HEADER TRANSFERASE 24-SEP-13 3WIR
TITLE CRYSTAL STRUCTURE OF KOJIBIOSE PHOSPHORYLASE COMPLEXED WITH GLUCOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KOJIBIOSE PHOSPHORYLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.4.1.230;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CALDICELLULOSIRUPTOR SACCHAROLYTICUS;
SOURCE 3 ORGANISM_TAXID: 351627;
SOURCE 4 STRAIN: ATCC 43494 / DSM 8903;
SOURCE 5 GENE: CSAC_0444;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 CODONPLUS(DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET0439-C-HIS
KEYWDS (ALPHA/ALPHA)6 BARREL, PHOSPHORYLASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.OKADA,T.YAMAMOTO,H.WATANABE,T.NISHIMOTO,H.CHAEN,S.FUKUDA,T.WAKAGI,
AUTHOR 2 S.FUSHINOBU
REVDAT 3 08-NOV-23 3WIR 1 HETSYN
REVDAT 2 29-JUL-20 3WIR 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 SITE
REVDAT 1 05-FEB-14 3WIR 0
JRNL AUTH S.OKADA,T.YAMAMOTO,H.WATANABE,T.NISHIMOTO,H.CHAEN,S.FUKUDA,
JRNL AUTH 2 T.WAKAGI,S.FUSHINOBU
JRNL TITL STRUCTURAL AND MUTATIONAL ANALYSIS OF SUBSTRATE RECOGNITION
JRNL TITL 2 IN KOJIBIOSE PHOSPHORYLASE
JRNL REF FEBS J. V. 281 778 2014
JRNL REFN ISSN 1742-464X
JRNL PMID 24255995
JRNL DOI 10.1111/FEBS.12622
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.YAMAMOTO,M.NISHIO-KOSAKA,S.IZAWA,H.AGA,T.NISHIMOTO,
REMARK 1 AUTH 2 H.CHAEN,S.FUKUDA
REMARK 1 TITL ENZYMATIC PROPERTIES OF RECOMBINANT KOJIBIOSE PHOSPHORYLASE
REMARK 1 TITL 2 FROM CALDICELLULOSIRUPTOR SACCHAROLYTICUS ATCC43494
REMARK 1 REF BIOSCI.BIOTECHNOL.BIOCHEM. V. 75 1208 2011
REMARK 1 REFN ISSN 0916-8451
REMARK 1 PMID 21670511
REMARK 1 DOI 10.1271/BBB.110116
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 193715
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 + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10235
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13615
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 693
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24748
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 180
REMARK 3 SOLVENT ATOMS : 1378
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : -0.02000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.05000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.219
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.194
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.210
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25478 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 24180 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34419 ; 1.853 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 55764 ; 0.874 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3020 ; 6.875 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1264 ;38.366 ;24.937
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4612 ;16.995 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 108 ;19.023 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3717 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 28508 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5880 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3WIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000096386.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : FIXED EXIT DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 203954
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1H54
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5MM D-GLUCOSE, 5MM SODIUM PHOSPHATE,
REMARK 280 10%(V/V) 2-PROPANOL, 10%(W/V) PEG3350, 0.1M TRIS-HCL, PH 8.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 GLY A 757
REMARK 465 SER A 758
REMARK 465 HIS A 759
REMARK 465 HIS A 760
REMARK 465 HIS A 761
REMARK 465 HIS A 762
REMARK 465 HIS A 763
REMARK 465 HIS A 764
REMARK 465 GLY B 757
REMARK 465 SER B 758
REMARK 465 HIS B 759
REMARK 465 HIS B 760
REMARK 465 HIS B 761
REMARK 465 HIS B 762
REMARK 465 HIS B 763
REMARK 465 HIS B 764
REMARK 465 GLY C 757
REMARK 465 SER C 758
REMARK 465 HIS C 759
REMARK 465 HIS C 760
REMARK 465 HIS C 761
REMARK 465 HIS C 762
REMARK 465 HIS C 763
REMARK 465 HIS C 764
REMARK 465 GLY D 757
REMARK 465 SER D 758
REMARK 465 HIS D 759
REMARK 465 HIS D 760
REMARK 465 HIS D 761
REMARK 465 HIS D 762
REMARK 465 HIS D 763
REMARK 465 HIS D 764
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 DISTANCE
REMARK 500 OH TYR C 105 OE2 GLU C 121 2.03
