13
HELIX 213 213 ALA J 148 TYR J 152 5 5
HELIX 214 214 GLY J 154 ASN J 162 1 9
HELIX 215 215 LEU J 172 PHE J 178 1 7
HELIX 216 216 ASN J 188 ASP J 203 1 16
HELIX 217 217 ASN J 204 PHE J 208 5 5
HELIX 218 218 SER J 221 SER J 233 1 13
HELIX 219 219 THR J 252 VAL J 256 5 5
HELIX 220 220 VAL J 261 ALA J 272 1 12
HELIX 221 221 THR J 278 LYS J 289 1 12
HELIX 222 222 THR J 290 LYS J 302 1 13
HELIX 223 223 THR J 331 GLN J 336 1 6
HELIX 224 224 TRP J 357 MET J 364 1 7
HELIX 225 225 ASP J 374 SER J 385 1 12
HELIX 226 226 SER J 385 CYS J 390 1 6
HELIX 227 227 ALA J 392 GLU J 394 5 3
HELIX 228 228 LEU J 395 LEU J 404 1 10
HELIX 229 229 ASP J 409 PHE J 426 1 18
HELIX 230 230 PHE J 426 ALA J 440 1 15
HELIX 231 231 ASP J 470 PHE J 476 1 7
HELIX 232 232 GLY J 477 LEU J 481 5 5
HELIX 233 233 SER J 486 GLY J 507 1 22
HELIX 234 234 LYS J 540 PHE J 551 1 12
HELIX 235 235 LEU K 60 ARG K 64 5 5
HELIX 236 236 ASP K 90 THR K 102 1 13
HELIX 237 237 GLY K 154 ASN K 162 1 9
HELIX 238 238 LEU K 172 PHE K 178 1 7
HELIX 239 239 ASN K 188 ASP K 203 1 16
HELIX 240 240 ASN K 204 PHE K 208 5 5
HELIX 241 241 SER K 221 SER K 233 1 13
HELIX 242 242 THR K 252 VAL K 256 5 5
HELIX 243 243 VAL K 261 GLY K 273 1 13
HELIX 244 244 THR K 278 LYS K 289 1 12
HELIX 245 245 THR K 290 LEU K 299 1 10
HELIX 246 246 ASP K 311 SER K 315 5 5
HELIX 247 247 THR K 331 GLN K 336 1 6
HELIX 248 248 TRP K 357 SER K 365 1 8
HELIX 249 249 ASP K 374 SER K 385 1 12
HELIX 250 250 SER K 385 CYS K 390 1 6
HELIX 251 251 LEU K 395 GLY K 405 1 11
HELIX 252 252 ASP K 409 PHE K 426 1 18
HELIX 253 253 PHE K 426 ALA K 440 1 15
HELIX 254 254 ASP K 470 PHE K 476 1 7
HELIX 255 255 GLY K 477 LEU K 481 5 5
HELIX 256 256 SER K 486 GLY K 507 1 22
HELIX 257 257 LYS K 540 PHE K 551 1 12
HELIX 258 258 LEU L 60 ARG L 64 5 5
HELIX 259 259 ASP L 90 THR L 102 1 13
HELIX 260 260 GLY L 154 ASN L 162 1 9
HELIX 261 261 GLY L 173 PHE L 178 1 6
HELIX 262 262 ASN L 188 ASP L 203 1 16
HELIX 263 263 ASN L 204 PHE L 208 5 5
HELIX 264 264 SER L 221 SER L 233 1 13
HELIX 265 265 THR L 252 VAL L 256 5 5
HELIX 266 266 VAL L 261 GLY L 273 1 13
HELIX 267 267 THR L 278 LYS L 289 1 12
HELIX 268 268 THR L 290 MET L 301 1 12
HELIX 269 269 THR L 331 ALA L 337 1 7
HELIX 270 270 TRP L 357 MET L 364 1 7
