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HEADER HYDROLASE 20-JUL-06 2HRQ
TITLE CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE 1 (HCE1)
TITLE 2 IN COVALENT COMPLEX WITH THE NERVE AGENT SOMAN (GD)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND 3 CHAIN: A, B, C, D, E, F;
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, SOMAN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.FLEMING,M.R.REDINBO
REVDAT 1 01-MAY-07 2HRQ 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) : 42.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 86030.230
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 108029
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) : 0.170
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7595
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 16109
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1199
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24757
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 468
REMARK 3 SOLVENT ATOMS : 1115
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.35000
REMARK 3 B22 (A**2) : 3.85000
REMARK 3 B33 (A**2) : -0.50000
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.25
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) : 0.38
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) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.81
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) : 1.350 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.310 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.180 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 31.03
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : SUC.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 5 : SUC.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HRQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-2006.
REMARK 100 THE RCSB ID CODE IS RCSB038684.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-2005
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 : 23-ID-D
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 : 109291
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10200
REMARK 200 FOR THE DATA SET : 19.7000
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 (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21600
REMARK 200 FOR SHELL : 7.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY: 1MX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.51
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 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 90.59650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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, G, H, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, J, K, L
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 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 465 SER E 5021
REMARK 465 SER F 6021
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 ND2 ASN A 1079 O5 NAG G 179 1.81
REMARK 500 ND2 ASN F 6079 O5 NAG L 679 1.84
REMARK 500 CG ASN A 1079 O5 NAG G 179 1.89
REMARK 500 ND2 ASN D 4079 O5 NAG J 479 1.95
REMARK 500 ND2 ASN F 6079 C2 NAG L 679 2.02
REMARK 500 C8 NAG G 179 O HOH 8924 2.04
REMARK 500 ND2 ASN D 4079 C2 NAG J 479 2.13
REMARK 500 CG ASN D 4079 O5 NAG J 479 2.14
REMARK 500 N2 NAG G 179 O HOH 8924 2.14
REMARK 500 O7 SIA I 382 O HOH 8364 2.18
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 -0.054
REMARK 500 LYS A1092 CE LYS A1092 NZ -0.155
REMARK 500 MET A1446 SD MET A1446 CE 0.079
REMARK 500 LYS B2092 CD LYS B2092 CE -0.057
REMARK 500 LYS B2092 CE LYS B2092 NZ -0.156
REMARK 500 MET B2459 SD MET B2459 CE 0.045
REMARK 500 LYS C3092 CD LYS C3092 CE -0.054
REMARK 500 LYS C3092 CE LYS C3092 NZ -0.158
REMARK 500 GLU C3292 CB GLU C3292 CG 0.050
REMARK 500 GLU C3292 CG GLU C3292 CD 0.051
REMARK 500 MET C3364 SD MET C3364 CE 0.049
REMARK 500 LYS D4092 CD LYS D4092 CE -0.055
REMARK 500 LYS D4092 CE LYS D4092 NZ -0.154
REMARK 500 MET D4136 SD MET D4136 CE 0.055
REMARK 500 MET D4446 SD MET D4446 CE 0.040
REMARK 500 MET D4459 SD MET D4459 CE 0.043
REMARK 500 LYS E5092 CD LYS E5092 CE -0.058
REMARK 500 LYS E5092 CE LYS E5092 NZ -0.155
REMARK 500 MET E5459 SD MET E5459 CE 0.053
REMARK 500 LYS F6092 CD LYS F6092 CE -0.060
REMARK 500 LYS F6092 CE LYS F6092 NZ -0.158