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 217 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 344 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 368 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 368 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 376 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 376 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 665 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 35 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 376 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 657 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 657 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG C 124 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG D 95 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG D 95 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG D 376 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP D 419 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG D 657 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG D 657 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 41 76.81 61.23
REMARK 500 SER A 58 -126.80 52.63
REMARK 500 ARG A 80 6.69 80.31
REMARK 500 ALA A 157 32.77 -94.37
REMARK 500 ALA A 182 -43.89 70.29
REMARK 500 TYR A 224 30.24 -99.61
REMARK 500 ASP A 300 95.80 -162.45
REMARK 500 ASN A 357 67.72 -166.23
REMARK 500 ALA A 394 -113.49 -130.42
REMARK 500 TYR A 408 -9.00 -54.27
REMARK 500 TYR A 448 -54.16 -133.01
REMARK 500 ASP A 477 67.51 64.43
REMARK 500 PRO A 547 68.05 -59.41
REMARK 500 ASP A 551 43.15 -100.23
REMARK 500 ASP A 599 -79.49 -137.87
REMARK 500 LEU A 607 50.25 -108.93
REMARK 500 GLU A 609 42.80 -82.11
REMARK 500 GLU A 610 7.07 -157.87
REMARK 500 LYS A 742 -98.03 -159.21
REMARK 500 LYS A 750 71.35 41.72
REMARK 500 VAL B 41 73.87 66.61
REMARK 500 ALA B 52 123.94 -36.15
REMARK 500 SER B 58 -132.19 52.36
REMARK 500 ALA B 182 -38.74 72.14
REMARK 500 SER B 251 2.93 -69.32
REMARK 500 ASP B 300 88.89 -153.50
REMARK 500 LEU B 332 52.74 -117.97
REMARK 500 ASN B 357 71.29 -162.54
REMARK 500 ALA B 394 -110.92 -125.75
REMARK 500 TYR B 448 -49.56 -133.78
REMARK 500 ASP B 477 72.34 60.10
REMARK 500 ASP B 599 -76.60 -138.26
REMARK 500 LYS B 742 65.82 -177.43
REMARK 500 VAL C 41 73.75 58.56
REMARK 500 CYS C 43 -60.91 -27.95
REMARK 500 SER C 58 -126.62 54.53
REMARK 500 ALA C 182 -50.03 77.05
REMARK 500 ASN C 210 29.17 49.33
REMARK 500 SER C 251 6.45 -64.25
REMARK 500 ASN C 255 -3.36 -141.88
REMARK 500 VAL C 256 -45.19 60.34
REMARK 500 ASN C 357 71.66 -157.31
REMARK 500 ALA C 394 -110.31 -123.18
REMARK 500 TYR C 448 -46.85 -134.09
REMARK 500 ASP C 477 73.80 70.11
REMARK 500 ASP C 599 -74.67 -136.48
REMARK 500 GLU C 609 2.33 -66.03
REMARK 500 ASP C 698 32.47 -94.01
REMARK 500 GLU C 709 -65.14 -21.53
REMARK 500 LYS C 742 134.92 117.56
REMARK 500
REMARK 500 THIS ENTRY HAS 73 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 551 LYS A 552 146.48
REMARK 500 ASN C 255 VAL C 256 148.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WIQ RELATED DB: PDB
DBREF 3WIR A 1 756 UNP A4XGP2 A4XGP2_CALS8 1 756
DBREF 3WIR B 1 756 UNP A4XGP2 A4XGP2_CALS8 1 756
DBREF 3WIR C 1 756 UNP A4XGP2 A4XGP2_CALS8 1 756
DBREF 3WIR D 1 756 UNP A4XGP2 A4XGP2_CALS8 1 756
SEQADV 3WIR GLY A 757 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR SER A 758 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS A 759 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS A 760 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS A 761 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS A 762 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS A 763 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS A 764 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR GLY B 757 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR SER B 758 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS B 759 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS B 760 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS B 761 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS B 762 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS B 763 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS B 764 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR GLY C 757 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR SER C 758 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS C 759 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS C 760 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS C 761 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS C 762 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS C 763 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS C 764 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR GLY D 757 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR SER D 758 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS D 759 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS D 760 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS D 761 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS D 762 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS D 763 UNP A4XGP2 EXPRESSION TAG
SEQADV 3WIR HIS D 764 UNP A4XGP2 EXPRESSION TAG
SEQRES 1 A 764 MET LYS LEU SER GLU ARG GLU TRP LEU ILE GLU GLN ASP
SEQRES 2 A 764 LYS LEU GLU ALA SER GLY LYS PHE GLU THR CYS PHE ALA
SEQRES 3 A 764 LEU THR ASN GLY TYR ILE GLY ILE ARG GLY ILE ASN GLU
