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HEADER HYDROLASE 02-JUN-06 2DQY
TITLE CRYSTAL STRUCTURE OF HUMAN CARBOXYLESTERASE IN COMPLEX WITH
TITLE 2 CHOLATE AND PALMITATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND 3 CHAIN: A, B, C;
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 CHOLESTEROL METABOLISM, FOAM CELLS, MACROPHAGE, MONOCYTE,
KEYWDS 2 ATHEROSCLEROSIS
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 2DQY 0
JRNL AUTH S.BENCHARIT,C.C.EDWARDS,C.L.MORTON,
JRNL AUTH 2 E.L.HOWARD-WILLIAMS,P.KUHN,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. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2305620.660
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 38284
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) : 0.226
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2693
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5219
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 424
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12390
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 276
REMARK 3 SOLVENT ATOMS : 301
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.01000
REMARK 3 B22 (A**2) : 5.10000
REMARK 3 B33 (A**2) : 0.91000
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) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.47
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) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.57
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.82
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) : 1.150 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.050 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.420 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.330 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 36.79
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 : CHD.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 : CHD.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DQY 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 RCSB025739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-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) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : MOSFLM
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38284
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 13.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11000
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34100
REMARK 200 FOR SHELL : 2.400
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: 1MX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
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 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.64600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.66150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 89.93850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.66150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.64600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 89.93850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 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 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 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 GLN A1069 CB GLN A1069 CG -0.051
REMARK 500 ALA A1206 CA ALA A1206 CB -0.053
REMARK 500 MET A1326 SD MET A1326 CE 0.055
REMARK 500 MET A1364 CG MET A1364 SD -0.059
REMARK 500 MET A1364 SD MET A1364 CE -0.075
REMARK 500 MET A1425 SD MET A1425 CE -0.074
REMARK 500 MET A1459 SD MET A1459 CE 0.114
REMARK 500 GLN B2069 CB GLN B2069 CG -0.054
REMARK 500 MET B2136 SD MET B2136 CE 0.053
REMARK 500 MET B2145 SD MET B2145 CE 0.073
REMARK 500 MET B2326 SD MET B2326 CE 0.073
REMARK 500 MET B2459 SD MET B2459 CE 0.097
REMARK 500 GLN C3069 CB GLN C3069 CG -0.051
REMARK 500 THR C3102 CA THR C3102 CB -0.051