REMARK 500 MET F6364 CG MET F6364 SD -0.041
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 LYS A1092 CD - CE - NZ ANGL. DEV. = 12.6 DEGREES
REMARK 500 ASP A1115 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A1126 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 PHE A1177 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 THR A1252 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 SER A1253 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 ILE A1323 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 GLY A1484 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU B2034 CA - CB - CG ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP B2090 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 LYS B2092 CD - CE - NZ ANGL. DEV. = 11.9 DEGREES
REMARK 500 ASP B2115 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 GLU B2183 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 ASN B2204 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 SER B2253 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU B2319 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 GLY B2484 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASN B2506 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 SER C3075 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 MET C3086 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 LYS C3092 CD - CE - NZ ANGL. DEV. = 12.6 DEGREES
REMARK 500 ASP C3126 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 GLU C3183 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 THR C3252 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 SER C3253 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLY C3320 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 LEU C3420 CA - CB - CG ANGL. DEV. = 10.2 DEGREES
REMARK 500 GLY C3484 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 GLN C3528 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 LYS C3538 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 LYS D4092 CD - CE - NZ ANGL. DEV. = 12.6 DEGREES
REMARK 500 ASP D4115 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 ASP D4126 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASN D4204 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 SER D4253 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU D4319 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 GLU D4448 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 GLY D4484 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 LEU E5034 CA - CB - CG ANGL. DEV. = 7.8 DEGREES
REMARK 500 SER E5075 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 THR E5081 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 MET E5086 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 LYS E5092 CD - CE - NZ ANGL. DEV. = 12.1 DEGREES
REMARK 500 ASP E5115 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ASN E5204 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 SER E5253 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 LEU E5319 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 ASN E5506 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU F6034 CA - CB - CG ANGL. DEV. = 8.2 DEGREES
REMARK 500 SER F6075 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 LYS F6092 CD - CE - NZ ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASP F6126 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLU F6183 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASN F6204 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 THR F6252 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 SER F6253 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 GLY F6320 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 LEU F6420 CA - CB - CG ANGL. DEV. = 10.2 DEGREES
REMARK 500 GLY F6484 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 GLN F6528 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 LYS F6538 N - CA - C ANGL. DEV. = 8.6 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 -118.31 73.00
REMARK 500 SER C3221 -117.08 64.16
REMARK 500 SER D4221 -119.98 68.71
REMARK 500 ASN E5238 9.14 142.29
REMARK 500 SER F6221 -116.32 60.38
DBREF 2HRQ A 1021 1553 UNP Q9UK77 EST1_HUMAN 21 553
DBREF 2HRQ B 2021 2553 UNP Q9UK77 EST1_HUMAN 21 553
DBREF 2HRQ C 3021 3553 UNP Q9UK77 EST1_HUMAN 21 553