SEQRES 4 A 764 GLU VAL PHE CYS GLU GLU THR PRO GLY THR TYR ILE ALA
SEQRES 5 A 764 GLY VAL PHE ASP LYS SER THR ALA GLN VAL THR GLU LEU
SEQRES 6 A 764 VAL ASN LEU PRO ASN PRO ILE GLY LEU ARG ILE TYR ILE
SEQRES 7 A 764 ASN ARG GLU PHE LEU ASN PRO LEU LYS CYS GLU ILE LEU
SEQRES 8 A 764 GLU PHE LYS ARG VAL LEU ASP LEU LYS GLN GLY ILE LEU
SEQRES 9 A 764 TYR ARG LYS LEU ARG LEU LYS ASP VAL LYS GLY ARG ILE
SEQRES 10 A 764 THR THR ILE GLU GLY PHE ARG PHE VAL SER MET ASN ASN
SEQRES 11 A 764 LYS ASN LEU ILE VAL GLN LYS TYR ASP VAL VAL CYS GLU
SEQRES 12 A 764 ASN TYR SER ALA VAL LEU ASN VAL GLU SER PHE ILE ASP
SEQRES 13 A 764 ALA THR THR VAL ASN SER LYS ASP VAL PRO ASN ASP ARG
SEQRES 14 A 764 VAL LYS HIS TYR GLU ILE ASP LYS LYS LYS ASP PHE ALA
SEQRES 15 A 764 ASP GLY ILE TYR LEU GLY ILE THR THR LYS ASP LYS LYS
SEQRES 16 A 764 TYR LYS VAL GLY ILE ALA SER SER THR LYS VAL LEU LEU
SEQRES 17 A 764 ASN ASN GLN ARG CYS TYR PHE ASN ARG PHE THR LYS ASP
SEQRES 18 A 764 LEU GLY TYR ILE ILE THR GLU ASN PHE GLU VAL GLU ALA
SEQRES 19 A 764 LYS GLN GLY GLU ARG TYR GLU ILE GLU LYS LEU THR VAL
SEQRES 20 A 764 LEU VAL SER SER ARG GLU LYS ASN VAL GLY ASP VAL PHE
SEQRES 21 A 764 GLU THR CYS THR ASN LYS LEU LYS GLU PHE GLU THR LYS
SEQRES 22 A 764 SER ALA GLU LYS LEU LEU PHE GLU HIS ILE GLU GLU TYR
SEQRES 23 A 764 LYS ARG LEU TRP ASP VAL ALA ASN ILE ASP ILE VAL GLY
SEQRES 24 A 764 ASP GLU VAL ALA ASN LYS SER VAL LYS PHE ASN ILE PHE
SEQRES 25 A 764 HIS LEU ILE SER MET ALA ASN PRO GLU ASP GLU HIS VAL
SEQRES 26 A 764 SER LEU GLY ALA LYS GLY LEU HIS GLY GLU GLY TYR LYS
SEQRES 27 A 764 GLY HIS VAL PHE TRP ASP THR GLU ILE PHE MET LEU PRO
SEQRES 28 A 764 PHE TYR ILE TYR THR ASN PRO ALA ALA ALA LYS ALA MET
SEQRES 29 A 764 LEU MET TYR ARG TYR ASN LEU LEU ASP ALA ALA ARG GLU
SEQRES 30 A 764 ASN ALA ARG LYS ASN GLY TYR LYS GLY ALA GLN PHE PRO
SEQRES 31 A 764 TRP GLU SER ALA ASP THR GLY GLU GLU GLU THR PRO LYS
SEQRES 32 A 764 TRP GLY TYR ASP TYR LEU GLY ASN PRO VAL ARG ILE TRP
SEQRES 33 A 764 THR GLY ASP ILE GLU TYR HIS ILE SER ALA ASP ILE ALA
SEQRES 34 A 764 TYR ALA VAL MET ASN TYR VAL ARG ALA THR ASP ASP ILE
SEQRES 35 A 764 ASP PHE LEU LEU ASN TYR GLY SER GLU ILE ILE ILE GLU
SEQRES 36 A 764 THR ALA ARG PHE TRP ALA SER ILE CYS LYS TYR ASN LYS
SEQRES 37 A 764 GLU LYS GLY ARG TYR GLU ILE ASN ASP VAL ILE GLY PRO
SEQRES 38 A 764 ASP GLU PHE HIS GLU HIS CYS ASN ASN ASN ALA TYR THR
SEQRES 39 A 764 ASN TYR LEU ALA LYS TRP ASN LEU LEU LYS ALA SER GLU
SEQRES 40 A 764 LEU CYS ASN LEU LEU LEU GLU LYS TYR PRO LYS TYR PHE
SEQRES 41 A 764 GLU LYS LEU SER LYS LYS ILE ASN LEU SER ASP GLU GLU
SEQRES 42 A 764 PRO PHE VAL TRP GLN GLU ILE ALA SER LYS ILE TYR ILE
SEQRES 43 A 764 PRO TYR HIS PRO ASP LYS LYS LEU ILE GLU GLN PHE GLU
SEQRES 44 A 764 GLY TYR PHE ASN LEU LYS ASP PHE VAL ILE LYS GLU TYR
SEQRES 45 A 764 ASP GLN ASN ASN MET PRO VAL TRP PRO GLU GLY VAL GLU
SEQRES 46 A 764 LEU ASP LYS LEU ASN ASN TYR GLN LEU ILE LYS GLN ALA
SEQRES 47 A 764 ASP VAL VAL MET LEU LEU TYR LEU LEU GLY GLU GLU PHE
SEQRES 48 A 764 ASP ASP GLN THR LYS LYS ILE ASN TYR ASP TYR TYR GLU
SEQRES 49 A 764 LYS ARG THR MET HIS LYS SER SER LEU SER PRO SER ILE
SEQRES 50 A 764 TYR ALA LEU MET GLY VAL ARG VAL GLY GLU THR ASN ARG
SEQRES 51 A 764 ALA TYR ILE ASN PHE MET ARG THR ALA LEU THR ASP LEU
SEQRES 52 A 764 GLU ASP ASN GLN GLY ASN THR HIS LEU GLY ILE HIS ALA
SEQRES 53 A 764 ALA SER LEU GLY GLY THR TRP GLN ALA LEU VAL PHE GLY
SEQRES 54 A 764 PHE GLY GLY ILE SER ILE GLU LYS ASP ASP VAL LEU SER
SEQRES 55 A 764 VAL ASN PRO TRP LEU PRO GLU LYS TRP GLU SER LEU LYS
SEQRES 56 A 764 PHE SER ILE TRP TRP LYS GLY ASN LEU LEU ASP PHE LYS
SEQRES 57 A 764 ILE THR LYS ASP ASN VAL GLU VAL LYS LYS ARG VAL GLU
SEQRES 58 A 764 LYS GLY ASN VAL LYS LEU LYS ILE LYS GLY GLN GLU ALA
SEQRES 59 A 764 ILE ILE GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 764 MET LYS LEU SER GLU ARG GLU TRP LEU ILE GLU GLN ASP
SEQRES 2 B 764 LYS LEU GLU ALA SER GLY LYS PHE GLU THR CYS PHE ALA
SEQRES 3 B 764 LEU THR ASN GLY TYR ILE GLY ILE ARG GLY ILE ASN GLU
SEQRES 4 B 764 GLU VAL PHE CYS GLU GLU THR PRO GLY THR TYR ILE ALA
SEQRES 5 B 764 GLY VAL PHE ASP LYS SER THR ALA GLN VAL THR GLU LEU
SEQRES 6 B 764 VAL ASN LEU PRO ASN PRO ILE GLY LEU ARG ILE TYR ILE
SEQRES 7 B 764 ASN ARG GLU PHE LEU ASN PRO LEU LYS CYS GLU ILE LEU
SEQRES 8 B 764 GLU PHE LYS ARG VAL LEU ASP LEU LYS GLN GLY ILE LEU
SEQRES 9 B 764 TYR ARG LYS LEU ARG LEU LYS ASP VAL LYS GLY ARG ILE
SEQRES 10 B 764 THR THR ILE GLU GLY PHE ARG PHE VAL SER MET ASN ASN
SEQRES 11 B 764 LYS ASN LEU ILE VAL GLN LYS TYR ASP VAL VAL CYS GLU
SEQRES 12 B 764 ASN TYR SER ALA VAL LEU ASN VAL GLU SER PHE ILE ASP
SEQRES 13 B 764 ALA THR THR VAL ASN SER LYS ASP VAL PRO ASN ASP ARG
SEQRES 14 B 764 VAL LYS HIS TYR GLU ILE ASP LYS LYS LYS ASP PHE ALA
SEQRES 15 B 764 ASP GLY ILE TYR LEU GLY ILE THR THR LYS ASP LYS LYS
SEQRES 16 B 764 TYR LYS VAL GLY ILE ALA SER SER THR LYS VAL LEU LEU
