HEADER HYDROLASE 28-MAR-04 1V0F
TITLE ENDOSIALIDASE OF BACTERIOPHAGE K1F IN COMPLEX WITH OLIGOMERIC ALPHA-2,
TITLE 2 8-SIALIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-ALPHA-SIALIDASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 246-911;
COMPND 5 SYNONYM: ENDOSIALIDASE;
COMPND 6 EC: 3.2.1.129;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COLIPHAGE K1F;
SOURCE 3 ORGANISM_TAXID: 344021;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENDOSIALIDASE, POLYSIALIC ACID DEGRADATION, HYDROLASE, GLYCOSIDASE.
EXPDTA X-RAY DIFFRACTION
AUTHOR K.STUMMEYER,A.DICKMANNS,M.MUEHLENHOFF,R.GERADY-SCHAHN,R.FICNER
REVDAT 5 29-JUL-20 1V0F 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 24-FEB-09 1V0F 1 VERSN
REVDAT 3 15-JUN-05 1V0F 1 JRNL
REVDAT 2 22-DEC-04 1V0F 1 JRNL
REVDAT 1 13-DEC-04 1V0F 0
JRNL AUTH K.STUMMEYER,A.DICKMANNS,M.MUEHLENHOFF,R.GERARDY-SCHAHN,
JRNL AUTH 2 R.FICNER
JRNL TITL CRYSTAL STRUCTURE OF THE POLYSIALIC ACID-DEGRADING
JRNL TITL 2 ENDOSIALIDASE OF BACTERIOPHAGE K1F
JRNL REF NAT.STRUCT.MOL.BIOL. V. 12 90 2005
JRNL REFN ISSN 1545-9993
JRNL PMID 15608653
JRNL DOI 10.1038/NSMB874
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.MUHLENHOFF,K.STUMMEYER,M.GROVE,M.SAUERBORN,
REMARK 1 AUTH 2 R.GERARDY-SCHAHN
REMARK 1 TITL PROTEOLYTIC PROCESSING AND OLIGOMERIZATION OF
REMARK 1 TITL 2 BACTERIOPHAGE-DERIVED ENDOSIALIDASES
REMARK 1 REF J.BIOL.CHEM. V. 278 12634 2003
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12556457
REMARK 1 DOI 10.1074/JBC.M212048200
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 3 NUMBER OF REFLECTIONS : 124204
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6565
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 31380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 279
REMARK 3 SOLVENT ATOMS : 921
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50000
REMARK 3 B22 (A**2) : 1.80000
REMARK 3 B33 (A**2) : -2.30000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.321
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.231
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.739
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V0F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1290014867.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9195
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 130540
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.30300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 173.02000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 173.02000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B2080 LIES ON A SPECIAL POSITION.
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 O HOH A 2054 O HOH A 2055 2.10
REMARK 500 O HOH A 2056 O HOH A 2070 2.17
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 ASP A 249 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 253 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 348 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU A 355 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 ASP A 364 CB - CG - OD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP A 420 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 455 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 478 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 545 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 558 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 LEU A 620 CA - CB - CG ANGL. DEV. = 18.7 DEGREES
REMARK 500 ASP A 639 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 741 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 746 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 757 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 795 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 865 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP B 253 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 LEU B 355 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 ASP B 381 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 420 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP B 478 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP B 480 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP B 545 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 558 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP B 588 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU B 607 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 ASP B 612 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU B 620 CA - CB - CG ANGL. DEV. = 18.1 DEGREES
REMARK 500 ASP B 731 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 736 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 741 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 863 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 LEU C 355 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 ASP C 364 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP C 533 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP C 545 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP C 558 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU C 620 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASP C 639 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP C 659 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP C 731 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP C 746 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP D 253 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 LEU D 355 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ASP D 381 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP D 448 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP D 480 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 558 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP D 578 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 88 ANGLE DEVIATIONS.