DBREF 2HRQ D 4021 4553 UNP Q9UK77 EST1_HUMAN 21 553
DBREF 2HRQ E 5021 5553 UNP Q9UK77 EST1_HUMAN 21 553
DBREF 2HRQ F 6021 6553 UNP Q9UK77 EST1_HUMAN 21 553
SEQADV 2HRQ A UNP Q9UK77 GLN 362 DELETION
SEQADV 2HRQ B UNP Q9UK77 GLN 362 DELETION
SEQADV 2HRQ C UNP Q9UK77 GLN 362 DELETION
SEQADV 2HRQ D UNP Q9UK77 GLN 362 DELETION
SEQADV 2HRQ E UNP Q9UK77 GLN 362 DELETION
SEQADV 2HRQ F 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
SEQRES 1 D 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 D 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 D 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 D 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 D 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 D 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 D 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 D 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 D 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 D 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 D 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 D 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 D 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 D 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 D 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 D 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 D 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 D 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 D 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 D 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 D 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 D 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 D 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 D 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 D 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 D 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 D 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 D 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 D 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 D 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 D 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 D 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 D 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 D 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 D 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 D 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 D 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 D 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 D 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 D 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 D 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 E 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 E 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 E 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 E 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 E 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 E 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 E 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 E 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 E 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 E 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 E 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 E 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 E 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 E 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 E 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 E 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 E 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 E 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 E 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 E 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 E 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 E 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 E 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 E 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 E 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 E 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 E 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 E 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 