REMARK 500 ARG C3171 CG ARG C3171 CD -0.052
REMARK 500 MET C3425 SD MET C3425 CE -0.053
REMARK 500 MET C3459 SD MET C3459 CE 0.093
REMARK 500 MET C3495 SD MET C3495 CE -0.052
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A1040 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 GLY A1052 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 SER A1305 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU A1318 CA - CB - CG ANGL. DEV. = -9.0 DEGREES
REMARK 500 LEU A1318 N - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 LEU A1319 N - CA - C ANGL. DEV. =-20.8 DEGREES
REMARK 500 LEU A1319 C - N - CA ANGL. DEV. = 7.1 DEGREES
REMARK 500 LEU A1420 CA - CB - CG ANGL. DEV. = 7.2 DEGREES
REMARK 500 LEU B2040 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 GLY B2052 N - CA - C ANGL. DEV. = 7.1 DEGREES
REMARK 500 PRO B2317 C - N - CA ANGL. DEV. = 7.0 DEGREES
REMARK 500 SER B2369 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU B2420 CA - CB - CG ANGL. DEV. = 7.2 DEGREES
REMARK 500 LEU C3040 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 SER C3253 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 LEU C3420 CA - CB - CG 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 C3221 -118.90 55.55
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2H7C RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH COENZYME A
REMARK 900 RELATED ID: 2DQZ RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH HOMATROPINE, COENZYME A, AND
REMARK 900 PALMITATE
REMARK 900 RELATED ID: 2DR0 RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH TAUROCHOLATE
DBREF 2DQY A 1019 1561 UNP P23141 EST1_HUMAN 19 561
DBREF 2DQY B 2019 2561 UNP P23141 EST1_HUMAN 19 561
DBREF 2DQY C 3019 3561 UNP P23141 EST1_HUMAN 19 561
SEQADV 2DQY A UNP P23141 GLN 362 DELETION
SEQADV 2DQY B UNP P23141 GLN 362 DELETION
SEQADV 2DQY C 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
MODRES 2DQY ASN A 1079 ASN GLYCOSYLATION SITE
MODRES 2DQY ASN B 2079 ASN GLYCOSYLATION SITE
MODRES 2DQY ASN C 3079 ASN GLYCOSYLATION SITE
HET NAG A 179 14
HET SIA 182 21
HET NAG B 279 14
HET SIA 282 21
HET NAG C 379 14
HET SIA 382 21
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 CHD 1 29
HET CHD 2 29
HET CHD 3 29
HET PLM 11 18
HET PLM 12 18
HET PLM 13 18
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SIA O-SIALIC ACID
HETNAM SO4 SULFATE ION
HETNAM CHD CHOLIC ACID
HETNAM PLM PALMITIC ACID
HETSYN NAG NAG
FORMUL 4 NAG 3(C8 H15 N1 O6)
FORMUL 5 SIA 3(C11 H19 N1 O9)
FORMUL 10 SO4 6(O4 S1 2-)
FORMUL 16 CHD 3(C24 H40 O5)
FORMUL 19 PLM 3(C16 H32 O2)
FORMUL 22 HOH *301(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 ASP A 1203 1 16
HELIX 6 6 ASN A 1204 PHE A 1208 5 5
HELIX 7 7 SER A 1221 SER A 1233 1 13
HELIX 8 8 THR A 1252 VAL A 1256 5 5
HELIX 9 9 VAL A 1261 ALA A 1272 1 12
HELIX 10 10 THR A 1278 LYS A 1289 1 12
HELIX 11 11 THR A 1290 LYS A 1302 1 13
HELIX 12 12 ASP A 1311 SER A 1315 5 5
HELIX 13 13 THR A 1331 ALA A 1337 1 7
HELIX 14 14 TRP A 1357 MET A 1364 1 7
HELIX 15 15 ASP A 1374 SER A 1385 1 12
HELIX 16 16 SER A 1385 CYS A 1390 1 6
HELIX 17 17 LEU A 1395 GLY A 1405 1 11
HELIX 18 18 ASP A 1409 PHE A 1426 1 18
HELIX 19 19 PHE A 1426 GLY A 1441 1 16
HELIX 20 20 GLU A 1471 PHE A 1476 1 6
HELIX 21 21 GLY A 1477 LEU A 1481 5 5
HELIX 22 22 SER A 1486 GLY A 1507 1 22
HELIX 23 23 LYS A 1540 ALA A 1552 1 13
HELIX 24 24 LEU B 2060 ARG B 2064 5 5
HELIX 25 25 ASP B 2090 THR B 2102 1 13
HELIX 26 26 GLY B 2154 ASN B 2162 1 9
HELIX 27 27 LEU B 2172 PHE B 2178 1 7
HELIX 28 28 ASN B 2188 ILE B 2205 1 18
HELIX 29 29 ALA B 2206 PHE B 2208 5 3
HELIX 30 30 SER B 2221 SER B 2233 1 13
HELIX 31 31 THR B 2252 VAL B 2256 5 5
HELIX 32 32 VAL B 2261 ALA B 2272 1 12
HELIX 33 33 THR B 2278 LYS B 2289 1 12
HELIX 34 34 THR B 2290 MET B 2301 1 12