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 PRO A 284 -167.58 -79.18
REMARK 500 ASP A 321 77.00 -158.64
REMARK 500 GLU A 337 58.40 39.12
REMARK 500 ASN A 338 -9.86 75.64
REMARK 500 SER A 347 -159.88 -131.28
REMARK 500 ARG A 349 -179.59 -170.01
REMARK 500 HIS A 350 84.95 -68.98
REMARK 500 ARG A 354 18.58 57.63
REMARK 500 ASP A 364 36.85 -140.78
REMARK 500 ASN A 495 94.52 -164.38
REMARK 500 ASN A 496 15.59 -67.40
REMARK 500 SER A 528 160.41 79.03
REMARK 500 ASP A 533 -159.56 -164.20
REMARK 500 GLU A 581 67.19 35.71
REMARK 500 HIS A 624 37.32 74.71
REMARK 500 HIS A 628 -6.76 72.56
REMARK 500 TRP A 678 56.64 34.95
REMARK 500 VAL A 704 63.03 32.77
REMARK 500 ASP A 711 -116.88 47.11
REMARK 500 SER A 740 -132.76 53.96
REMARK 500 SER A 806 -13.15 -148.82
REMARK 500 SER A 808 71.57 62.66
REMARK 500 SER A 878 -15.54 76.52
REMARK 500 VAL B 251 -38.15 -132.90
REMARK 500 ASP B 321 79.56 -151.23
REMARK 500 ASN B 338 -5.76 65.21
REMARK 500 SER B 347 -157.10 -137.59
REMARK 500 HIS B 350 83.24 -69.58
REMARK 500 ARG B 354 16.62 57.28
REMARK 500 PRO B 383 30.29 -95.52
REMARK 500 ASN B 397 18.60 59.66
REMARK 500 THR B 465 129.90 -38.24
REMARK 500 ALA B 497 126.75 -39.37
REMARK 500 SER B 528 158.26 80.13
REMARK 500 ASP B 533 -160.14 -168.88
REMARK 500 GLU B 581 67.75 35.74
REMARK 500 HIS B 628 -7.37 72.30
REMARK 500 TRP B 678 51.79 33.77
REMARK 500 VAL B 704 62.17 34.66
REMARK 500 ASP B 711 -116.17 49.02
REMARK 500 SER B 740 -131.79 54.67
REMARK 500 SER B 806 -25.66 -149.06
REMARK 500 SER B 808 70.26 61.47
REMARK 500 SER B 878 -15.88 76.25
REMARK 500 THR B 900 -174.55 -175.27
REMARK 500 VAL C 251 -37.45 -130.78
REMARK 500 ASP C 321 79.12 -157.67
REMARK 500 GLU C 337 60.68 39.46
REMARK 500 ASN C 338 -6.60 71.86
REMARK 500 SER C 347 -158.13 -129.46
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V0E RELATED DB: PDB
REMARK 900 ENDOSIALIDASE OF BACTERIOPHAGE K1F
DBREF 1V0F A 245 245 PDB 1V0F 1V0F 245 245
DBREF 1V0F A 246 910 UNP Q858B1 Q858B1 246 910
DBREF 1V0F B 245 245 PDB 1V0F 1V0F 245 245
DBREF 1V0F B 246 910 UNP Q858B1 Q858B1 246 910
DBREF 1V0F C 245 245 PDB 1V0F 1V0F 245 245
DBREF 1V0F C 246 910 UNP Q858B1 Q858B1 246 910
DBREF 1V0F D 245 245 PDB 1V0F 1V0F 245 245
DBREF 1V0F D 246 910 UNP Q858B1 Q858B1 246 910
DBREF 1V0F E 245 245 PDB 1V0F 1V0F 245 245
DBREF 1V0F E 246 910 UNP Q858B1 Q858B1 246 910
DBREF 1V0F F 245 245 PDB 1V0F 1V0F 245 245
DBREF 1V0F F 246 910 UNP Q858B1 Q858B1 246 910
SEQRES 1 A 666 SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES 2 A 666 LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES 3 A 666 ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES 4 A 666 PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES 5 A 666 GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES 6 A 666 GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES 7 A 666 PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES 8 A 666 TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES 9 A 666 ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES 10 A 666 SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES 11 A 666 LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES 12 A 666 HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES 13 A 666 ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES 14 A 666 THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES 15 A 666 LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES 16 A 666 ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES 17 A 666 VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES 18 A 666 GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES 19 A 666 LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES 20 A 666 SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES 21 A 666 THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES 22 A 666 GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES 23 A 666 THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES 24 A 666 GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES 25 A 666 PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES 26 A 666 GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES 27 A 666 CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES 28 A 666 ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES 29 A 666 ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES 30 A 666 PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES 31 A 666 LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES 32 A 666 ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES 33 A 666 TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES 34 A 666 ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES 35 A 666 ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES 36 A 666 SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES 37 A 666 TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES 38 A 666 PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES 39 A 666 LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES 40 A 666 MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES 41 A 666 ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES 42 A 666 PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES 43 A 666 GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES 44 A 666 ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES 45 A 666 MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES 46 A 666 THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES 47 A 666 GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES 48 A 666 LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES 49 A 666 TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES 50 A 666 LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES 51 A 666 SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES 52 A 666 ILE VAL THR