E 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 E 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 E 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 E 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 E 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 E 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 E 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 E 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 E 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 E 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 E 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 E 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 E 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
SEQRES 1 F 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 F 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 F 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 F 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 F 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 F 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 F 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 F 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 F 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 F 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 F 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 F 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 F 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 F 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 F 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 F 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 F 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 F 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 F 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 F 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 F 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 F 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 F 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 F 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 F 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 F 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 F 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 F 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 F 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 F 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 F 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 F 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 F 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 F 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 F 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 F 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 F 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 F 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 F 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 F 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 F 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
MODRES 2HRQ ASN A 1079 ASN GLYCOSYLATION SITE
MODRES 2HRQ ASN B 2079 ASN GLYCOSYLATION SITE
MODRES 2HRQ ASN C 3079 ASN GLYCOSYLATION SITE
MODRES 2HRQ ASN D 4079 ASN GLYCOSYLATION SITE
MODRES 2HRQ ASN E 5079 ASN GLYCOSYLATION SITE
MODRES 2HRQ ASN F 6079 ASN GLYCOSYLATION SITE
HET NAG G 179 14
HET SIA G 182 21
HET NAG H 279 14
HET SIA H 282 21
HET NAG I 379 14
HET SIA I 382 21
HET NAG J 479 14
HET SIA J 482 21
HET NAG K 579 14
HET SIA K 582 21
HET NAG L 679 14
HET SIA L 682 21
HET SUC 11 23
HET SUC 22 23
HET SUC 33 23
HET SUC 44 23
HET SUC 55 23
HET SUC 66 23
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 GD7 A 1 10
HET GD7 B 1 10
HET GD7 C 1 10
HET GD7 D 1 10
HET GD7 E 1 10
HET GD7 F 1 10
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SIA O-SIALIC ACID
HETNAM SUC SUCROSE
HETNAM SO4 SULFATE ION
HETNAM GD7 (1R)-1,2,2-TRIMETHYLPROPYL (R)-METHYLPHOSPHINATE
HETSYN NAG NAG
FORMUL 7 NAG 6(C8 H15 N1 O6)
FORMUL 8 SIA 6(C11 H19 N1 O9)
FORMUL 19 SUC 6(C12 H22 O11)
FORMUL 25 SO4 12(O4 S1 2-)
FORMUL 37 GD7 6(C7 H17 O2 P1)
FORMUL 43 HOH *1115(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 ASP A 1182 ARG A 1186 5 5
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 LEU A 1232 1 12
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 LYS A 1302 1 13
