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HEADER HYDROLASE 20-JUL-06 2HRR
TITLE CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE 1 (HCE1)
TITLE 2 IN COVALENT COMPLEX WITH THE NERVE AGENT TABUN (GA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: ACYL COENZYME A:CHOLESTEROL ACYLTRANSFERASE, ACAT,
COMPND 5 MONOCYTE/MACROPHAGE SERINE ESTERASE, HMSE, SERINE ESTERASE
COMPND 6 1, BRAIN CARBOXYLESTERASE HBR1, TRIACYLGLYCEROL HYDROLASE,
COMPND 7 TGH, EGASYN;
COMPND 8 EC: 3.1.1.1;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: CES1;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM
KEYWDS HYDROLASE, CARBOXYLESTERASE, TABUN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.FLEMING,M.R.REDINBO
REVDAT 1 01-MAY-07 2HRR 0
JRNL AUTH C.D.FLEMING,C.C.EDWARDS,S.D.KIRBY,D.M.MAXWELL,
JRNL AUTH 2 P.M.POTTER,D.M.CERASOLI,M.R.REDINBO
JRNL TITL CRYSTAL STRUCTURES OF HUMAN CARBOXYLESTERASE 1 IN
JRNL TITL 2 COVALENT COMPLEXES WITH THE CHEMICAL WARFARE
JRNL TITL 3 AGENTS SOMAN AND TABUN.
JRNL REF BIOCHEMISTRY 2007
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 72889.760
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 52209
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) : 0.167
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3705
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7979
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 626
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12379
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 223
REMARK 3 SOLVENT ATOMS : 827
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.90000
REMARK 3 B22 (A**2) : 1.30000
REMARK 3 B33 (A**2) : -0.40000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.24
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84
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) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.270 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 28.98
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 : GAC.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 : GAC.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HRR COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-2006.
REMARK 100 THE RCSB ID CODE IS RCSB038685.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-2006
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53127
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11700
REMARK 200 FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29200
REMARK 200 FOR SHELL : 7.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY: 1MX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE PH 5.5, 8-11% PEG
REMARK 280 3350, 0.1-0.4M LITHIUM SULFATE, 0.1M LITHIUM CHLORIDE, 0.1M
REMARK 280 SODIUM CHLORIDE, 5% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.78500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.46000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.52500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 101.46000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.78500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.52500
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 SER B 2021
REMARK 465 SER C 3021
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 OG SER B 2221 O1 NTJ 2 1.59
REMARK 500 ND2 ASN A 1079 O5 NAG A 179 1.81
REMARK 500 ND2 ASN C 3079 O5 NAG C 379 1.88
REMARK 500 ND2 ASN C 3079 C2 NAG C 379 2.16
REMARK 500 O ASN B 2079 O2 SIA 282 2.17
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A1092 CD LYS A1092 CE -0.056
REMARK 500 LYS A1092 CE LYS A1092 NZ -0.154
REMARK 500 PRO A1317 CB PRO A1317 CG 0.097
REMARK 500 PRO A1317 CG PRO A1317 CD 0.054
REMARK 500 MET A1459 SD MET A1459 CE 0.040
REMARK 500 LYS B2092 CD LYS B2092 CE -0.058
REMARK 500 LYS B2092 CE LYS B2092 NZ -0.158
REMARK 500 LYS C3092 CD LYS C3092 CE -0.058
REMARK 500 LYS C3092 CE LYS C3092 NZ -0.156
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 SER A1075 N - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 ASP A1090 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 LYS A1092 CD - CE - NZ ANGL. DEV. = 12.4 DEGREES
REMARK 500 ASP A1126 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ARG A1242 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 THR A1252 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 SER A1253 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 GLN A1316 N - CA - C ANGL. DEV. = 14.0 DEGREES
REMARK 500 PRO A1317 N - CA - C ANGL. DEV. =-15.4 DEGREES
REMARK 500 PRO A1317 C - N - CA ANGL. DEV. =-12.3 DEGREES
REMARK 500 PRO A1317 C - N - CD ANGL. DEV. = 7.7 DEGREES
REMARK 500 ILE A1323 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 GLU A1448 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 TRP A1517 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 GLN A1528 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 SER B2075 N - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 LYS B2092 CD - CE - NZ ANGL. DEV. = 12.0 DEGREES
REMARK 500 ASP B2115 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 PHE B2177 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 THR B2252 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 SER B2253 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 LEU B2319 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 LEU C3034 CA - CB - CG ANGL. DEV. = 9.7 DEGREES
REMARK 500 SER C3075 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 MET C3086 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 PRO C3091 C - N - CD ANGL. DEV. = 8.1 DEGREES
REMARK 500 LYS C3092 CD - CE - NZ ANGL. DEV. = 12.3 DEGREES
REMARK 500 ASP C3115 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 TYR C3122 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 PHE C3177 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 ASN C3204 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 SER C3253 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU C3319 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 ILE C3323 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 ALA C3536 N - CA - C ANGL. DEV. = -8.0 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 A1221 -119.59 63.81
REMARK 500 SER C3221 -115.03 64.19
