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HEADER HYDROLASE 02-JUN-06 2H7C
TITLE CRYSTAL STRUCTURE OF HUMAN CARBOXYLESTERASE IN COMPLEX WITH
TITLE 2 COENZYME A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: RESIDUES 19-561;
COMPND 5 SYNONYM: ACYL COENZYME A:CHOLESTEROL ACYLTRANSFERASE, ACAT,
COMPND 6 MONOCYTE/MACROPHAGE SERINE ESTERASE, HMSE, SERINE ESTERASE
COMPND 7 1, BRAIN CARBOXYLESTERASE HBR1, TRIACYLGLYCEROL HYDROLASE,
COMPND 8 TGH, EGASYN;
COMPND 9 EC: 3.1.1.1;
COMPND 10 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: SF9;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS ENZYME, ESTERASE, CHOLESTERYL ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BENCHARIT,C.C.EDWARDS,C.L.MORTON,E.L.HOWARD-WILLIAMS,
AUTHOR 2 P.M.POTTER,M.R.REDINBO
REVDAT 1 29-AUG-06 2H7C 0
JRNL AUTH S.BENCHARIT,C.C.EDWARDS,C.L.MORTON,
JRNL AUTH 2 E.L.HOWARD-WILLIAMS,P.M.POTTER,M.R.REDINBO
JRNL TITL MULTISITE PROMISCUITY ENABLES HUMAN
JRNL TITL 2 CARBOXYLESTERASE 1 TO METABOLIZE A VARIETY OF
JRNL TITL 3 ENDOGENOUS SUBSTRATES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3374696.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 232335
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) : 0.183
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11633
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 33146
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1771
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 : 24761
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 502
REMARK 3 SOLVENT ATOMS : 2715
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.51000
REMARK 3 B22 (A**2) : -3.19000
REMARK 3 B33 (A**2) : 4.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.360 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.090 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.170 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.250 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 48.20
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 : COA.PARAM
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 : COA.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H7C COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUN-2006.
REMARK 100 THE RCSB ID CODE IS RCSB038020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-2001
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : MOSFLM
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 233023
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33500
REMARK 200 FOR SHELL : 2.900
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 1MX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, 0.4M LI2SO4, 0.1M
REMARK 280 NACL, 0.1M LICL, 0.1M CITRATE (PH 5.5), 5% GLYCEROL, PH 5.6,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 57.68500
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 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, G, H
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 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 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 HIS D 4019
REMARK 465 PRO D 4020
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 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 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 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 GLU A1099 CG CD OE1 OE2
REMARK 470 GLU B2099 CG CD OE1 OE2
REMARK 470 ILE B2108 CD1
REMARK 470 LYS B2111 CD CE NZ
REMARK 470 LYS B2237 CG CD CE NZ
REMARK 470 LYS B2257 CG CD CE NZ
REMARK 470 LYS B2258 CG CD CE NZ
REMARK 470 GLU B2292 CD OE1 OE2
REMARK 470 GLU B2314 CD OE1 OE2
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 VAL A1389 C CYS A1390 N 0.057
REMARK 500 CYS A1390 C ILE A1391 N -0.225
REMARK 500 MET A1425 SD MET A1425 CE -0.054
REMARK 500 VAL B2389 C CYS B2390 N 0.230
REMARK 500 CYS B2390 C ILE B2391 N -0.061
REMARK 500 MET B2446 SD MET B2446 CE 0.051
REMARK 500 GLU C3106 CB GLU C3106 CG 0.053
REMARK 500 VAL C3389 C CYS C3390 N 0.250
REMARK 500 CYS C3390 C ILE C3391 N 0.074
REMARK 500 MET D4145 SD MET D4145 CE 0.043
REMARK 500 VAL D4389 C CYS D4390 N 0.283
REMARK 500 CYS D4390 C ILE D4391 N -0.108
REMARK 500 VAL E5389 C CYS E5390 N -0.047
REMARK 500 MET E5446 SD MET E5446 CE 0.043
REMARK 500 VAL F6389 C CYS F6390 N 0.128
REMARK 500 CYS F6390 C ILE F6391 N 0.213
REMARK 500 MET F6446 SD MET F6446 CE 0.041
REMARK 500 MET F6497 SD MET F6497 CE 0.051
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 ASP A1115 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP A1126 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 PHE A1177 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASN A1204 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 THR A1252 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 SER A1253 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 LEU A1319 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 GLY A1320 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 CYS A1390 CA - C - N ANGL. DEV. = 8.1 DEGREES
REMARK 500 CYS A1390 O - C - N ANGL. DEV. = -8.6 DEGREES
REMARK 500 GLY A1441 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU A1448 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 GLY A1484 N - CA - C ANGL. DEV. = 11.4 DEGREES