HELIX 13 13 ASP A 1311 SER A 1315 5 5
HELIX 14 14 THR A 1331 GLU A 1338 1 8
HELIX 15 15 TRP A 1357 SER A 1365 1 8
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 PHE A 1551 1 12
HELIX 25 25 LEU B 2060 ARG B 2064 5 5
HELIX 26 26 ASP B 2090 THR B 2102 1 13
HELIX 27 27 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 THR B 2252 VAL B 2256 5 5
HELIX 33 33 VAL B 2261 ALA B 2272 1 12
HELIX 34 34 THR B 2278 ARG B 2287 1 10
HELIX 35 35 THR B 2290 MET B 2301 1 12
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 ASP B 2374 SER B 2385 1 12
HELIX 39 39 SER B 2385 CYS B 2390 1 6
HELIX 40 40 ALA B 2392 GLU B 2394 5 3
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 ALA B 2440 1 15
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 ILE C 3205 1 18
HELIX 53 53 ALA C 3206 PHE C 3208 5 3
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 GLN C 3288 1 11
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 MET C 3364 1 7
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 ALA C 3440 1 15
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 PHE C 3551 1 12
HELIX 71 71 LEU D 4060 ARG D 4064 5 5
HELIX 72 72 ASP D 4090 THR D 4102 1 13
HELIX 73 73 GLY D 4154 ASN D 4162 1 9
HELIX 74 74 LEU D 4172 PHE D 4178 1 7
HELIX 75 75 ASN D 4188 ILE D 4205 1 18
HELIX 76 76 ALA D 4206 PHE D 4208 5 3
HELIX 77 77 SER D 4221 SER D 4233 1 13
HELIX 78 78 THR D 4252 VAL D 4256 5 5
HELIX 79 79 VAL D 4261 GLY D 4273 1 13
HELIX 80 80 THR D 4278 ARG D 4287 1 10
HELIX 81 81 THR D 4290 LYS D 4302 1 13
HELIX 82 82 ASP D 4311 SER D 4315 5 5
HELIX 83 83 THR D 4331 GLU D 4338 1 8
HELIX 84 84 TRP D 4357 SER D 4365 1 8
HELIX 85 85 ASP D 4374 SER D 4385 1 12
HELIX 86 86 SER D 4385 CYS D 4390 1 6
HELIX 87 87 LEU D 4395 GLY D 4405 1 11
HELIX 88 88 ASP D 4409 PHE D 4426 1 18
HELIX 89 89 PHE D 4426 ALA D 4440 1 15
HELIX 90 90 GLU D 4471 PHE D 4476 1 6
HELIX 91 91 GLY D 4477 LEU D 4481 5 5
HELIX 92 92 SER D 4486 GLY D 4507 1 22
HELIX 93 93 LYS D 4540 PHE D 4551 1 12
HELIX 94 94 LEU E 5060 ARG E 5064 5 5
HELIX 95 95 ASP E 5090 THR E 5102 1 13
HELIX 96 96 GLY E 5154 ASN E 5162 1 9
HELIX 97 97 LEU E 5172 PHE E 5178 1 7
HELIX 98 98 ASN E 5188 ILE E 5205 1 18
HELIX 99 99 ALA E 5206 PHE E 5208 5 3
HELIX 100 100 SER E 5221 SER E 5233 1 13
HELIX 101 101 PRO E 5234 LYS E 5237 5 4
HELIX 102 102 THR E 5252 VAL E 5256 5 5
HELIX 103 103 VAL E 5261 GLY E 5273 1 13
HELIX 104 104 THR E 5278 GLN E 5288 1 11
HELIX 105 105 THR E 5290 LYS E 5302 1 13
HELIX 106 106 ASP E 5311 SER E 5315 5 5
HELIX 107 107 THR E 5331 ALA E 5337 1 7
HELIX 108 108 TRP E 5357 MET E 5364 1 7
HELIX 109 109 ASP E 5374 SER E 5385 1 12
HELIX 110 110 SER E 5385 CYS E 5390 1 6
HELIX 111 111 LEU E 5395 GLY E 5405 1 11
HELIX 112 112 ASP E 5409 PHE E 5426 1 18
HELIX 113 113 PHE E 5426 ALA E 5440 1 15
HELIX 114 114 GLU E 5471 PHE E 5476 1 6
HELIX 115 115 GLY E 5477 LEU E 5481 5 5
HELIX 116 116 SER E 5486 GLY E 5507 1 22
HELIX 117 117 LYS E 5540 ALA E 5552 1 13
HELIX 118 118 LEU F 6060 ARG F 6064 5 5
HELIX 119 119 ASP F 6090 THR F 6102 1 13
HELIX 120 120 GLY F 6154 ASN F 6162 1 9
HELIX 121 121 LEU F 6172 PHE F 6178 1 7
HELIX 122 122 ASN F 6188 ILE F 6205 1 18
HELIX 123 123 ALA F 6206 PHE F 6208 5 3
HELIX 124 124 SER F 6221 SER F 6233 1 13
HELIX 125 125 THR F 6252 VAL F 6256 5 5
HELIX 126 126 VAL F 6261 ALA F 6272 1 12
HELIX 127 127 THR F 6278 LYS F 6289 1 12
HELIX 128 128 THR F 6290 LYS F 6302 1 13
HELIX 129 129 THR F 6331 ALA F 6337 1 7
HELIX 130 130 TRP F 6357 MET F 6364 1 7
HELIX 131 131 ASP F 6374 SER F 6385 1 12
HELIX 132 132 SER F 6385 CYS F 6390 1 6
HELIX 133 133 LEU F 6395 GLY F 6405 1 11
HELIX 134 134 ASP F 6409 PHE F 6426 1 18
HELIX 135 135 PHE F 6426 ALA F 6440 1 15
HELIX 136 136 ASP F 6470 PHE F 6476 1 7
HELIX 137 137 GLY F 6477 LYS F 6482 1 6
HELIX 138 138 SER F 6486 GLY F 6507 1 22
HELIX 139 139 LYS F 6540 PHE F 6551 1 12
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 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 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 GLU A1448
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 LEU B2040 0
SHEET 2 E11 PHE B2043 PRO B2054 -1 O VAL B2047 N VAL B2038
SHEET 3 E11 TYR B2118 THR B2123 -1 O THR B2123 N ALA B2048
SHEET 4 E11 VAL B2164 ILE B2168 -1 O THR B2167 N ASN B2120