HELIX 271 271 ASP L 374 SER L 385 1 12
HELIX 272 272 SER L 385 CYS L 390 1 6
HELIX 273 273 LEU L 395 GLY L 405 1 11
HELIX 274 274 VAL L 411 PHE L 426 1 16
HELIX 275 275 PHE L 426 GLY L 441 1 16
HELIX 276 276 GLU L 471 PHE L 476 1 6
HELIX 277 277 GLY L 477 LYS L 482 1 6
HELIX 278 278 SER L 486 GLY L 507 1 22
HELIX 279 279 LYS L 540 PHE L 551 1 12
SHEET 1 A 3 VAL A 25 THR A 28 0
SHEET 2 A 3 GLY A 31 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 LEU A 34
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 THR A 167 N ASN A 120
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 ARG A 242 N ILE A 217
SHEET 8 B11 TYR A 346 ASN A 351 1 O MET A 347 N SER A 245
SHEET 9 B11 THR A 444 GLN A 450 1 O PHE A 449 N ILE A 350
SHEET 10 B11 TYR A 526 GLY A 530 1 O ILE A 529 N GLN A 450
SHEET 11 B11 GLN A 534 ALA A 535 -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 ASP B 27 0
SHEET 2 D 3 LYS B 32 LEU B 34 -1 O VAL B 33 N VAL B 26
SHEET 3 D 3 VAL B 77 LYS B 78 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 LEU B 51 -1 O VAL B 47 N VAL B 38
SHEET 3 E11 LEU B 119 THR B 123 -1 O ILE B 121 N PHE B 50
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 ASN B 211 N LEU B 133
SHEET 7 E11 ARG B 242 GLU B 246 1 O GLU B 246 N GLY B 219
SHEET 8 E11 TYR B 346 ASN B 351 1 O MET B 347 N SER B 245
SHEET 9 E11 THR B 444 GLN B 450 1 O TYR B 445 N VAL B 348
SHEET 10 E11 GLY B 525 GLY B 530 1 O ILE B 529 N GLN B 450
SHEET 11 E11 GLN B 534 GLN B 537 -1 O GLN B 534 N GLN B 528
SHEET 1 F 3 VAL C 25 THR C 28 0
SHEET 2 F 3 GLY C 31 LEU C 34 -1 O VAL C 33 N VAL C 26
SHEET 3 F 3 VAL C 77 ASN C 79 1 O LYS C 78 N LEU C 34
SHEET 1 G11 LYS C 36 VAL C 38 0
SHEET 2 G11 VAL C 47 PRO C 54 -1 O VAL C 47 N VAL C 38
SHEET 3 G11 TYR C 118 THR C 123 -1 O ILE C 121 N PHE C 50
SHEET 4 G11 VAL C 164 ILE C 168 -1 O VAL C 165 N TYR C 122
SHEET 5 G11 LEU C 133 ILE C 139 1 N TRP C 138 O VAL C 166
SHEET 6 G11 GLY C 210 GLU C 220 1 O PHE C 218 N ILE C 139
SHEET 7 G11 ARG C 242 GLU C 246 1 O ILE C 244 N ILE C 217
SHEET 8 G11 TYR C 346 ASN C 351 1 O MET C 347 N ALA C 243
SHEET 9 G11 THR C 444 GLN C 450 1 O TYR C 447 N ILE C 350
SHEET 10 G11 GLY C 525 GLY C 530 1 O ILE C 529 N GLN C 450