REMARK 500 ASN A1506 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASN A1508 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLN A1528 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 MET B2086 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP B2115 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 PHE B2177 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASN B2204 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 LYS B2237 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 THR B2252 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 SER B2253 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 LEU B2319 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 LEU B2368 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 CYS B2390 C - N - CA ANGL. DEV. = -9.7 DEGREES
REMARK 500 CYS B2390 CA - C - N ANGL. DEV. = 7.7 DEGREES
REMARK 500 CYS B2390 O - C - N ANGL. DEV. = -8.3 DEGREES
REMARK 500 LEU B2420 CA - CB - CG ANGL. DEV. = 9.0 DEGREES
REMARK 500 GLU B2448 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 GLY B2484 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASN B2508 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 GLN B2528 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ASP C3115 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 PHE C3177 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASN C3204 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 LYS C3237 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 THR C3252 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 SER C3253 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 LEU C3319 N - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 ILE C3323 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP C3324 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 LEU C3420 CA - CB - CG ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLY C3484 N - CA - C ANGL. DEV. = 10.2 DEGREES
REMARK 500 ASN C3508 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLN C3528 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP D4090 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP D4115 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 ASP D4126 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 GLU D4161 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 PHE D4177 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASN D4204 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 THR D4252 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 SER D4253 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 LEU D4319 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 ILE D4323 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP D4374 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 CYS D4390 C - N - CA ANGL. DEV. = -8.8 DEGREES
REMARK 500 CYS D4390 CA - C - N ANGL. DEV. = 9.0 DEGREES
REMARK 500 CYS D4390 O - C - N ANGL. DEV. =-15.7 DEGREES
REMARK 500 LEU D4420 CA - CB - CG ANGL. DEV. = 12.0 DEGREES
REMARK 500 GLU D4448 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASN D4506 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASN D4508 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASN D4510 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 GLN D4528 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASP E5115 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 PHE E5177 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASN E5204 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 THR E5252 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 SER E5253 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 LEU E5319 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ILE E5323 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 THR E5343 N - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 VAL E5389 CA - C - N ANGL. DEV. = 8.4 DEGREES
REMARK 500 VAL E5389 O - C - N ANGL. DEV. = -8.1 DEGREES
REMARK 500 CYS E5390 C - N - CA ANGL. DEV. = 15.5 DEGREES
REMARK 500 GLU E5448 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASN E5506 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASN E5508 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLN E5528 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASP F6115 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP F6126 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 PHE F6177 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 THR F6252 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 SER F6253 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 LEU F6319 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 GLY F6320 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 CYS F6390 CA - C - N ANGL. DEV. = -9.0 DEGREES
REMARK 500 GLU F6448 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASN F6508 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLN F6528 N - CA - C ANGL. DEV. = -8.1 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 D4221 -119.44 59.93
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 7883 DISTANCE = 6.00 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MX1 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH TACRINE.
REMARK 900 RELATED ID: 1MX5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH COCAINE ANALOG, HOMATROPINE.
REMARK 900 RELATED ID: 1MX9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH HEROIN ANALOG, NALOXONE.
REMARK 900 RELATED ID: 1YA4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH TAMOXIFEN.
REMARK 900 RELATED ID: 1YA8 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PRODUCT OF MEVASTATIN.