SEQRES 17 B 764 ASN ASN GLN ARG CYS TYR PHE ASN ARG PHE THR LYS ASP
SEQRES 18 B 764 LEU GLY TYR ILE ILE THR GLU ASN PHE GLU VAL GLU ALA
SEQRES 19 B 764 LYS GLN GLY GLU ARG TYR GLU ILE GLU LYS LEU THR VAL
SEQRES 20 B 764 LEU VAL SER SER ARG GLU LYS ASN VAL GLY ASP VAL PHE
SEQRES 21 B 764 GLU THR CYS THR ASN LYS LEU LYS GLU PHE GLU THR LYS
SEQRES 22 B 764 SER ALA GLU LYS LEU LEU PHE GLU HIS ILE GLU GLU TYR
SEQRES 23 B 764 LYS ARG LEU TRP ASP VAL ALA ASN ILE ASP ILE VAL GLY
SEQRES 24 B 764 ASP GLU VAL ALA ASN LYS SER VAL LYS PHE ASN ILE PHE
SEQRES 25 B 764 HIS LEU ILE SER MET ALA ASN PRO GLU ASP GLU HIS VAL
SEQRES 26 B 764 SER LEU GLY ALA LYS GLY LEU HIS GLY GLU GLY TYR LYS
SEQRES 27 B 764 GLY HIS VAL PHE TRP ASP THR GLU ILE PHE MET LEU PRO
SEQRES 28 B 764 PHE TYR ILE TYR THR ASN PRO ALA ALA ALA LYS ALA MET
SEQRES 29 B 764 LEU MET TYR ARG TYR ASN LEU LEU ASP ALA ALA ARG GLU
SEQRES 30 B 764 ASN ALA ARG LYS ASN GLY TYR LYS GLY ALA GLN PHE PRO
SEQRES 31 B 764 TRP GLU SER ALA ASP THR GLY GLU GLU GLU THR PRO LYS
SEQRES 32 B 764 TRP GLY TYR ASP TYR LEU GLY ASN PRO VAL ARG ILE TRP
SEQRES 33 B 764 THR GLY ASP ILE GLU TYR HIS ILE SER ALA ASP ILE ALA
SEQRES 34 B 764 TYR ALA VAL MET ASN TYR VAL ARG ALA THR ASP ASP ILE
SEQRES 35 B 764 ASP PHE LEU LEU ASN TYR GLY SER GLU ILE ILE ILE GLU
SEQRES 36 B 764 THR ALA ARG PHE TRP ALA SER ILE CYS LYS TYR ASN LYS
SEQRES 37 B 764 GLU LYS GLY ARG TYR GLU ILE ASN ASP VAL ILE GLY PRO
SEQRES 38 B 764 ASP GLU PHE HIS GLU HIS CYS ASN ASN ASN ALA TYR THR
SEQRES 39 B 764 ASN TYR LEU ALA LYS TRP ASN LEU LEU LYS ALA SER GLU
SEQRES 40 B 764 LEU CYS ASN LEU LEU LEU GLU LYS TYR PRO LYS TYR PHE
SEQRES 41 B 764 GLU LYS LEU SER LYS LYS ILE ASN LEU SER ASP GLU GLU
SEQRES 42 B 764 PRO PHE VAL TRP GLN GLU ILE ALA SER LYS ILE TYR ILE
SEQRES 43 B 764 PRO TYR HIS PRO ASP LYS LYS LEU ILE GLU GLN PHE GLU
SEQRES 44 B 764 GLY TYR PHE ASN LEU LYS ASP PHE VAL ILE LYS GLU TYR
SEQRES 45 B 764 ASP GLN ASN ASN MET PRO VAL TRP PRO GLU GLY VAL GLU
SEQRES 46 B 764 LEU ASP LYS LEU ASN ASN TYR GLN LEU ILE LYS GLN ALA
SEQRES 47 B 764 ASP VAL VAL MET LEU LEU TYR LEU LEU GLY GLU GLU PHE
SEQRES 48 B 764 ASP ASP GLN THR LYS LYS ILE ASN TYR ASP TYR TYR GLU
SEQRES 49 B 764 LYS ARG THR MET HIS LYS SER SER LEU SER PRO SER ILE
SEQRES 50 B 764 TYR ALA LEU MET GLY VAL ARG VAL GLY GLU THR ASN ARG
SEQRES 51 B 764 ALA TYR ILE ASN PHE MET ARG THR ALA LEU THR ASP LEU
SEQRES 52 B 764 GLU ASP ASN GLN GLY ASN THR HIS LEU GLY ILE HIS ALA
SEQRES 53 B 764 ALA SER LEU GLY GLY THR TRP GLN ALA LEU VAL PHE GLY
SEQRES 54 B 764 PHE GLY GLY ILE SER ILE GLU LYS ASP ASP VAL LEU SER
SEQRES 55 B 764 VAL ASN PRO TRP LEU PRO GLU LYS TRP GLU SER LEU LYS
SEQRES 56 B 764 PHE SER ILE TRP TRP LYS GLY ASN LEU LEU ASP PHE LYS
SEQRES 57 B 764 ILE THR LYS ASP ASN VAL GLU VAL LYS LYS ARG VAL GLU
SEQRES 58 B 764 LYS GLY ASN VAL LYS LEU LYS ILE LYS GLY GLN GLU ALA
SEQRES 59 B 764 ILE ILE GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 C 764 MET LYS LEU SER GLU ARG GLU TRP LEU ILE GLU GLN ASP
SEQRES 2 C 764 LYS LEU GLU ALA SER GLY LYS PHE GLU THR CYS PHE ALA
SEQRES 3 C 764 LEU THR ASN GLY TYR ILE GLY ILE ARG GLY ILE ASN GLU
SEQRES 4 C 764 GLU VAL PHE CYS GLU GLU THR PRO GLY THR TYR ILE ALA
SEQRES 5 C 764 GLY VAL PHE ASP LYS SER THR ALA GLN VAL THR GLU LEU
SEQRES 6 C 764 VAL ASN LEU PRO ASN PRO ILE GLY LEU ARG ILE TYR ILE
SEQRES 7 C 764 ASN ARG GLU PHE LEU ASN PRO LEU LYS CYS GLU ILE LEU
SEQRES 8 C 764 GLU PHE LYS ARG VAL LEU ASP LEU LYS GLN GLY ILE LEU
SEQRES 9 C 764 TYR ARG LYS LEU ARG LEU LYS ASP VAL LYS GLY ARG ILE
SEQRES 10 C 764 THR THR ILE GLU GLY PHE ARG PHE VAL SER MET ASN ASN
SEQRES 11 C 764 LYS ASN LEU ILE VAL GLN LYS TYR ASP VAL VAL CYS GLU
SEQRES 12 C 764 ASN TYR SER ALA VAL LEU ASN VAL GLU SER PHE ILE ASP
SEQRES 13 C 764 ALA THR THR VAL ASN SER LYS ASP VAL PRO ASN ASP ARG
SEQRES 14 C 764 VAL LYS HIS TYR GLU ILE ASP LYS LYS LYS ASP PHE ALA
SEQRES 15 C 764 ASP GLY ILE TYR LEU GLY ILE THR THR LYS ASP LYS LYS
SEQRES 16 C 764 TYR LYS VAL GLY ILE ALA SER SER THR LYS VAL LEU LEU
SEQRES 17 C 764 ASN ASN GLN ARG CYS TYR PHE ASN ARG PHE THR LYS ASP
SEQRES 18 C 764 LEU GLY TYR ILE ILE THR GLU ASN PHE GLU VAL GLU ALA
SEQRES 19 C 764 LYS GLN GLY GLU ARG TYR GLU ILE GLU LYS LEU THR VAL
SEQRES 20 C 764 LEU VAL SER SER ARG GLU LYS ASN VAL GLY ASP VAL PHE
SEQRES 21 C 764 GLU THR CYS THR ASN LYS LEU LYS GLU PHE GLU THR LYS
SEQRES 22 C 764 SER ALA GLU LYS LEU LEU PHE GLU HIS ILE GLU GLU TYR
SEQRES 23 C 764 LYS ARG LEU TRP ASP VAL ALA ASN ILE ASP ILE VAL GLY
SEQRES 24 C 764 ASP GLU VAL ALA ASN LYS SER VAL LYS PHE ASN ILE PHE
SEQRES 25 C 764 HIS LEU ILE SER MET ALA ASN PRO GLU ASP GLU HIS VAL
SEQRES 26 C 764 SER LEU GLY ALA LYS GLY LEU HIS GLY GLU GLY TYR LYS
SEQRES 27 C 764 GLY HIS VAL PHE TRP ASP THR GLU ILE PHE MET LEU PRO
SEQRES 28 C 764 PHE TYR ILE TYR THR ASN PRO ALA ALA ALA LYS ALA MET