SHEET 5 E11 LEU B2133 ILE B2139 1 N MET B2136 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 SER B2245
SHEET 9 E11 THR B2444 GLN B2450 1 O TYR B2445 N VAL B2348
SHEET 10 E11 GLY B2525 GLY B2530 1 O ILE B2529 N GLN B2450
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 LEU C3034
SHEET 1 H11 LYS C3036 VAL C3038 0
SHEET 2 H11 VAL C3047 PRO C3054 -1 O ILE C3049 N LYS C3036
SHEET 3 H11 TYR C3118 THR C3123 -1 O ILE C3121 N PHE C3050
SHEET 4 H11 VAL C3164 ILE C3168 -1 O VAL C3165 N TYR C3122
SHEET 5 H11 LEU C3133 ILE C3139 1 N MET C3136 O VAL C3164
SHEET 6 H11 GLY C3210 GLU C3220 1 O THR C3216 N VAL C3135
SHEET 7 H11 ARG C3242 GLU C3246 1 O GLU C3246 N GLY C3219
SHEET 8 H11 TYR C3346 ASN C3351 1 O MET C3347 N ALA C3243
SHEET 9 H11 THR C3444 PHE C3449 1 O TYR C3445 N VAL C3348
SHEET 10 H11 TYR C3526 ILE C3529 1 O LEU C3527 N MET C3446
SHEET 11 H11 GLN C3534 ALA C3536 -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
SHEET 1 J 3 VAL D4025 THR D4028 0
SHEET 2 J 3 GLY D4031 LEU D4034 -1 O VAL D4033 N VAL D4026
SHEET 3 J 3 VAL D4077 ASN D4079 1 O LYS D4078 N LEU D4034
SHEET 1 K11 LYS D4036 VAL D4038 0
SHEET 2 K11 VAL D4047 PRO D4054 -1 O ILE D4049 N LYS D4036
SHEET 3 K11 TYR D4118 THR D4123 -1 O THR D4123 N ALA D4048
SHEET 4 K11 VAL D4164 ILE D4168 -1 O THR D4167 N ASN D4120
SHEET 5 K11 LEU D4133 ILE D4139 1 N MET D4136 O VAL D4164
SHEET 6 K11 GLY D4210 GLU D4220 1 O THR D4216 N VAL D4137
SHEET 7 K11 ARG D4242 GLU D4246 1 O GLU D4246 N GLY D4219
SHEET 8 K11 TYR D4346 ASN D4351 1 O MET D4347 N ALA D4243
SHEET 9 K11 THR D4444 PHE D4449 1 O PHE D4449 N ILE D4350
SHEET 10 K11 GLY D4525 ILE D4529 1 O LEU D4527 N GLU D4448
SHEET 11 K11 GLN D4534 GLN D4537 -1 O GLN D4534 N GLN D4528
SHEET 1 L 2 MET D4086 CYS D4087 0
SHEET 2 L 2 LEU D4112 SER D4113 1 O SER D4113 N MET D4086
SHEET 1 M 3 VAL E5025 THR E5028 0
SHEET 2 M 3 GLY E5031 LEU E5034 -1 O VAL E5033 N VAL E5026
SHEET 3 M 3 VAL E5077 ASN E5079 1 O LYS E5078 N LEU E5034
SHEET 1 N11 LYS E5036 LEU E5040 0
SHEET 2 N11 PHE E5043 PRO E5054 -1 O VAL E5047 N VAL E5038
SHEET 3 N11 TYR E5118 THR E5123 -1 O THR E5123 N ALA E5048
SHEET 4 N11 VAL E5164 ILE E5168 -1 O VAL E5165 N TYR E5122
SHEET 5 N11 LEU E5133 ILE E5139 1 N MET E5136 O VAL E5166
SHEET 6 N11 GLY E5210 GLU E5220 1 O THR E5216 N VAL E5137
SHEET 7 N11 ARG E5242 GLU E5246 1 O GLU E5246 N GLY E5219
SHEET 8 N11 TYR E5346 ASN E5351 1 O MET E5347 N ALA E5243
SHEET 9 N11 THR E5444 PHE E5449 1 O TYR E5445 N VAL E5348
SHEET 10 N11 GLY E5525 ILE E5529 1 O ILE E5529 N GLU E5448
SHEET 11 N11 GLN E5534 GLN E5537 -1 O GLN E5534 N GLN E5528
SHEET 1 O 2 MET E5086 CYS E5087 0
SHEET 2 O 2 LEU E5112 SER E5113 1 O SER E5113 N MET E5086
SHEET 1 P 3 VAL F6025 THR F6028 0
SHEET 2 P 3 GLY F6031 LEU F6034 -1 O VAL F6033 N VAL F6026
SHEET 3 P 3 VAL F6077 ASN F6079 1 O LYS F6078 N LEU F6034
SHEET 1 Q11 LYS F6036 VAL F6038 0
SHEET 2 Q11 VAL F6047 PRO F6054 -1 O ILE F6049 N LYS F6036
SHEET 3 Q11 TYR F6118 THR F6123 -1 O ILE F6121 N PHE F6050
SHEET 4 Q11 VAL F6164 ILE F6168 -1 O THR F6167 N ASN F6120
SHEET 5 Q11 LEU F6133 ILE F6139 1 N MET F6136 O VAL F6164
SHEET 6 Q11 GLY F6210 GLU F6220 1 O THR F6216 N VAL F6135
SHEET 7 Q11 ARG F6242 GLU F6246 1 O ILE F6244 N ILE F6217
SHEET 8 Q11 TYR F6346 ASN F6351 1 O MET F6347 N ALA F6243
SHEET 9 Q11 THR F6444 PHE F6449 1 O TYR F6445 N VAL F6348
SHEET 10 Q11 TYR F6526 ILE F6529 1 O LEU F6527 N MET F6446
SHEET 11 Q11 GLN F6534 ALA F6536 -1 O ALA F6536 N TYR F6526
SHEET 1 R 2 MET F6086 CYS F6087 0
SHEET 2 R 2 LEU F6112 SER F6113 1 O SER F6113 N MET F6086
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 B2079 C1 NAG H 279
LINK ND2 ASN C3079 C1 NAG I 379
LINK ND2 ASN E5079 C1 NAG K 579
LINK OG SER A1221 P1 GD7 A 1
LINK OG SER B2221 P1 GD7 B 1
LINK OG SER C3221 P1 GD7 C 1
LINK OG SER D4221 P1 GD7 D 1
LINK OG SER E5221 P1 GD7 E 1
LINK OG SER F6221 P1 GD7 F 1
LINK ND2 ASN A1079 C1 NAG G 179
LINK ND2 ASN D4079 C1 NAG J 479
LINK ND2 ASN F6079 C1 NAG L 679
CRYST1 55.463 181.193 203.051 90.00 89.99 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 0.018030 0.000000 -0.000003 0.00000
SCALE2 0.000000 0.005519 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004925 0.00000
TER 4131 LYS A1553
TER 8256 LYS B2553
TER 12381 LYS C3553
TER 16512 LYS D4553
TER 20637 LYS E5553
TER 24763 LYS F6553
MASTER 374 0 36 139 96 0 0 626340 6 504 246
END |