REMARK 900 RELATED ID: 1YAH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ETHYL ACETATE
REMARK 900 RELATED ID: 2DQY RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CHOLATE AND PALMITATE
REMARK 900 RELATED ID: 2DQZ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH HOMATROPINE, COENZYME A,
REMARK 900 AND PALMITATE
REMARK 900 RELATED ID: 2DR0 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH TAUROCHOLATE
DBREF 2H7C A 1019 1561 UNP P23141 EST1_HUMAN 19 561
DBREF 2H7C B 2019 2561 UNP P23141 EST1_HUMAN 19 561
DBREF 2H7C C 3019 3561 UNP P23141 EST1_HUMAN 19 561
DBREF 2H7C D 4019 4561 UNP P23141 EST1_HUMAN 19 561
DBREF 2H7C E 5019 5561 UNP P23141 EST1_HUMAN 19 561
DBREF 2H7C F 6019 6561 UNP P23141 EST1_HUMAN 19 561
SEQADV 2H7C A UNP P23141 GLN 362 DELETION
SEQADV 2H7C B UNP P23141 GLN 362 DELETION
SEQADV 2H7C C UNP P23141 GLN 362 DELETION
SEQADV 2H7C D UNP P23141 GLN 362 DELETION
SEQADV 2H7C E UNP P23141 GLN 362 DELETION
SEQADV 2H7C F UNP P23141 GLN 362 DELETION
SEQRES 1 A 542 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 A 542 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 A 542 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 A 542 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 A 542 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 A 542 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 A 542 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 A 542 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 A 542 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 A 542 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 A 542 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 A 542 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 A 542 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 A 542 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 A 542 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 A 542 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 A 542 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 A 542 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 A 542 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 A 542 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 A 542 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 A 542 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 A 542 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 A 542 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 A 542 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 A 542 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 A 542 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 A 542 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 A 542 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 A 542 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 A 542 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 A 542 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 A 542 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 A 542 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 A 542 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 A 542 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 A 542 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 A 542 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 A 542 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 A 542 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 A 542 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 A 542 LYS LYS ALA VAL GLU LYS PRO PRO GLN
SEQRES 1 B 542 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 B 542 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 B 542 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 B 542 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 B 542 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 B 542 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 B 542 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 B 542 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 B 542 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 B 542 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 B 542 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 B 542 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 B 542 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 B 542 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 B 542 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 B 542 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 B 542 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 B 542 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 B 542 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 B 