SHEET 11 G11 GLN C 534 GLN C 537 -1 O ALA C 536 N TYR C 526
SHEET 1 H 2 MET C 86 CYS C 87 0
SHEET 2 H 2 LEU C 112 SER C 113 1 O SER C 113 N MET C 86
SHEET 1 I 2 VAL C 256 LYS C 257 0
SHEET 2 I 2 THR C 321 VAL C 322 1 O THR C 321 N LYS C 257
SHEET 1 J 3 VAL D 25 THR D 28 0
SHEET 2 J 3 GLY D 31 LEU D 34 -1 O VAL D 33 N VAL D 26
SHEET 3 J 3 VAL D 77 ASN D 79 1 O LYS D 78 N LEU D 34
SHEET 1 K11 LYS D 36 VAL D 38 0
SHEET 2 K11 VAL D 47 PRO D 54 -1 O ILE D 49 N LYS D 36
SHEET 3 K11 TYR D 118 THR D 123 -1 O THR D 123 N ALA D 48
SHEET 4 K11 VAL D 164 ILE D 168 -1 O VAL D 165 N TYR D 122
SHEET 5 K11 LEU D 133 ILE D 139 1 N TRP D 138 O VAL D 166
SHEET 6 K11 GLY D 210 GLU D 220 1 O PHE D 218 N ILE D 139
SHEET 7 K11 ARG D 242 GLU D 246 1 O GLU D 246 N GLY D 219
SHEET 8 K11 TYR D 346 ASN D 351 1 O MET D 347 N SER D 245
SHEET 9 K11 THR D 444 GLN D 450 1 O PHE D 449 N ILE D 350
SHEET 10 K11 GLY D 525 GLY D 530 1 O ILE D 529 N GLN D 450
SHEET 11 K11 GLN D 534 GLN D 537 -1 O ALA D 536 N TYR D 526
SHEET 1 L 2 MET D 86 CYS D 87 0
SHEET 2 L 2 LEU D 112 SER D 113 1 O SER D 113 N MET D 86
SHEET 1 M 3 VAL E 25 VAL E 26 0
SHEET 2 M 3 LYS E 32 LEU E 34 -1 O VAL E 33 N VAL E 26
SHEET 3 M 3 VAL E 77 ASN E 79 1 O LYS E 78 N LEU E 34
SHEET 1 N 9 LYS E 36 VAL E 38 0
SHEET 2 N 9 VAL E 47 PRO E 54 -1 O VAL E 47 N VAL E 38
SHEET 3 N 9 TYR E 118 THR E 123 -1 O THR E 123 N ALA E 48
SHEET 4 N 9 VAL E 164 ILE E 168 -1 O VAL E 165 N TYR E 122
SHEET 5 N 9 LEU E 133 ILE E 139 1 N MET E 136 O VAL E 166
SHEET 6 N 9 GLY E 210 GLU E 220 1 O THR E 216 N VAL E 135
SHEET 7 N 9 ARG E 242 GLU E 246 1 O GLU E 246 N GLY E 219
SHEET 8 N 9 TYR E 346 ASN E 351 1 O MET E 347 N ALA E 243
SHEET 9 N 9 THR E 444 PHE E 449 1 O TYR E 445 N VAL E 348
SHEET 1 O 2 GLY E 525 GLN E 528 0
SHEET 2 O 2 GLN E 534 GLN E 537 -1 O GLN E 534 N GLN E 528
SHEET 1 P 3 VAL F 25 ASP F 27 0
SHEET 2 P 3 LYS F 32 LEU F 34 -1 O VAL F 33 N VAL F 26
SHEET 3 P 3 LYS F 78 ASN F 79 1 O LYS F 78 N LYS F 32
SHEET 1 Q11 LYS F 36 PHE F 37 0
SHEET 2 Q11 ALA F 48 PRO F 54 -1 O ILE F 49 N LYS F 36
SHEET 3 Q11 TYR F 118 THR F 123 -1 O ILE F 121 N PHE F 50
SHEET 4 Q11 VAL F 164 ILE F 168 -1 O THR F 167 N ASN F 120
SHEET 5 Q11 LEU F 133 ILE F 139 1 N TRP F 138 O VAL F 166