DBREF 2HRR A 1021 1553 UNP Q9UK77 EST1_HUMAN 21 553
DBREF 2HRR B 2021 2553 UNP Q9UK77 EST1_HUMAN 21 553
DBREF 2HRR C 3021 3553 UNP Q9UK77 EST1_HUMAN 21 553
SEQADV 2HRR A UNP Q9UK77 GLN 362 DELETION
SEQADV 2HRR B UNP Q9UK77 GLN 362 DELETION
SEQADV 2HRR C UNP Q9UK77 GLN 362 DELETION
SEQRES 1 A 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 A 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 A 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 A 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 A 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 A 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 A 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 A 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 A 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 A 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 A 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 A 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 A 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 A 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 A 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 A 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 A 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 A 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 A 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 A 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 A 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 A 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 A 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 A 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 A 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 A 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 A 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 A 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 A 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 A 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 A 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 A 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 A 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 A 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 A 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 A 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 A 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 A 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 A 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 A 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 A 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 B 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 B 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 B 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 B 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 B 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 B 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 B 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 B 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 B 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 B 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 B 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 B 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 B 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 B 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 B 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 B 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 B 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 B 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 B 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 B 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 B 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 B 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 B 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 B 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 B 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 B 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 B 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 B 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 B 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 B 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 B 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 B 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 B 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 B 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 B 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 B 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 B 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 B 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 B 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 B 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 B 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 C 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 C 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 C 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 C 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 C 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 C 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 C 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 C 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 C 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 C 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 C 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 C 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 C 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 C 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 C 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 C 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 C 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 C 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 C 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 C 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 C 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 C 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 C 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 C 