542 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 B 542 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 B 542 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 B 542 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 B 542 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 B 542 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 B 542 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 B 542 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 B 542 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 B 542 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 B 542 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 B 542 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 B 542 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 B 542 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 B 542 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 B 542 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 B 542 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 B 542 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 B 542 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 B 542 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 B 542 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 B 542 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 B 542 LYS LYS ALA VAL GLU LYS PRO PRO GLN
SEQRES 1 C 542 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 C 542 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 C 542 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 C 542 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 C 542 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 C 542 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 C 542 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 C 542 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 C 542 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 C 542 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 C 542 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 C 542 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 C 542 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 C 542 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 C 542 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 C 542 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 C 542 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 C 542 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 C 542 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 C 542 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 C 542 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 C 542 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 C 542 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 C 542 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 C 542 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 C 542 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 C 542 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 C 542 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 C 542 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 C 542 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 C 542 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 C 542 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 C 542 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 C 542 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 C 542 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 C 542 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 C 542 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 C 542 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 C 542 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 C 542 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 C 542 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 C 542 LYS LYS ALA VAL GLU LYS PRO PRO GLN
SEQRES 1 D 542 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 D 542 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 D 542 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 D 542 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 D 542 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 D 542 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 D 542 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 D 542 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 D 542 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 D 542 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 D 542 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 D 542 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 D 542 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 