SHEET 6 Q11 GLY F 210 GLU F 220 1 O PHE F 218 N ILE F 139
SHEET 7 Q11 ARG F 242 GLU F 246 1 O ILE F 244 N ILE F 217
SHEET 8 Q11 TYR F 346 ASN F 351 1 O MET F 347 N ALA F 243
SHEET 9 Q11 THR F 444 GLN F 450 1 O TYR F 445 N VAL F 348
SHEET 10 Q11 GLY F 525 GLY F 530 1 O ILE F 529 N GLU F 448
SHEET 11 Q11 GLN F 534 GLN F 537 -1 O GLN F 534 N GLN F 528
SHEET 1 R 3 VAL G 25 ASP G 27 0
SHEET 2 R 3 LYS G 32 LEU G 34 -1 O VAL G 33 N VAL G 26
SHEET 3 R 3 VAL G 77 ASN G 79 1 O LYS G 78 N LYS G 32
SHEET 1 S11 LYS G 36 VAL G 38 0
SHEET 2 S11 VAL G 47 PRO G 54 -1 O VAL G 47 N VAL G 38
SHEET 3 S11 TYR G 118 THR G 123 -1 O ILE G 121 N PHE G 50
SHEET 4 S11 VAL G 164 ILE G 168 -1 O VAL G 165 N TYR G 122
SHEET 5 S11 LEU G 133 ILE G 139 1 N TRP G 138 O VAL G 166
SHEET 6 S11 GLY G 210 GLU G 220 1 O ASN G 211 N LEU G 133
SHEET 7 S11 ARG G 242 GLU G 246 1 O GLU G 246 N GLY G 219
SHEET 8 S11 TYR G 346 ASN G 351 1 O MET G 347 N ALA G 243
SHEET 9 S11 THR G 444 PHE G 449 1 O PHE G 449 N ILE G 350
SHEET 10 S11 GLY G 525 GLN G 528 1 O LEU G 527 N MET G 446
SHEET 11 S11 GLN G 534 GLN G 537 -1 O ALA G 536 N TYR G 526
SHEET 1 T 3 VAL H 25 THR H 28 0
SHEET 2 T 3 GLY H 31 LEU H 34 -1 O VAL H 33 N VAL H 26
SHEET 3 T 3 VAL H 77 ASN H 79 1 O LYS H 78 N LEU H 34
SHEET 1 U11 LYS H 36 VAL H 38 0
SHEET 2 U11 VAL H 47 PRO H 54 -1 O ILE H 49 N LYS H 36
SHEET 3 U11 TYR H 118 THR H 123 -1 O LEU H 119 N ILE H 53
SHEET 4 U11 VAL H 164 ILE H 168 -1 O VAL H 165 N TYR H 122
SHEET 5 U11 LEU H 133 ILE H 139 1 N TRP H 138 O VAL H 166
SHEET 6 U11 GLY H 210 GLU H 220 1 O THR H 216 N VAL H 135
SHEET 7 U11 ARG H 242 GLU H 246 1 O GLU H 246 N GLY H 219
SHEET 8 U11 TYR H 346 ASN H 351 1 O GLY H 349 N SER H 245
SHEET 9 U11 THR H 444 GLN H 450 1 O TYR H 447 N ILE H 350
SHEET 10 U11 GLY H 525 GLY H 530 1 O LEU H 527 N GLU H 448
SHEET 11 U11 GLN H 534 GLN H 537 -1 O ALA H 536 N TYR H 526
SHEET 1 V 2 MET H 86 CYS H 87 0
SHEET 2 V 2 LEU H 112 SER H 113 1 O SER H 113 N MET H 86
SHEET 1 W 3 VAL I 25 THR I 28 0
SHEET 2 W 3 GLY I 31 LEU I 34 -1 O VAL I 33 N VAL I 26
SHEET 3 W 3 VAL I 77 ASN I 79 1 O LYS I 78 N LYS I 32
SHEET 1 X11 LYS I 36 VAL I 38 0
SHEET 2 X11 VAL I 47 PRO I 54 -1 O VAL I 47 N VAL I 38
SHEET 3 X11 TYR I 118 THR I 123 -1 O THR I 123 N ALA I 48