SEQRES 29 C 764 LEU MET TYR ARG TYR ASN LEU LEU ASP ALA ALA ARG GLU
SEQRES 30 C 764 ASN ALA ARG LYS ASN GLY TYR LYS GLY ALA GLN PHE PRO
SEQRES 31 C 764 TRP GLU SER ALA ASP THR GLY GLU GLU GLU THR PRO LYS
SEQRES 32 C 764 TRP GLY TYR ASP TYR LEU GLY ASN PRO VAL ARG ILE TRP
SEQRES 33 C 764 THR GLY ASP ILE GLU TYR HIS ILE SER ALA ASP ILE ALA
SEQRES 34 C 764 TYR ALA VAL MET ASN TYR VAL ARG ALA THR ASP ASP ILE
SEQRES 35 C 764 ASP PHE LEU LEU ASN TYR GLY SER GLU ILE ILE ILE GLU
SEQRES 36 C 764 THR ALA ARG PHE TRP ALA SER ILE CYS LYS TYR ASN LYS
SEQRES 37 C 764 GLU LYS GLY ARG TYR GLU ILE ASN ASP VAL ILE GLY PRO
SEQRES 38 C 764 ASP GLU PHE HIS GLU HIS CYS ASN ASN ASN ALA TYR THR
SEQRES 39 C 764 ASN TYR LEU ALA LYS TRP ASN LEU LEU LYS ALA SER GLU
SEQRES 40 C 764 LEU CYS ASN LEU LEU LEU GLU LYS TYR PRO LYS TYR PHE
SEQRES 41 C 764 GLU LYS LEU SER LYS LYS ILE ASN LEU SER ASP GLU GLU
SEQRES 42 C 764 PRO PHE VAL TRP GLN GLU ILE ALA SER LYS ILE TYR ILE
SEQRES 43 C 764 PRO TYR HIS PRO ASP LYS LYS LEU ILE GLU GLN PHE GLU
SEQRES 44 C 764 GLY TYR PHE ASN LEU LYS ASP PHE VAL ILE LYS GLU TYR
SEQRES 45 C 764 ASP GLN ASN ASN MET PRO VAL TRP PRO GLU GLY VAL GLU
SEQRES 46 C 764 LEU ASP LYS LEU ASN ASN TYR GLN LEU ILE LYS GLN ALA
SEQRES 47 C 764 ASP VAL VAL MET LEU LEU TYR LEU LEU GLY GLU GLU PHE
SEQRES 48 C 764 ASP ASP GLN THR LYS LYS ILE ASN TYR ASP TYR TYR GLU
SEQRES 49 C 764 LYS ARG THR MET HIS LYS SER SER LEU SER PRO SER ILE
SEQRES 50 C 764 TYR ALA LEU MET GLY VAL ARG VAL GLY GLU THR ASN ARG
SEQRES 51 C 764 ALA TYR ILE ASN PHE MET ARG THR ALA LEU THR ASP LEU
SEQRES 52 C 764 GLU ASP ASN GLN GLY ASN THR HIS LEU GLY ILE HIS ALA
SEQRES 53 C 764 ALA SER LEU GLY GLY THR TRP GLN ALA LEU VAL PHE GLY
SEQRES 54 C 764 PHE GLY GLY ILE SER ILE GLU LYS ASP ASP VAL LEU SER
SEQRES 55 C 764 VAL ASN PRO TRP LEU PRO GLU LYS TRP GLU SER LEU LYS
SEQRES 56 C 764 PHE SER ILE TRP TRP LYS GLY ASN LEU LEU ASP PHE LYS
SEQRES 57 C 764 ILE THR LYS ASP ASN VAL GLU VAL LYS LYS ARG VAL GLU
SEQRES 58 C 764 LYS GLY ASN VAL LYS LEU LYS ILE LYS GLY GLN GLU ALA
SEQRES 59 C 764 ILE ILE GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 D 764 MET LYS LEU SER GLU ARG GLU TRP LEU ILE GLU GLN ASP
SEQRES 2 D 764 LYS LEU GLU ALA SER GLY LYS PHE GLU THR CYS PHE ALA
SEQRES 3 D 764 LEU THR ASN GLY TYR ILE GLY ILE ARG GLY ILE ASN GLU
SEQRES 4 D 764 GLU VAL PHE CYS GLU GLU THR PRO GLY THR TYR ILE ALA
SEQRES 5 D 764 GLY VAL PHE ASP LYS SER THR ALA GLN VAL THR GLU LEU
SEQRES 6 D 764 VAL ASN LEU PRO ASN PRO ILE GLY LEU ARG ILE TYR ILE
SEQRES 7 D 764 ASN ARG GLU PHE LEU ASN PRO LEU LYS CYS GLU ILE LEU
SEQRES 8 D 764 GLU PHE LYS ARG VAL LEU ASP LEU LYS GLN GLY ILE LEU
SEQRES 9 D 764 TYR ARG LYS LEU ARG LEU LYS ASP VAL LYS GLY ARG ILE
SEQRES 10 D 764 THR THR ILE GLU GLY PHE ARG PHE VAL SER MET ASN ASN
SEQRES 11 D 764 LYS ASN LEU ILE VAL GLN LYS TYR ASP VAL VAL CYS GLU
SEQRES 12 D 764 ASN TYR SER ALA VAL LEU ASN VAL GLU SER PHE ILE ASP
SEQRES 13 D 764 ALA THR THR VAL ASN SER LYS ASP VAL PRO ASN ASP ARG
SEQRES 14 D 764 VAL LYS HIS TYR GLU ILE ASP LYS LYS LYS ASP PHE ALA
SEQRES 15 D 764 ASP GLY ILE TYR LEU GLY ILE THR THR LYS ASP LYS LYS
SEQRES 16 D 764 TYR LYS VAL GLY ILE ALA SER SER THR LYS VAL LEU LEU
SEQRES 17 D 764 ASN ASN GLN ARG CYS TYR PHE ASN ARG PHE THR LYS ASP
SEQRES 18 D 764 LEU GLY TYR ILE ILE THR GLU ASN PHE GLU VAL GLU ALA
SEQRES 19 D 764 LYS GLN GLY GLU ARG TYR GLU ILE GLU LYS LEU THR VAL
SEQRES 20 D 764 LEU VAL SER SER ARG GLU LYS ASN VAL GLY ASP VAL PHE
SEQRES 21 D 764 GLU THR CYS THR ASN LYS LEU LYS GLU PHE GLU THR LYS
SEQRES 22 D 764 SER ALA GLU LYS LEU LEU PHE GLU HIS ILE GLU GLU TYR
SEQRES 23 D 764 LYS ARG LEU TRP ASP VAL ALA ASN ILE ASP ILE VAL GLY
SEQRES 24 D 764 ASP GLU VAL ALA ASN LYS SER VAL LYS PHE ASN ILE PHE
SEQRES 25 D 764 HIS LEU ILE SER MET ALA ASN PRO GLU ASP GLU HIS VAL
SEQRES 26 D 764 SER LEU GLY ALA LYS GLY LEU HIS GLY GLU GLY TYR LYS
SEQRES 27 D 764 GLY HIS VAL PHE TRP ASP THR GLU ILE PHE MET LEU PRO
SEQRES 28 D 764 PHE TYR ILE TYR THR ASN PRO ALA ALA ALA LYS ALA MET
SEQRES 29 D 764 LEU MET TYR ARG TYR ASN LEU LEU ASP ALA ALA ARG GLU
SEQRES 30 D 764 ASN ALA ARG LYS ASN GLY TYR LYS GLY ALA GLN PHE PRO
SEQRES 31 D 764 TRP GLU SER ALA ASP THR GLY GLU GLU GLU THR PRO LYS
SEQRES 32 D 764 TRP GLY TYR ASP TYR LEU GLY ASN PRO VAL ARG ILE TRP
SEQRES 33 D 764 THR GLY ASP ILE GLU TYR HIS ILE SER ALA ASP ILE ALA
SEQRES 34 D 764 TYR ALA VAL MET ASN TYR VAL ARG ALA THR ASP ASP ILE
SEQRES 35 D 764 ASP PHE LEU LEU ASN TYR GLY SER GLU ILE ILE ILE GLU
SEQRES 36 D 764 THR ALA ARG PHE TRP ALA SER ILE CYS LYS TYR ASN LYS
SEQRES 37 D 764 GLU LYS GLY ARG TYR GLU ILE ASN ASP VAL ILE GLY PRO
SEQRES 38 D 764 ASP GLU PHE HIS GLU HIS CYS ASN ASN ASN ALA TYR THR
SEQRES 39 D 764 ASN TYR LEU ALA LYS TRP ASN LEU LEU LYS ALA SER GLU
SEQRES 40 D 764 LEU CYS ASN LEU LEU LEU GLU LYS TYR PRO LYS TYR PHE
SEQRES 41 D 764 GLU LYS LEU SER LYS LYS ILE ASN LEU SER ASP GLU GLU