D 542 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 D 542 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 D 542 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 D 542 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 D 542 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 D 542 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 D 542 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 D 542 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 D 542 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 D 542 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 D 542 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 D 542 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 D 542 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 D 542 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 D 542 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 D 542 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 D 542 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 D 542 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 D 542 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 D 542 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 D 542 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 D 542 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 D 542 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 D 542 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 D 542 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 D 542 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 D 542 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 D 542 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 D 542 LYS LYS ALA VAL GLU LYS PRO PRO GLN
SEQRES 1 E 542 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 E 542 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 E 542 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 E 542 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 E 542 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 E 542 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 E 542 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 E 542 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 E 542 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 E 542 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 E 542 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 E 542 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 E 542 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 E 542 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 E 542 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 E 542 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 E 542 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 E 542 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 E 542 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 E 542 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 E 542 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 E 542 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 E 542 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 E 542 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 E 542 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 E 542 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 E 542 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 E 542 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 E 542 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 E 542 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 E 542 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 E 542 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 E 542 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 E 542 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 E 542 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 E 542 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 E 542 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 E 542 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 E 542 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 E 542 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 E 542 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 E 542 LYS LYS ALA VAL GLU LYS PRO PRO GLN
SEQRES 1 F 542 HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES 2 F 542 LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES 3 F 542 GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES 4 F 542 PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES 5 F 542 ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES 6 F 542 PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES 7 F 542 LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES 8 F 542 LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 9 F 542 THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES 10 F 542 MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES 11 F 542 ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES 12 F 542 ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES 13 F 542 TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES 14 F 542 ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES 15 F 542 VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES 16 F 542 SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES 17 F 542 VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES 18 F 542 PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES 19 F 542 SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES 20 F 542 GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES 21 F 542 SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES 22 F 542 GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES 23 F 542 SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES 24 F 542 LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES 25 F 542 THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES 26 F 542 VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 F 542 TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES 28 F 542 GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES 29 F 542 LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES 30 F 542 PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 F 542 THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES 32 F 542 ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES 33 F 542 ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 F 542 PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES 35 F 542 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES 36 F 542 VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES 37 F 542 GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES 38 F 542 ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 F 542 LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES 40 F 542 LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES 41 F 542 LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES 42 F 542 LYS LYS ALA VAL GLU LYS PRO PRO GLN
MODRES 2H7C ASN A 1079 ASN GLYCOSYLATION SITE
MODRES 2H7C ASN B 2079 ASN GLYCOSYLATION SITE
MODRES 2H7C ASN C 3079 ASN GLYCOSYLATION SITE
MODRES 2H7C ASN D 4079 ASN GLYCOSYLATION SITE
MODRES 2H7C ASN E 5079 ASN GLYCOSYLATION SITE
MODRES 2H7C ASN F 6079 ASN GLYCOSYLATION SITE
HET NAG G 179 14
HET NAG G 180 14
HET NAG B 279 14
HET NAG C 379 14
HET NAG D 479 14
HET SIA 482 21
HET NAG E 579 14
HET SIA 582 21
HET NAG H 679 14
HET NAG H 680 14
HET SO4 184 5
HET SO4 185 5
HET SO4 284 5
HET SO4 285 5
HET SO4 384 5
HET SO4 385 5
HET SO4 484 5
HET SO4 485 5
HET SO4 584 5
HET SO4 585 5
HET SO4 684 5
HET SO4 685 5
HET COA 1 48
HET COA 2 48
HET COA 3 48
HET COA 4 48
HET COA 5 48
HET COA 6 48
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SIA O-SIALIC ACID
HETNAM SO4 SULFATE ION
HETNAM COA COENZYME A
HETSYN NAG NAG
FORMUL 7 NAG 8(C8 H15 N1 O6)
FORMUL 11 SIA 2(C11 H19 N1 O9)
FORMUL 15 SO4 12(O4 S1 2-)
FORMUL 27 COA 6(C21 H36 N7 O16 P3 S1)
FORMUL 33 HOH *2715(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 SER A 1233 1 13
HELIX 8 8 PRO A 1234 LYS A 1237 5 4
HELIX 9 9 THR A 1252 VAL A 1256 5 5
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 GLN A 1336 1 6
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 ALA A 1392 GLU A 1394 5 3
HELIX 19 19 LEU A 1395 GLY A 1405 1 11
HELIX 20 20 ASP A 1409 PHE A 1426 1 18
HELIX 21 21 PHE A 1426 ALA A 1440 1 15
HELIX 22 22 GLU A 1471 PHE A 1476 1 6
HELIX 23 23 GLY A 1477 LEU A 1481 5 5
HELIX 24 24 SER A 1486 GLY A 1507 1 22
HELIX 25 25 LYS A 1540 LYS A 1553 1 14
HELIX 26 26 LEU B 2060 ARG B 2064 5 5
HELIX 27 27 ASP B 2090 THR B 2102 1 13
HELIX 28 28 ALA B 2148 TYR B 2152 5 5
HELIX 29 29 GLY B 2154 ASN B 2162 1 9
HELIX 30 30 LEU B 2172 PHE B 2178 1 7
HELIX 31 31 ASN B 2188 ILE B 2205 1 18
HELIX 32 32 ALA B 2206 PHE B 2208 5 3
HELIX 33 33 SER B 2221 LEU B 2232 1 12
HELIX 34 34 SER B 2233 LYS B 2237 5 5
HELIX 35 35 THR B 2252 VAL B 2254 5 3
HELIX 36 36 VAL B 2261 GLY B 2273 1 13
HELIX 37 37 THR B 2278 LYS B 2289 1 12
HELIX 38 38 THR B 2290 LYS B 2302 1 13
HELIX 39 39 ASP B 2311 SER B 2315 5 5
HELIX 40 40 THR B 2331 GLU B 2338 1 8
HELIX 41 41 TRP B 2357 MET B 2364 1 7
HELIX 42 42 ASP B 2374 SER B 2385 1 12
HELIX 43 43 SER B 2385 CYS B 2390 1 6
HELIX 44 44 ALA B 2392 GLU B 2394 5 3
HELIX 45 45 LEU B 2395 GLY B 2405 1 11
HELIX 46 46 ASP B 2409 PHE B 2426 1 18