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 C 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 C 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 C 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 C 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 C 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 C 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 C 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 C 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 C 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 C 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 C 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 C 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 C 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 C 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 C 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 C 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 C 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
MODRES 2HRR ASN A 1079 ASN GLYCOSYLATION SITE
MODRES 2HRR ASN B 2079 ASN GLYCOSYLATION SITE
MODRES 2HRR 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 SUC 11 23
HET SUC 22 23
HET SUC 33 23
HET SO4 184 5
HET SO4 185 5
HET SO4 284 5
HET SO4 285 5
HET SO4 384 5
HET NTJ 1 8
HET NTJ 2 8
HET NTJ 3 8
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SIA O-SIALIC ACID
HETNAM SUC SUCROSE
HETNAM SO4 SULFATE ION
HETNAM NTJ R-ETHYL N,N-DIMETHYLPHOSPHONAMIDOATE
HETSYN NAG NAG
FORMUL 4 NAG 3(C8 H15 N1 O6)
FORMUL 5 SIA 3(C11 H19 N1 O9)
FORMUL 10 SUC 3(C12 H22 O11)
FORMUL 13 SO4 5(O4 S1 2-)
FORMUL 18 NTJ 3(C4 H11 N1 O2 P1)
FORMUL 21 HOH *827(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 ALA A 1148 TYR A 1152 5 5
HELIX 4 4 GLY A 1154 ASN A 1162 1 9
HELIX 5 5 LEU A 1172 PHE A 1178 1 7
HELIX 6 6 ASN A 1188 ILE A 1205 1 18
HELIX 7 7 ALA A 1206 PHE A 1208 5 3
HELIX 8 8 SER A 1221 SER A 1233 1 13
HELIX 9 9 THR A 1252 VAL A 1256 5 5
HELIX 10 10 VAL A 1261 GLY A 1273 1 13
HELIX 11 11 THR A 1278 GLN A 1288 1 11
HELIX 12 12 THR A 1290 MET A 1301 1 12
HELIX 13 13 ASP A 1311 SER A 1315 5 5
HELIX 14 14 THR A 1331 ALA A 1337 1 7
HELIX 15 15 TRP A 1357 MET A 1364 1 7
HELIX 16 16 ASP A 1374 SER A 1385 1 12
HELIX 17 17 SER A 1385 CYS A 1390 1 6
HELIX 18 18 LEU A 1395 GLY A 1405 1 11
HELIX 19 19 ASP A 1409 PHE A 1426 1 18
HELIX 20 20 PHE A 1426 ALA A 1440 1 15
HELIX 21 21 GLU A 1471 PHE A 1476 1 6
HELIX 22 22 GLY A 1477 LEU A 1481 5 5
HELIX 23 23 SER A 1486 GLY A 1507 1 22
HELIX 24 24 LYS A 1540 ALA A 1552 1 13
HELIX 25 25 LEU B 2060 ARG B 2064 5 5
HELIX 26 26 ASP B 2090 THR B 2102 1 13
HELIX 27 27 GLY B 2154 ASN B 2162 1 9
HELIX 28 28 LEU B 2172 PHE B 2178 1 7
HELIX 29 29 ASN B 2188 ILE B 2205 1 18
HELIX 30 30 ALA B 2206 PHE B 2208 5 3
HELIX 31 31 SER B 2221 SER B 2233 1 13
HELIX 32 32 PRO B 2234 LYS B 2237 5 4
HELIX 33 33 THR B 2252 VAL B 2256 5 5
HELIX 34 34 VAL B 2261 ALA B 2272 1 12
HELIX 35 35 THR B 2278 ARG B 2287 1 10
HELIX 36 36 THR B 2290 LYS B 2302 1 13
HELIX 37 37 THR B 2331 ALA B 2337 1 7
HELIX 38 38 TRP B 2357 MET B 2364 1 7
HELIX 39 39 PRO B 2367 GLY B 2371 5 5
HELIX 40 40 ASP B 2374 SER B 2385 1 12
HELIX 41 41 SER B 2385 CYS B 2390 1 6
HELIX 42 42 LEU B 2395 GLY B 2405 1 11
HELIX 43 43 ASP B 2409 PHE B 2426 1 18
HELIX 44 44 PHE B 2426 ALA B 2440 1 15
HELIX 45 45 GLU B 2471 PHE B 2476 1 6
HELIX 46 46 GLY B 2477 LEU B 2481 5 5
HELIX 47 47 SER B 2486 GLY B 2507 1 22
HELIX 48 48 LYS B 2540 ALA B 2552 1 13
HELIX 49 49 LEU C 3060 ARG C 3064 5 5
HELIX 50 50 ASP C 3090 THR C 3102 1 13
HELIX 51 51 GLY C 3154 ASN C 3162 1 9
HELIX 52 52 LEU C 3172 PHE C 3178 1 7
HELIX 53 53 ASN C 3188 ILE C 3205 1 18
HELIX 54 54 ALA C 3206 PHE C 3208 5 3
HELIX 55 55 SER C 3221 SER C 3233 1 13
HELIX 56 56 ALA C 3236 PHE C 3240 5 5
HELIX 57 57 THR C 3252 VAL C 3256 5 5
HELIX 58 58 VAL C 3261 ALA C 3272 1 12
HELIX 59 59 THR C 3278 GLN C 3288 1 11
HELIX 60 60 THR C 3290 LYS C 3302 1 13
HELIX 61 61 ASP C 3311 SER C 3315 5 5
HELIX 62 62 THR C 3331 GLU C 3338 1 8
HELIX 63 63 TRP C 3357 SER C 3365 1 8
HELIX 64 64 ASP C 3374 SER C 3385 1 12
HELIX 65 65 SER C 3385 CYS C 3390 1 6
HELIX 66 66 LEU C 3395 GLY C 3405 1 11
HELIX 67 67 ASP C 3409 PHE C 3426 1 18
HELIX 68 68 PHE C 3426 ALA C 3440 1 15
HELIX 69 69 GLU C 3471 PHE C 3476 1 6
HELIX 70 70 GLY C 3477 LEU C 3481 5 5
HELIX 71 71 SER C 3486 GLY C 3507 1 22
HELIX 72 72 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 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 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 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 SER A1245
SHEET 9 B11 THR A1444 PHE A1449 1 O TYR A1445 N VAL A1348
SHEET 10 B11 GLY A1525 ILE A1529 1 O LEU A1527 N MET A1446
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 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 TRP B2138 O VAL B2166
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 3 VAL C3025 THR C3028 0
SHEET 2 G 3 GLY C3031 LEU C3034 -1 O VAL C3033 N VAL C3026
SHEET 3 G 3 VAL C3077 ASN C3079 1 O LYS C3078 N LYS C3032
SHEET 1 H11 LYS C3036 VAL C3038 0
SHEET 2 H11 VAL C3047 PRO C3054 -1 O VAL C3047 N VAL C3038
SHEET 3 H11 TYR C3118 THR C3123 -1 O THR C3123 N ALA C3048
SHEET 4 H11 VAL C3164 ILE C3168 -1 O VAL C3165 N TYR C3122
SHEET 5 H11 LEU C3133 ILE C3139 1 N TRP C3138 O VAL C3166
SHEET 6 H11 GLY C3210 GLU C3220 1 O THR C3216 N VAL C3135
SHEET 7 H11 ARG C3242 GLU C3246 1 O ILE C3244 N ILE C3217
SHEET 8 H11 TYR C3346 ASN C3351 1 O MET C3347 N ALA C3243
SHEET 9 H11 THR C3444 GLN C3450 1 O TYR C3445 N VAL C3348
SHEET 10 H11 GLY C3525 GLY C3530 1 O ILE C3529 N GLN C3450
SHEET 11 H11 GLN C3534 GLN C3537 -1 O ALA C3536 N TYR C3526
SHEET 1 I 2 MET C3086 CYS C3087 0
SHEET 2 I 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 OG SER A1221 P1 NTJ 1
LINK OG SER B2221 P1 NTJ 2
LINK OG SER C3221 P1 NTJ 3
LINK ND2 ASN B2079 C1 NAG B 279
LINK ND2 ASN A1079 C2 NAG A 179
LINK ND2 ASN A1079 C1 NAG A 179
LINK ND2 ASN C3079 C1 NAG C 379
CRYST1 55.570 181.050 202.920 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 0.017995 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004928 0.00000
TER 4131 LYS A1553
TER 8256 LYS B2553
TER 12382 LYS C3553
MASTER 328 0 17 72 48 0 0 613429 3 241 123
END |