SEQRES 42 D 764 PRO PHE VAL TRP GLN GLU ILE ALA SER LYS ILE TYR ILE
SEQRES 43 D 764 PRO TYR HIS PRO ASP LYS LYS LEU ILE GLU GLN PHE GLU
SEQRES 44 D 764 GLY TYR PHE ASN LEU LYS ASP PHE VAL ILE LYS GLU TYR
SEQRES 45 D 764 ASP GLN ASN ASN MET PRO VAL TRP PRO GLU GLY VAL GLU
SEQRES 46 D 764 LEU ASP LYS LEU ASN ASN TYR GLN LEU ILE LYS GLN ALA
SEQRES 47 D 764 ASP VAL VAL MET LEU LEU TYR LEU LEU GLY GLU GLU PHE
SEQRES 48 D 764 ASP ASP GLN THR LYS LYS ILE ASN TYR ASP TYR TYR GLU
SEQRES 49 D 764 LYS ARG THR MET HIS LYS SER SER LEU SER PRO SER ILE
SEQRES 50 D 764 TYR ALA LEU MET GLY VAL ARG VAL GLY GLU THR ASN ARG
SEQRES 51 D 764 ALA TYR ILE ASN PHE MET ARG THR ALA LEU THR ASP LEU
SEQRES 52 D 764 GLU ASP ASN GLN GLY ASN THR HIS LEU GLY ILE HIS ALA
SEQRES 53 D 764 ALA SER LEU GLY GLY THR TRP GLN ALA LEU VAL PHE GLY
SEQRES 54 D 764 PHE GLY GLY ILE SER ILE GLU LYS ASP ASP VAL LEU SER
SEQRES 55 D 764 VAL ASN PRO TRP LEU PRO GLU LYS TRP GLU SER LEU LYS
SEQRES 56 D 764 PHE SER ILE TRP TRP LYS GLY ASN LEU LEU ASP PHE LYS
SEQRES 57 D 764 ILE THR LYS ASP ASN VAL GLU VAL LYS LYS ARG VAL GLU
SEQRES 58 D 764 LYS GLY ASN VAL LYS LEU LYS ILE LYS GLY GLN GLU ALA
SEQRES 59 D 764 ILE ILE GLY SER HIS HIS HIS HIS HIS HIS
HET BGC A 801 12
HET BGC A 802 12
HET GOL A 803 6
HET GOL A 804 6
HET PO4 A 805 5
HET BGC B 801 12
HET BGC B 802 12
HET GOL B 803 6
HET PO4 B 804 5
HET PO4 B 805 5
HET BGC C 801 12
HET BGC C 802 12
HET GOL C 803 6
HET GOL C 804 6
HET PO4 C 805 5
HET PO4 C 806 5
HET BGC D 801 12
HET BGC D 802 12
HET GOL D 803 6
HET GOL D 804 6
HET GOL D 805 6
HET GOL D 806 6
HET PO4 D 807 5
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 BGC 8(C6 H12 O6)
FORMUL 7 GOL 9(C3 H8 O3)
FORMUL 9 PO4 6(O4 P 3-)
FORMUL 28 HOH *1378(H2 O)
HELIX 1 1 GLU A 5 GLU A 7 5 3
HELIX 2 2 SER A 18 PHE A 25 1 8
HELIX 3 3 ASN A 84 CYS A 88 5 5
HELIX 4 4 ASP A 258 GLU A 271 1 14
HELIX 5 5 SER A 274 ASN A 294 1 21
HELIX 6 6 ASP A 300 ALA A 318 1 19
HELIX 7 7 GLU A 335 HIS A 340 5 6
HELIX 8 8 PHE A 342 PHE A 348 1 7
HELIX 9 9 MET A 349 ASN A 357 1 9
HELIX 10 10 ASN A 357 ASN A 370 1 14
HELIX 11 11 LEU A 371 ASN A 382 1 12
HELIX 12 12 TRP A 416 GLU A 421 1 6
HELIX 13 13 HIS A 423 ASP A 440 1 18
HELIX 14 14 ASP A 441 TYR A 448 1 8
HELIX 15 15 TYR A 448 CYS A 464 1 17
HELIX 16 16 ASN A 491 TYR A 516 1 26
HELIX 17 17 TYR A 516 ILE A 527 1 12
HELIX 18 18 GLU A 532 ILE A 544 1 13
HELIX 19 19 GLY A 560 LEU A 564 5 5
HELIX 20 20 LYS A 588 TYR A 592 5 5
HELIX 21 21 ASP A 599 LEU A 607 1 9
HELIX 22 22 ASP A 612 LYS A 625 1 14
HELIX 23 23 LEU A 633 VAL A 645 1 13
HELIX 24 24 THR A 648 LEU A 660 1 13
HELIX 25 25 ASN A 669 GLY A 673 5 5
HELIX 26 26 HIS A 675 GLY A 689 1 15
HELIX 27 27 GLU B 5 GLU B 7 5 3
HELIX 28 28 SER B 18 PHE B 25 1 8
HELIX 29 29 ASN B 84 CYS B 88 5 5
HELIX 30 30 ASP B 258 GLU B 271 1 14
HELIX 31 31 SER B 274 ASN B 294 1 21
HELIX 32 32 ASP B 300 ALA B 318 1 19
HELIX 33 33 GLU B 335 HIS B 340 5 6
HELIX 34 34 PHE B 342 PHE B 348 1 7
HELIX 35 35 MET B 349 ASN B 357 1 9
HELIX 36 36 ASN B 357 ASN B 370 1 14
HELIX 37 37 LEU B 371 ASN B 382 1 12
HELIX 38 38 TRP B 416 GLU B 421 1 6
HELIX 39 39 HIS B 423 ASP B 440 1 18
HELIX 40 40 ASP B 441 TYR B 448 1 8
HELIX 41 41 TYR B 448 CYS B 464 1 17
HELIX 42 42 ASN B 491 TYR B 516 1 26
HELIX 43 43 TYR B 516 ASN B 528 1 13
HELIX 44 44 GLU B 532 ILE B 544 1 13
HELIX 45 45 GLY B 560 LEU B 564 5 5
HELIX 46 46 LYS B 588 TYR B 592 5 5
HELIX 47 47 ASP B 599 LEU B 607 1 9
HELIX 48 48 GLY B 608 PHE B 611 5 4
HELIX 49 49 ASP B 612 LYS B 625 1 14
HELIX 50 50 LEU B 633 VAL B 645 1 13
HELIX 51 51 ARG B 650 LEU B 660 1 11
HELIX 52 52 ASN B 669 GLY B 673 5 5
HELIX 53 53 HIS B 675 GLY B 689 1 15
HELIX 54 54 GLU C 5 GLU C 7 5 3
HELIX 55 55 SER C 18 PHE C 25 1 8
HELIX 56 56 ASN C 84 CYS C 88 5 5
HELIX 57 57 ASP C 258 THR C 272 1 15
HELIX 58 58 SER C 274 ASN C 294 1 21
HELIX 59 59 ASP C 300 ALA C 318 1 19
HELIX 60 60 GLU C 335 HIS C 340 5 6
HELIX 61 61 PHE C 342 PHE C 348 1 7
HELIX 62 62 MET C 349 ASN C 357 1 9
HELIX 63 63 ASN C 357 LEU C 371 1 15
HELIX 64 64 LEU C 371 ASN C 382 1 12
HELIX 65 65 TRP C 416 GLU C 421 1 6
HELIX 66 66 HIS C 423 ASP C 440 1 18
HELIX 67 67 ASP C 441 TYR C 448 1 8
HELIX 68 68 TYR C 448 CYS C 464 1 17
HELIX 69 69 ASN C 491 TYR C 516 1 26
HELIX 70 70 TYR C 516 ASN C 528 1 13
HELIX 71 71 GLU C 532 LYS C 543 1 12
HELIX 72 72 GLY C 560 LEU C 564 5 5
HELIX 73 73 LYS C 588 TYR C 592 5 5
HELIX 74 74 ASP C 599 LEU C 607 1 9
HELIX 75 75 GLY C 608 PHE C 611 5 4
HELIX 76 76 ASP C 612 LYS C 625 1 14
HELIX 77 77 LEU C 633 VAL C 645 1 13
HELIX 78 78 ARG C 650 LEU C 660 1 11
HELIX 79 79 ASN C 669 GLY C 673 5 5
HELIX 80 80 HIS C 675 PHE C 688 1 14
HELIX 81 81 GLU D 5 GLU D 7 5 3
HELIX 82 82 SER D 18 PHE D 25 1 8
HELIX 83 83 ASN D 84 CYS D 88 5 5
HELIX 84 84 VAL D 259 GLU D 271 1 13
HELIX 85 85 SER D 274 ASN D 294 1 21
HELIX 86 86 ASP D 300 ALA D 318 1 19
HELIX 87 87 GLU D 335 HIS D 340 5 6