SHEET 4 X11 VAL I 164 ILE I 168 -1 O THR I 167 N ASN I 120
SHEET 5 X11 LEU I 133 ILE I 139 1 N MET I 136 O VAL I 166
SHEET 6 X11 GLY I 210 GLU I 220 1 O ASN I 211 N LEU I 133
SHEET 7 X11 ARG I 242 GLU I 246 1 O GLU I 246 N GLY I 219
SHEET 8 X11 TYR I 346 ASN I 351 1 O MET I 347 N SER I 245
SHEET 9 X11 THR I 444 PHE I 449 1 O TYR I 445 N VAL I 348
SHEET 10 X11 GLY I 525 GLN I 528 1 O LEU I 527 N GLU I 448
SHEET 11 X11 GLN I 534 GLN I 537 -1 O GLN I 534 N GLN I 528
SHEET 1 Y 3 VAL J 25 THR J 28 0
SHEET 2 Y 3 GLY J 31 LEU J 34 -1 O VAL J 33 N VAL J 26
SHEET 3 Y 3 VAL J 77 ASN J 79 1 O LYS J 78 N LYS J 32
SHEET 1 Z11 LYS J 36 VAL J 38 0
SHEET 2 Z11 VAL J 47 PRO J 54 -1 O ILE J 49 N LYS J 36
SHEET 3 Z11 TYR J 118 THR J 123 -1 O ILE J 121 N PHE J 50
SHEET 4 Z11 VAL J 164 ILE J 168 -1 O THR J 167 N ASN J 120
SHEET 5 Z11 LEU J 133 ILE J 139 1 N TRP J 138 O VAL J 166
SHEET 6 Z11 GLY J 210 GLU J 220 1 O ASN J 211 N LEU J 133
SHEET 7 Z11 ARG J 242 GLU J 246 1 O GLU J 246 N GLY J 219
SHEET 8 Z11 TYR J 346 ASN J 351 1 O MET J 347 N ALA J 243
SHEET 9 Z11 THR J 444 PHE J 449 1 O PHE J 449 N ILE J 350
SHEET 10 Z11 GLY J 525 GLN J 528 1 O LEU J 527 N MET J 446
SHEET 11 Z11 GLN J 534 GLN J 537 -1 O GLN J 534 N GLN J 528
SHEET 1 AA 3 VAL K 25 ASP K 27 0
SHEET 2 AA 3 LYS K 32 LEU K 34 -1 O VAL K 33 N VAL K 26
SHEET 3 AA 3 VAL K 77 ASN K 79 1 O LYS K 78 N LYS K 32
SHEET 1 AB11 LYS K 36 VAL K 38 0
SHEET 2 AB11 VAL K 47 PRO K 54 -1 O VAL K 47 N VAL K 38
SHEET 3 AB11 TYR K 118 THR K 123 -1 O ILE K 121 N PHE K 50
SHEET 4 AB11 VAL K 164 ILE K 168 -1 O VAL K 165 N TYR K 122
SHEET 5 AB11 LEU K 133 ILE K 139 1 N TRP K 138 O VAL K 166
SHEET 6 AB11 GLY K 210 GLU K 220 1 O THR K 216 N VAL K 135
SHEET 7 AB11 ARG K 242 GLU K 246 1 O GLU K 246 N GLY K 219
SHEET 8 AB11 TYR K 346 ASN K 351 1 O MET K 347 N SER K 245
SHEET 9 AB11 THR K 444 GLN K 450 1 O TYR K 447 N ILE K 350
SHEET 10 AB11 GLY K 525 GLY K 530 1 O LEU K 527 N GLU K 448
SHEET 11 AB11 GLN K 534 GLN K 537 -1 O GLN K 534 N GLN K 528
SHEET 1 AC 2 MET K 86 CYS K 87 0
SHEET 2 AC 2 LEU K 112 SER K 113 1 O SER K 113 N MET K 86
SHEET 1 AD 3 VAL L 25 THR L 28 0
SHEET 2 AD 3 GLY L 31 LEU L 34 -1 O VAL L 33 N VAL L 26
SHEET 3 AD 3 VAL L 77 ASN L 79 1 O LYS L 78 N LYS L 32