HELIX 47 47 PHE B 2426 ALA B 2440 1 15
HELIX 48 48 GLU B 2471 PHE B 2476 1 6
HELIX 49 49 GLY B 2477 LEU B 2481 5 5
HELIX 50 50 SER B 2486 GLY B 2507 1 22
HELIX 51 51 LYS B 2540 PHE B 2551 1 12
HELIX 52 52 LEU C 3060 ARG C 3064 5 5
HELIX 53 53 ASP C 3090 THR C 3102 1 13
HELIX 54 54 GLY C 3154 ASN C 3162 1 9
HELIX 55 55 LEU C 3172 PHE C 3178 1 7
HELIX 56 56 ASN C 3188 ILE C 3205 1 18
HELIX 57 57 ALA C 3206 PHE C 3208 5 3
HELIX 58 58 SER C 3221 SER C 3233 1 13
HELIX 59 59 PRO C 3234 LYS C 3237 5 4
HELIX 60 60 THR C 3252 VAL C 3256 5 5
HELIX 61 61 VAL C 3261 ALA C 3272 1 12
HELIX 62 62 THR C 3278 LYS C 3289 1 12
HELIX 63 63 THR C 3290 LYS C 3302 1 13
HELIX 64 64 ASP C 3311 SER C 3315 5 5
HELIX 65 65 THR C 3331 GLU C 3338 1 8
HELIX 66 66 TRP C 3357 MET C 3364 1 7
HELIX 67 67 ASP C 3374 SER C 3385 1 12
HELIX 68 68 SER C 3385 CYS C 3390 1 6
HELIX 69 69 ALA C 3392 GLU C 3394 5 3
HELIX 70 70 LEU C 3395 GLY C 3405 1 11
HELIX 71 71 ASP C 3409 PHE C 3426 1 18
HELIX 72 72 PHE C 3426 ASP C 3439 1 14
HELIX 73 73 GLU C 3471 PHE C 3476 1 6
HELIX 74 74 GLY C 3477 LEU C 3481 5 5
HELIX 75 75 SER C 3486 GLY C 3507 1 22
HELIX 76 76 LYS C 3540 LYS C 3553 1 14
HELIX 77 77 LEU D 4060 ARG D 4064 5 5
HELIX 78 78 ASP D 4090 THR D 4102 1 13
HELIX 79 79 GLY D 4154 ASN D 4162 1 9
HELIX 80 80 LEU D 4172 PHE D 4178 1 7
HELIX 81 81 ASN D 4188 ILE D 4205 1 18
HELIX 82 82 ALA D 4206 PHE D 4208 5 3
HELIX 83 83 SER D 4221 LEU D 4232 1 12
HELIX 84 84 SER D 4233 LYS D 4237 5 5
HELIX 85 85 THR D 4252 VAL D 4256 5 5
HELIX 86 86 VAL D 4261 ALA D 4272 1 12
HELIX 87 87 THR D 4278 LYS D 4289 1 12
HELIX 88 88 THR D 4290 LYS D 4302 1 13
HELIX 89 89 ASP D 4311 SER D 4315 5 5
HELIX 90 90 THR D 4331 ARG D 4339 1 9
HELIX 91 91 TRP D 4357 MET D 4364 1 7
HELIX 92 92 ASP D 4374 SER D 4385 1 12
HELIX 93 93 SER D 4385 CYS D 4390 1 6
HELIX 94 94 LEU D 4395 LEU D 4404 1 10
HELIX 95 95 ASP D 4409 PHE D 4426 1 18
HELIX 96 96 PHE D 4426 ALA D 4440 1 15
HELIX 97 97 GLU D 4471 PHE D 4476 1 6
HELIX 98 98 GLY D 4477 LEU D 4481 5 5
HELIX 99 99 SER D 4486 GLY D 4507 1 22
HELIX 100 100 LYS D 4540 LYS D 4553 1 14
HELIX 101 101 LEU E 5060 ARG E 5064 5 5
HELIX 102 102 ASP E 5090 THR E 5102 1 13
HELIX 103 103 GLY E 5154 ASN E 5162 1 9
HELIX 104 104 LEU E 5172 PHE E 5178 1 7
HELIX 105 105 ASN E 5188 ILE E 5205 1 18
HELIX 106 106 ALA E 5206 PHE E 5208 5 3
HELIX 107 107 SER E 5221 SER E 5233 1 13
HELIX 108 108 PRO E 5234 LYS E 5237 5 4
HELIX 109 109 THR E 5252 VAL E 5254 5 3
HELIX 110 110 VAL E 5261 ALA E 5272 1 12
HELIX 111 111 THR E 5278 LYS E 5289 1 12
HELIX 112 112 THR E 5290 LYS E 5302 1 13
HELIX 113 113 ASP E 5311 SER E 5315 5 5
HELIX 114 114 THR E 5331 GLU E 5338 1 8
HELIX 115 115 TRP E 5357 MET E 5364 1 7
HELIX 116 116 ASP E 5374 SER E 5385 1 12
HELIX 117 117 SER E 5385 CYS E 5390 1 6
HELIX 118 118 ALA E 5392 GLU E 5394 5 3
HELIX 119 119 LEU E 5395 GLY E 5405 1 11
HELIX 120 120 ASP E 5409 PHE E 5426 1 18
HELIX 121 121 PHE E 5426 ASP E 5439 1 14
HELIX 122 122 GLU E 5471 PHE E 5476 1 6
HELIX 123 123 GLY E 5477 LEU E 5481 5 5
HELIX 124 124 SER E 5486 GLY E 5507 1 22
HELIX 125 125 LYS E 5540 ALA E 5552 1 13
HELIX 126 126 LEU F 6060 ARG F 6064 5 5
HELIX 127 127 ASP F 6090 THR F 6102 1 13
HELIX 128 128 GLY F 6154 ASN F 6162 1 9
HELIX 129 129 LEU F 6172 PHE F 6178 1 7
HELIX 130 130 ASN F 6188 ILE F 6205 1 18
HELIX 131 131 ALA F 6206 PHE F 6208 5 3
HELIX 132 132 SER F 6221 LEU F 6232 1 12
HELIX 133 133 SER F 6233 LYS F 6237 5 5
HELIX 134 134 THR F 6252 VAL F 6254 5 3
HELIX 135 135 VAL F 6261 GLY F 6273 1 13
HELIX 136 136 THR F 6278 LYS F 6289 1 12
HELIX 137 137 THR F 6290 LYS F 6302 1 13
HELIX 138 138 ASP F 6311 SER F 6315 5 5
HELIX 139 139 THR F 6331 GLU F 6338 1 8
HELIX 140 140 TRP F 6357 MET F 6364 1 7
HELIX 141 141 ASP F 6374 SER F 6385 1 12
HELIX 142 142 SER F 6385 CYS F 6390 1 6
HELIX 143 143 ALA F 6392 GLU F 6394 5 3
HELIX 144 144 LEU F 6395 GLY F 6405 1 11
HELIX 145 145 VAL F 6411 PHE F 6426 1 16
HELIX 146 146 PHE F 6426 ASP F 6439 1 14
HELIX 147 147 GLU F 6471 PHE F 6476 1 6
HELIX 148 148 GLY F 6477 LEU F 6481 5 5
HELIX 149 149 SER F 6486 GLY F 6507 1 22
HELIX 150 150 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 MET A1136 O VAL A1164
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 3 VAL B2025 THR B2028 0
SHEET 2 D 3 GLY B2031 LEU B2034 -1 O VAL B2033 N VAL B2026
SHEET 3 D 3 VAL B2077 ASN B2079 1 O LYS B2078 N LEU B2034
SHEET 1 E11 LYS B2036 VAL B2038 0
SHEET 2 E11 VAL B2047 PRO B2054 -1 O ILE B2049 N LYS B2036
SHEET 3 E11 TYR B2118 THR B2123 -1 O ILE B2121 N PHE B2050
SHEET 4 E11 VAL B2164 ILE B2168 -1 O VAL B2165 N TYR B2122
SHEET 5 E11 LEU B2133 ILE B2139 1 N MET B2136 O VAL B2164
SHEET 6 E11 GLY B2210 GLU B2220 1 O THR B2216 N VAL B2135