HELIX 88 88 PHE D 342 PHE D 348 1 7
HELIX 89 89 MET D 349 ASN D 357 1 9
HELIX 90 90 ASN D 357 LEU D 371 1 15
HELIX 91 91 LEU D 371 ASN D 382 1 12
HELIX 92 92 TRP D 416 GLU D 421 1 6
HELIX 93 93 HIS D 423 ASP D 440 1 18
HELIX 94 94 ASP D 441 TYR D 448 1 8
HELIX 95 95 TYR D 448 CYS D 464 1 17
HELIX 96 96 ASN D 491 TYR D 516 1 26
HELIX 97 97 TYR D 516 ASN D 528 1 13
HELIX 98 98 GLU D 532 ILE D 544 1 13
HELIX 99 99 GLY D 560 LEU D 564 5 5
HELIX 100 100 LYS D 588 TYR D 592 5 5
HELIX 101 101 ASP D 599 LEU D 607 1 9
HELIX 102 102 GLY D 608 PHE D 611 5 4
HELIX 103 103 ASP D 612 LYS D 625 1 14
HELIX 104 104 LEU D 633 VAL D 645 1 13
HELIX 105 105 GLU D 647 ASN D 649 5 3
HELIX 106 106 ARG D 650 LEU D 660 1 11
HELIX 107 107 ASN D 669 GLY D 673 5 5
HELIX 108 108 HIS D 675 GLY D 689 1 15
SHEET 1 A 9 LEU A 9 GLN A 12 0
SHEET 2 A 9 GLU A 89 ASP A 98 -1 O ARG A 95 N GLN A 12
SHEET 3 A 9 ILE A 103 LYS A 111 -1 O LYS A 111 N GLU A 89
SHEET 4 A 9 ILE A 117 VAL A 126 -1 O THR A 118 N LEU A 110
SHEET 5 A 9 LEU A 133 CYS A 142 -1 O VAL A 141 N THR A 119
SHEET 6 A 9 TYR A 240 SER A 250 -1 O ILE A 242 N TYR A 138
SHEET 7 A 9 LYS A 197 LEU A 208 -1 N ALA A 201 O VAL A 247
SHEET 8 A 9 ILE A 185 THR A 191 -1 N ILE A 185 O SER A 202
SHEET 9 A 9 TYR A 173 ASP A 180 -1 N ASP A 176 O GLY A 188
SHEET 1 B 8 LEU A 9 GLN A 12 0
SHEET 2 B 8 GLU A 89 ASP A 98 -1 O ARG A 95 N GLN A 12
SHEET 3 B 8 ILE A 103 LYS A 111 -1 O LYS A 111 N GLU A 89
SHEET 4 B 8 ILE A 117 VAL A 126 -1 O THR A 118 N LEU A 110
SHEET 5 B 8 LEU A 133 CYS A 142 -1 O VAL A 141 N THR A 119
SHEET 6 B 8 TYR A 240 SER A 250 -1 O ILE A 242 N TYR A 138
SHEET 7 B 8 LYS A 197 LEU A 208 -1 N ALA A 201 O VAL A 247
SHEET 8 B 8 GLN A 211 ARG A 212 -1 O GLN A 211 N LEU A 208
SHEET 1 C 3 LEU A 27 THR A 28 0
SHEET 2 C 3 ILE A 32 ILE A 34 -1 O ILE A 34 N LEU A 27
SHEET 3 C 3 THR A 49 ILE A 51 -1 O TYR A 50 N GLY A 33
SHEET 1 D 2 PHE A 55 ASP A 56 0
SHEET 2 D 2 GLU A 64 LEU A 65 -1 O GLU A 64 N ASP A 56
SHEET 1 E 5 GLU A 81 PHE A 82 0
SHEET 2 E 5 ASN A 70 ILE A 78 -1 N ILE A 78 O GLU A 81
SHEET 3 E 5 ALA A 147 ASP A 156 -1 O GLU A 152 N ARG A 75
SHEET 4 E 5 ILE A 225 ALA A 234 -1 O GLU A 228 N SER A 153
SHEET 5 E 5 ASN A 216 ASP A 221 -1 N PHE A 218 O ASN A 229
SHEET 1 F 4 ASP A 296 VAL A 298 0
SHEET 2 F 4 SER A 713 TRP A 720 -1 O LYS A 715 N ASP A 296
SHEET 3 F 4 ASN A 723 THR A 730 -1 O PHE A 727 N PHE A 716
SHEET 4 F 4 VAL A 734 VAL A 740 -1 O ARG A 739 N LEU A 724
SHEET 1 G 2 TRP A 404 TYR A 406 0
SHEET 2 G 2 PRO A 412 ARG A 414 -1 O VAL A 413 N GLY A 405
SHEET 1 H 2 LYS A 465 ASN A 467 0
SHEET 2 H 2 ARG A 472 GLU A 474 -1 O ARG A 472 N ASN A 467
SHEET 1 I 2 ASN A 476 VAL A 478 0
SHEET 2 I 2 CYS A 488 ASN A 489 -1 O CYS A 488 N VAL A 478
SHEET 1 J 2 TYR A 548 HIS A 549 0
SHEET 2 J 2 LEU A 554 ILE A 555 -1 O LEU A 554 N HIS A 549
SHEET 1 K 4 ILE A 693 GLU A 696 0
SHEET 2 K 4 VAL A 700 VAL A 703 -1 O SER A 702 N SER A 694
SHEET 3 K 4 LYS A 746 ILE A 749 1 O LYS A 746 N LEU A 701
SHEET 4 K 4 GLN A 752 ALA A 754 -1 O GLN A 752 N ILE A 749
SHEET 1 L 9 LEU B 9 GLN B 12 0
SHEET 2 L 9 GLU B 89 ASP B 98 -1 O LEU B 97 N ILE B 10
SHEET 3 L 9 ILE B 103 LYS B 111 -1 O LYS B 111 N GLU B 89
SHEET 4 L 9 ILE B 117 VAL B 126 -1 O THR B 118 N LEU B 110
SHEET 5 L 9 LEU B 133 CYS B 142 -1 O VAL B 135 N PHE B 125
SHEET 6 L 9 TYR B 240 SER B 250 -1 O ILE B 242 N TYR B 138
SHEET 7 L 9 LYS B 197 LEU B 207 -1 N LEU B 207 O GLU B 241
SHEET 8 L 9 ILE B 185 THR B 191 -1 N ILE B 189 O VAL B 198
SHEET 9 L 9 TYR B 173 ASP B 180 -1 N LYS B 179 O TYR B 186
SHEET 1 M 3 LEU B 27 THR B 28 0
SHEET 2 M 3 ILE B 32 ILE B 34 -1 O ILE B 34 N LEU B 27
SHEET 3 M 3 THR B 49 ILE B 51 -1 O TYR B 50 N GLY B 33
SHEET 1 N 2 PHE B 55 ASP B 56 0
SHEET 2 N 2 GLU B 64 LEU B 65 -1 O GLU B 64 N ASP B 56
SHEET 1 O 5 GLU B 81 PHE B 82 0
SHEET 2 O 5 ASN B 70 ILE B 78 -1 N ILE B 78 O GLU B 81
SHEET 3 O 5 ALA B 147 ASP B 156 -1 O ASP B 156 N ASN B 70
SHEET 4 O 5 ILE B 225 ALA B 234 -1 O VAL B 232 N LEU B 149
SHEET 5 O 5 ASN B 216 ASP B 221 -1 N ASN B 216 O GLU B 231
SHEET 1 P 4 ASP B 296 VAL B 298 0
SHEET 2 P 4 SER B 713 TRP B 720 -1 O SER B 713 N VAL B 298
SHEET 3 P 4 ASN B 723 THR B 730 -1 O PHE B 727 N PHE B 716
SHEET 4 P 4 VAL B 734 VAL B 740 -1 O ARG B 739 N LEU B 724
SHEET 1 Q 2 TRP B 404 TYR B 406 0
SHEET 2 Q 2 PRO B 412 ARG B 414 -1 O VAL B 413 N GLY B 405
SHEET 1 R 2 LYS B 465 ASN B 467 0
SHEET 2 R 2 ARG B 472 GLU B 474 -1 O ARG B 472 N ASN B 467
SHEET 1 S 2 ASN B 476 VAL B 478 0
SHEET 2 S 2 CYS B 488 ASN B 489 -1 O CYS B 488 N VAL B 478
SHEET 1 T 2 TYR B 548 HIS B 549 0
SHEET 2 T 2 LEU B 554 ILE B 555 -1 O LEU B 554 N HIS B 549
SHEET 1 U 4 ILE B 693 ILE B 695 0
SHEET 2 U 4 VAL B 700 VAL B 703 -1 O SER B 702 N SER B 694
SHEET 3 U 4 LYS B 746 ILE B 749 1 O LYS B 746 N LEU B 701
SHEET 4 U 4 GLN B 752 ALA B 754 -1 O GLN B 752 N ILE B 749
SHEET 1 V 9 LEU C 9 GLU C 11 0
SHEET 2 V 9 GLU C 89 ASP C 98 -1 O LEU C 97 N ILE C 10