SHEET 1 AE11 LYS L 36 VAL L 38 0
SHEET 2 AE11 VAL L 47 LEU L 51 -1 O VAL L 47 N VAL L 38
SHEET 3 AE11 LEU L 119 THR L 123 -1 O ILE L 121 N PHE L 50
SHEET 4 AE11 VAL L 164 ILE L 168 -1 O THR L 167 N ASN L 120
SHEET 5 AE11 LEU L 133 ILE L 139 1 N TRP L 138 O VAL L 166
SHEET 6 AE11 GLY L 210 GLU L 220 1 O ASN L 211 N LEU L 133
SHEET 7 AE11 ARG L 242 GLU L 246 1 O GLU L 246 N GLY L 219
SHEET 8 AE11 TYR L 346 ASN L 351 1 O MET L 347 N SER L 245
SHEET 9 AE11 THR L 444 GLN L 450 1 O TYR L 445 N VAL L 348
SHEET 10 AE11 GLY L 525 GLY L 530 1 O LEU L 527 N MET L 446
SHEET 11 AE11 GLN L 534 GLN L 537 -1 O ALA L 536 N TYR L 526
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
SSBOND 7 CYS D 87 CYS D 116
SSBOND 8 CYS D 274 CYS D 285
SSBOND 9 CYS E 87 CYS E 116
SSBOND 10 CYS E 274 CYS E 285
SSBOND 11 CYS F 87 CYS F 116
SSBOND 12 CYS F 274 CYS F 285
SSBOND 13 CYS G 87 CYS G 116
SSBOND 14 CYS G 274 CYS G 285
SSBOND 15 CYS H 87 CYS H 116
SSBOND 16 CYS H 274 CYS H 285
SSBOND 17 CYS I 87 CYS I 116
SSBOND 18 CYS I 274 CYS I 285
SSBOND 19 CYS J 87 CYS J 116
SSBOND 20 CYS J 274 CYS J 285
SSBOND 21 CYS K 87 CYS K 116
SSBOND 22 CYS K 274 CYS K 285
SSBOND 23 CYS L 87 CYS L 116
SSBOND 24 CYS L 274 CYS L 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
LINK ND2 ASN D 79 C1 NAG D2179
LINK ND2 ASN E 79 C1 NAG E2279
LINK ND2 ASN F 79 C1 NAG F2379
LINK ND2 ASN G 79 C1 NAG G3179
LINK ND2 ASN H 79 C1 NAG H3279
LINK ND2 ASN I 79 C1 NAG I3379
LINK ND2 ASN J 79 C1 NAG J4179
LINK ND2 ASN K 79 C1 NAG K4279
LINK ND2 ASN L 79 C1 NAG L4379
LINK OG SER C 221 C BEZ C5013
LINK OG SER J 221 C BEZ J5041
LINK OG SER F 221 C BEZ F5023
CRYST1 54.560 181.493 202.712 90.12 89.93 89.72 P 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 0.018328 -0.000090 -0.000023 0.00000
SCALE2 0.000000 0.005510 0.000012 0.00000
SCALE3 0.000000 0.000000 0.004933 0.00000
TER 4131 LYS A 553
TER 8263 LYS B 553
TER 12395 LYS C 553
TER 16526 LYS D 553
TER 20658 LYS E 553
TER 24790 LYS F 553
TER 28921 LYS G 553
TER 33051 LYS H 553
TER 37183 LYS I 553
TER 41315 LYS J 553
TER 45446 LYS K 553
TER 49578 LYS L 553
MASTER 468 0 72 279 180 0 0 650793 12 816 492
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