SHEET 7 E11 ARG B2242 GLU B2246 1 O GLU B2246 N GLY B2219
SHEET 8 E11 TYR B2346 ASN B2351 1 O MET B2347 N ALA B2243
SHEET 9 E11 THR B2444 PHE B2449 1 O TYR B2445 N VAL B2348
SHEET 10 E11 GLY B2525 ILE B2529 1 O LEU B2527 N GLU B2448
SHEET 11 E11 GLN B2534 GLN B2537 -1 O GLN B2534 N GLN B2528
SHEET 1 F 2 MET B2086 CYS B2087 0
SHEET 2 F 2 LEU B2112 SER B2113 1 O SER B2113 N MET B2086
SHEET 1 G 2 VAL B2256 LYS B2257 0
SHEET 2 G 2 THR B2321 VAL B2322 1 O THR B2321 N LYS B2257
SHEET 1 H 3 VAL C3025 THR C3028 0
SHEET 2 H 3 GLY C3031 LEU C3034 -1 O VAL C3033 N VAL C3026
SHEET 3 H 3 VAL C3077 ASN C3079 1 O LYS C3078 N LYS C3032
SHEET 1 I11 LYS C3036 VAL C3038 0
SHEET 2 I11 VAL C3047 PRO C3054 -1 O ILE C3049 N LYS C3036
SHEET 3 I11 TYR C3118 THR C3123 -1 O ILE C3121 N PHE C3050
SHEET 4 I11 VAL C3164 ILE C3168 -1 O VAL C3165 N TYR C3122
SHEET 5 I11 LEU C3133 ILE C3139 1 N TRP C3138 O VAL C3166
SHEET 6 I11 GLY C3210 GLU C3220 1 O THR C3216 N VAL C3135
SHEET 7 I11 ARG C3242 GLU C3246 1 O GLU C3246 N GLY C3219
SHEET 8 I11 TYR C3346 ASN C3351 1 O MET C3347 N ALA C3243
SHEET 9 I11 THR C3444 PHE C3449 1 O TYR C3445 N VAL C3348
SHEET 10 I11 GLY C3525 ILE C3529 1 O LEU C3527 N MET C3446
SHEET 11 I11 GLN C3534 GLN C3537 -1 O ALA C3536 N TYR C3526
SHEET 1 J 2 MET C3086 CYS C3087 0
SHEET 2 J 2 LEU C3112 SER C3113 1 O SER C3113 N MET C3086
SHEET 1 K 3 VAL D4025 THR D4028 0
SHEET 2 K 3 GLY D4031 LEU D4034 -1 O VAL D4033 N VAL D4026
SHEET 3 K 3 VAL D4077 ASN D4079 1 O LYS D4078 N LEU D4034
SHEET 1 L11 LYS D4036 VAL D4038 0
SHEET 2 L11 VAL D4047 PRO D4054 -1 O VAL D4047 N VAL D4038
SHEET 3 L11 TYR D4118 THR D4123 -1 O ILE D4121 N PHE D4050
SHEET 4 L11 VAL D4164 ILE D4168 -1 O VAL D4165 N TYR D4122
SHEET 5 L11 LEU D4133 ILE D4139 1 N TRP D4138 O VAL D4166
SHEET 6 L11 GLY D4210 GLU D4220 1 O THR D4216 N VAL D4135
SHEET 7 L11 ARG D4242 GLU D4246 1 O GLU D4246 N GLY D4219
SHEET 8 L11 TYR D4346 ASN D4351 1 O MET D4347 N ALA D4243
SHEET 9 L11 THR D4444 GLN D4450 1 O TYR D4445 N VAL D4348
SHEET 10 L11 GLY D4525 GLY D4530 1 O ILE D4529 N GLN D4450
SHEET 11 L11 GLN D4534 GLN D4537 -1 O GLN D4534 N GLN D4528
SHEET 1 M 2 MET D4086 CYS D4087 0
SHEET 2 M 2 LEU D4112 SER D4113 1 O SER D4113 N MET D4086
SHEET 1 N 3 VAL E5025 THR E5028 0
SHEET 2 N 3 GLY E5031 LEU E5034 -1 O VAL E5033 N VAL E5026
SHEET 3 N 3 VAL E5077 ASN E5079 1 O LYS E5078 N LYS E5032
SHEET 1 O11 LYS E5036 VAL E5038 0
SHEET 2 O11 VAL E5047 PRO E5054 -1 O ILE E5049 N LYS E5036
SHEET 3 O11 TYR E5118 THR E5123 -1 O ILE E5121 N PHE E5050
SHEET 4 O11 VAL E5164 ILE E5168 -1 O VAL E5165 N TYR E5122
SHEET 5 O11 LEU E5133 ILE E5139 1 N TRP E5138 O VAL E5166
SHEET 6 O11 GLY E5210 GLU E5220 1 O THR E5216 N VAL E5137
SHEET 7 O11 ARG E5242 GLU E5246 1 O GLU E5246 N GLY E5219
SHEET 8 O11 TYR E5346 ASN E5351 1 O MET E5347 N ALA E5243
SHEET 9 O11 THR E5444 GLN E5450 1 O TYR E5445 N VAL E5348
SHEET 10 O11 GLY E5525 GLY E5530 1 O ILE E5529 N GLN E5450
SHEET 11 O11 GLN E5534 GLN E5537 -1 O GLN E5534 N GLN E5528
SHEET 1 P 2 MET E5086 CYS E5087 0
SHEET 2 P 2 LEU E5112 SER E5113 1 O SER E5113 N MET E5086
SHEET 1 Q 2 VAL E5256 LYS E5257 0
SHEET 2 Q 2 THR E5321 VAL E5322 1 O THR E5321 N LYS E5257
SHEET 1 R 3 VAL F6025 THR F6028 0
SHEET 2 R 3 GLY F6031 LEU F6034 -1 O VAL F6033 N VAL F6026
SHEET 3 R 3 VAL F6077 ASN F6079 1 O LYS F6078 N LEU F6034
SHEET 1 S11 LYS F6036 VAL F6038 0
SHEET 2 S11 VAL F6047 PRO F6054 -1 O ILE F6049 N LYS F6036
SHEET 3 S11 TYR F6118 THR F6123 -1 O ILE F6121 N PHE F6050
SHEET 4 S11 VAL F6164 ILE F6168 -1 O VAL F6165 N TYR F6122
SHEET 5 S11 LEU F6133 ILE F6139 1 N TRP F6138 O VAL F6166
SHEET 6 S11 GLY F6210 GLU F6220 1 O THR F6216 N VAL F6135
SHEET 7 S11 ARG F6242 GLU F6246 1 O GLU F6246 N GLY F6219
SHEET 8 S11 TYR F6346 ASN F6351 1 O MET F6347 N ALA F6243
SHEET 9 S11 THR F6444 PHE F6449 1 O TYR F6445 N VAL F6348
SHEET 10 S11 GLY F6525 ILE F6529 1 O LEU F6527 N GLU F6448
SHEET 11 S11 GLN F6534 GLN F6537 -1 O GLN F6534 N GLN F6528
SHEET 1 T 2 MET F6086 CYS F6087 0
SHEET 2 T 2 LEU F6112 SER F6113 1 O SER F6113 N MET F6086
SHEET 1 U 2 VAL F6256 LYS F6257 0
SHEET 2 U 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 G 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 H 679
LINK O4 NAG G 179 C1 NAG G 180
LINK O4 NAG H 679 C1 NAG H 680
CRYST1 88.990 115.370 175.530 90.00 90.05 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 0.011237 0.000000 0.000010 0.00000
SCALE2 0.000000 0.008668 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005697 0.00000
TER 4133 LYS A1553
TER 8238 LYS B2553
TER 12369 LYS C3553
TER 16506 LYS D4553
TER 20637 LYS E5553
TER 24767 LYS F6553
MASTER 480 0 28 150 102 0 0 627978 6 532 252
END |