SHEET 3 V 9 ILE C 103 LYS C 111 -1 O LYS C 111 N GLU C 89
SHEET 4 V 9 ILE C 117 VAL C 126 -1 O ILE C 120 N LEU C 108
SHEET 5 V 9 LEU C 133 CYS C 142 -1 O ASP C 139 N GLU C 121
SHEET 6 V 9 TYR C 240 SER C 250 -1 O LYS C 244 N GLN C 136
SHEET 7 V 9 LYS C 197 LEU C 208 -1 N GLY C 199 O VAL C 249
SHEET 8 V 9 ILE C 185 THR C 191 -1 N ILE C 189 O VAL C 198
SHEET 9 V 9 TYR C 173 ASP C 180 -1 N GLU C 174 O THR C 190
SHEET 1 W 8 LEU C 9 GLU C 11 0
SHEET 2 W 8 GLU C 89 ASP C 98 -1 O LEU C 97 N ILE C 10
SHEET 3 W 8 ILE C 103 LYS C 111 -1 O LYS C 111 N GLU C 89
SHEET 4 W 8 ILE C 117 VAL C 126 -1 O ILE C 120 N LEU C 108
SHEET 5 W 8 LEU C 133 CYS C 142 -1 O ASP C 139 N GLU C 121
SHEET 6 W 8 TYR C 240 SER C 250 -1 O LYS C 244 N GLN C 136
SHEET 7 W 8 LYS C 197 LEU C 208 -1 N GLY C 199 O VAL C 249
SHEET 8 W 8 GLN C 211 ARG C 212 -1 O GLN C 211 N LEU C 208
SHEET 1 X 3 LEU C 27 THR C 28 0
SHEET 2 X 3 ILE C 32 ILE C 34 -1 O ILE C 34 N LEU C 27
SHEET 3 X 3 THR C 49 ILE C 51 -1 O TYR C 50 N GLY C 33
SHEET 1 Y 2 PHE C 55 ASP C 56 0
SHEET 2 Y 2 GLU C 64 LEU C 65 -1 O GLU C 64 N ASP C 56
SHEET 1 Z 5 GLU C 81 PHE C 82 0
SHEET 2 Z 5 ASN C 70 ILE C 78 -1 N ILE C 78 O GLU C 81
SHEET 3 Z 5 ALA C 147 ASP C 156 -1 O GLU C 152 N ARG C 75
SHEET 4 Z 5 ILE C 225 ALA C 234 -1 O GLU C 228 N SER C 153
SHEET 5 Z 5 ASN C 216 ASP C 221 -1 N ASN C 216 O GLU C 231
SHEET 1 AA 4 ASP C 296 VAL C 298 0
SHEET 2 AA 4 SER C 713 TRP C 720 -1 O SER C 713 N VAL C 298
SHEET 3 AA 4 ASN C 723 THR C 730 -1 O LEU C 725 N ILE C 718
SHEET 4 AA 4 VAL C 734 LYS C 738 -1 O LYS C 737 N ASP C 726
SHEET 1 AB 2 TRP C 404 TYR C 406 0
SHEET 2 AB 2 PRO C 412 ARG C 414 -1 O VAL C 413 N GLY C 405
SHEET 1 AC 2 LYS C 465 ASN C 467 0
SHEET 2 AC 2 ARG C 472 GLU C 474 -1 O ARG C 472 N ASN C 467
SHEET 1 AD 2 ASN C 476 VAL C 478 0
SHEET 2 AD 2 CYS C 488 ASN C 489 -1 O CYS C 488 N VAL C 478
SHEET 1 AE 2 TYR C 548 HIS C 549 0
SHEET 2 AE 2 LEU C 554 ILE C 555 -1 O LEU C 554 N HIS C 549
SHEET 1 AF 4 ILE C 693 GLU C 696 0
SHEET 2 AF 4 VAL C 700 VAL C 703 -1 O SER C 702 N SER C 694
SHEET 3 AF 4 VAL C 745 ILE C 749 1 O LYS C 748 N VAL C 703
SHEET 4 AF 4 GLN C 752 ILE C 756 -1 O ALA C 754 N LEU C 747
SHEET 1 AG 9 LEU D 9 GLN D 12 0
SHEET 2 AG 9 GLU D 89 ASP D 98 -1 O LEU D 97 N ILE D 10
SHEET 3 AG 9 ILE D 103 LYS D 111 -1 O LYS D 111 N GLU D 89
SHEET 4 AG 9 ILE D 117 VAL D 126 -1 O THR D 118 N LEU D 110
SHEET 5 AG 9 LEU D 133 CYS D 142 -1 O VAL D 141 N THR D 119
SHEET 6 AG 9 TYR D 240 SER D 250 -1 O ILE D 242 N TYR D 138
SHEET 7 AG 9 LYS D 197 LEU D 208 -1 N GLY D 199 O VAL D 249
SHEET 8 AG 9 ILE D 185 THR D 191 -1 N ILE D 185 O SER D 202
SHEET 9 AG 9 TYR D 173 ASP D 180 -1 N LYS D 179 O TYR D 186
SHEET 1 AH 8 LEU D 9 GLN D 12 0
SHEET 2 AH 8 GLU D 89 ASP D 98 -1 O LEU D 97 N ILE D 10
SHEET 3 AH 8 ILE D 103 LYS D 111 -1 O LYS D 111 N GLU D 89
SHEET 4 AH 8 ILE D 117 VAL D 126 -1 O THR D 118 N LEU D 110
SHEET 5 AH 8 LEU D 133 CYS D 142 -1 O VAL D 141 N THR D 119
SHEET 6 AH 8 TYR D 240 SER D 250 -1 O ILE D 242 N TYR D 138
SHEET 7 AH 8 LYS D 197 LEU D 208 -1 N GLY D 199 O VAL D 249
SHEET 8 AH 8 GLN D 211 ARG D 212 -1 O GLN D 211 N LEU D 208
SHEET 1 AI 3 LEU D 27 THR D 28 0
SHEET 2 AI 3 ILE D 32 ILE D 34 -1 O ILE D 34 N LEU D 27
SHEET 3 AI 3 THR D 49 ILE D 51 -1 O TYR D 50 N GLY D 33
SHEET 1 AJ 2 PHE D 55 ASP D 56 0
SHEET 2 AJ 2 GLU D 64 LEU D 65 -1 O GLU D 64 N ASP D 56
SHEET 1 AK 5 GLU D 81 PHE D 82 0
SHEET 2 AK 5 ASN D 70 ILE D 78 -1 N ILE D 78 O GLU D 81
SHEET 3 AK 5 ALA D 147 ASP D 156 -1 O GLU D 152 N ARG D 75
SHEET 4 AK 5 ILE D 225 ALA D 234 -1 O GLU D 228 N SER D 153
SHEET 5 AK 5 ASN D 216 ASP D 221 -1 N ASN D 216 O GLU D 231
SHEET 1 AL 4 ASP D 296 VAL D 298 0
SHEET 2 AL 4 SER D 713 TRP D 720 -1 O SER D 713 N VAL D 298
SHEET 3 AL 4 ASN D 723 THR D 730 -1 O PHE D 727 N PHE D 716
SHEET 4 AL 4 VAL D 734 LYS D 738 -1 O LYS D 737 N ASP D 726
SHEET 1 AM 2 TRP D 404 TYR D 406 0
SHEET 2 AM 2 PRO D 412 ARG D 414 -1 O VAL D 413 N GLY D 405
SHEET 1 AN 2 LYS D 465 ASN D 467 0
SHEET 2 AN 2 ARG D 472 GLU D 474 -1 O ARG D 472 N ASN D 467
SHEET 1 AO 2 VAL D 478 ILE D 479 0
SHEET 2 AO 2 GLU D 486 CYS D 488 -1 O CYS D 488 N VAL D 478
SHEET 1 AP 2 TYR D 548 HIS D 549 0
SHEET 2 AP 2 LEU D 554 ILE D 555 -1 O LEU D 554 N HIS D 549
SHEET 1 AQ 4 ILE D 693 GLU D 696 0
SHEET 2 AQ 4 VAL D 700 VAL D 703 -1 O VAL D 700 N GLU D 696
SHEET 3 AQ 4 LYS D 746 ILE D 749 1 O LYS D 748 N VAL D 703
SHEET 4 AQ 4 GLN D 752 ILE D 755 -1 O ALA D 754 N LEU D 747
SSBOND 1 CYS A 43 CYS C 43 1555 1555 2.61
SSBOND 2 CYS B 43 CYS D 43 1555 1555 2.05
CISPEP 1 PRO A 550 ASP A 551 0 -16.13
CISPEP 2 LYS C 254 ASN C 255 0 -6.57
CRYST1 71.581 104.464 124.164 68.83 86.02 90.06 P 1 4
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 0.013970 0.000014 -0.001049 0.00000
SCALE2 0.000000 0.009573 -0.003718 0.00000
SCALE3 0.000000 0.000000 0.008661 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