HELIX 35 35 ASP B 2311 SER B 2315 5 5
HELIX 36 36 THR B 2331 ALA B 2337 1 7
HELIX 37 37 TRP B 2357 MET B 2364 1 7
HELIX 38 38 PRO B 2367 GLY B 2371 5 5
HELIX 39 39 ASP B 2374 SER B 2385 1 12
HELIX 40 40 SER B 2385 CYS B 2390 1 6
HELIX 41 41 LEU B 2395 GLY B 2405 1 11
HELIX 42 42 ASP B 2409 PHE B 2426 1 18
HELIX 43 43 PHE B 2426 GLY B 2441 1 16
HELIX 44 44 GLU B 2471 PHE B 2476 1 6
HELIX 45 45 GLY B 2477 LEU B 2481 5 5
HELIX 46 46 SER B 2486 GLY B 2507 1 22
HELIX 47 47 LYS B 2540 ALA B 2552 1 13
HELIX 48 48 LEU C 3060 ARG C 3064 5 5
HELIX 49 49 ASP C 3090 THR C 3102 1 13
HELIX 50 50 GLY C 3154 ASN C 3162 1 9
HELIX 51 51 LEU C 3172 PHE C 3178 1 7
HELIX 52 52 ASN C 3188 ASP C 3203 1 16
HELIX 53 53 ASN C 3204 PHE C 3208 5 5
HELIX 54 54 SER C 3221 SER C 3233 1 13
HELIX 55 55 THR C 3252 VAL C 3256 5 5
HELIX 56 56 VAL C 3261 ALA C 3272 1 12
HELIX 57 57 THR C 3278 LYS C 3289 1 12
HELIX 58 58 THR C 3290 LYS C 3302 1 13
HELIX 59 59 ASP C 3311 SER C 3315 5 5
HELIX 60 60 THR C 3331 ALA C 3337 1 7
HELIX 61 61 TRP C 3357 SER C 3365 1 8
HELIX 62 62 ASP C 3374 SER C 3385 1 12
HELIX 63 63 SER C 3385 CYS C 3390 1 6
HELIX 64 64 LEU C 3395 GLY C 3405 1 11
HELIX 65 65 ASP C 3409 PHE C 3426 1 18
HELIX 66 66 PHE C 3426 GLY C 3441 1 16
HELIX 67 67 GLU C 3471 PHE C 3476 1 6
HELIX 68 68 GLY C 3477 LEU C 3481 5 5
HELIX 69 69 SER C 3486 GLY C 3507 1 22
HELIX 70 70 LYS C 3540 ALA C 3552 1 13
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 LYS A1078 ASN A1079 1 O LYS A1078 N LEU A1034
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 THR A1123 N ALA A1048
SHEET 4 B11 VAL A1164 ILE A1168 -1 O VAL A1165 N TYR A1122
SHEET 5 B11 LEU A1133 ILE A1139 1 N TRP A1138 O VAL A1166
SHEET 6 B11 GLY A1210 GLU A1220 1 O ASN A1211 N LEU A1133
SHEET 7 B11 ARG A1242 GLU A1246 1 O ARG A1242 N ILE A1217
SHEET 8 B11 TYR A1346 ASN A1351 1 O MET A1347 N SER A1245
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 GLN A1534 N GLN A1528
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 LYS B2078 ASN B2079 1 O LYS B2078 N LEU B2034
SHEET 1 E 9 LYS B2036 VAL B2038 0
SHEET 2 E 9 VAL B2047 PRO B2054 -1 O VAL B2047 N VAL B2038
SHEET 3 E 9 TYR B2118 THR B2123 -1 O THR B2123 N ALA B2048
SHEET 4 E 9 VAL B2164 ILE B2168 -1 O THR B2167 N ASN B2120
SHEET 5 E 9 LEU B2133 ILE B2139 1 N TRP B2138 O VAL B2166
SHEET 6 E 9 GLY B2210 GLU B2220 1 O ASN B2211 N LEU B2133
SHEET 7 E 9 ARG B2242 GLU B2246 1 O ARG B2242 N ILE B2217
SHEET 8 E 9 TYR B2346 ASN B2351 1 O MET B2347 N SER B2245
SHEET 9 E 9 THR B2444 PHE B2449 1 O TYR B2445 N VAL B2348
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 GLY B2525 GLN B2528 0
SHEET 2 G 2 GLN B2534 GLN B2537 -1 O GLN B2534 N GLN B2528
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 LYS C3078 ASN C3079 1 O LYS C3078 N LEU C3034
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 THR C3123 N ALA C3048
SHEET 4 I11 VAL C3164 ILE C3168 -1 O THR C3167 N ASN C3120
SHEET 5 I11 LEU C3133 ILE C3139 1 N TRP C3138 O VAL C3166
SHEET 6 I11 GLY C3210 GLU C3220 1 O ASN C3211 N LEU C3133
SHEET 7 I11 ARG C3242 GLU C3246 1 O ARG C3242 N ILE C3217
SHEET 8 I11 TYR C3346 ASN C3351 1 O MET C3347 N SER C3245
SHEET 9 I11 THR C3444 GLN C3450 1 O TYR C3445 N VAL C3348
SHEET 10 I11 GLY C3525 GLY C3530 1 O ILE C3529 N GLN C3450
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
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
LINK ND2 ASN A1079 C1 NAG A 179
LINK ND2 ASN B2079 C1 NAG B 279
LINK ND2 ASN C3079 C1 NAG C 379
CRYST1 55.292 179.877 201.323 90.00 90.00 90.00 P 21 21 21 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018086 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005559 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004967 0.00000
TER 4131 LYS A1553
TER 8262 LYS B2553
TER 12393 LYS C3553
MASTER 341 0 18 70 48 0 0 612967 3 291 126
END |