SEQRES 1 B 666 SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES 2 B 666 LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES 3 B 666 ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES 4 B 666 PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES 5 B 666 GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES 6 B 666 GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES 7 B 666 PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES 8 B 666 TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES 9 B 666 ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES 10 B 666 SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES 11 B 666 LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES 12 B 666 HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES 13 B 666 ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES 14 B 666 THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES 15 B 666 LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES 16 B 666 ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES 17 B 666 VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES 18 B 666 GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES 19 B 666 LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES 20 B 666 SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES 21 B 666 THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES 22 B 666 GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES 23 B 666 THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES 24 B 666 GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES 25 B 666 PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES 26 B 666 GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES 27 B 666 CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES 28 B 666 ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES 29 B 666 ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES 30 B 666 PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES 31 B 666 LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES 32 B 666 ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES 33 B 666 TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES 34 B 666 ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES 35 B 666 ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES 36 B 666 SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES 37 B 666 TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES 38 B 666 PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES 39 B 666 LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES 40 B 666 MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES 41 B 666 ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES 42 B 666 PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES 43 B 666 GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES 44 B 666 ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES 45 B 666 MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES 46 B 666 THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES 47 B 666 GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES 48 B 666 LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES 49 B 666 TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES 50 B 666 LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES 51 B 666 SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES 52 B 666 ILE VAL THR
SEQRES 1 C 666 SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES 2 C 666 LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES 3 C 666 ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES 4 C 666 PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES 5 C 666 GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES 6 C 666 GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES 7 C 666 PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES 8 C 666 TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES 9 C 666 ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES 10 C 666 SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES 11 C 666 LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES 12 C 666 HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES 13 C 666 ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES 14 C 666 THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES 15 C 666 LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES 16 C 666 ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES 17 C 666 VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES 18 C 666 GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES 19 C 666 LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES 20 C 666 SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES 21 C 666 THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES 22 C 666 GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES 23 C 666 THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES 24 C 666 GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES 25 C 666 PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES 26 C 666 GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES 27 C 666 CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES 28 C 666 ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES 29 C 666 ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES 30 C 666 PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES 31 C 666 LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES 32 C 666 ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES 33 C 666 TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES 34 C 666 ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES 35 C 666 ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES 36 C 666 SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES 37 C 666 TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES 38 C 666 PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES 39 C 666 LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES 40 C 666 MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES 41 C 666 ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES 42 C 666 PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES 43 C 666 GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES 44 C 666 ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES 45 C 666 MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES 46 C 666 THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES 47 C 666 GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES 48 C 666 LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES 49 C 666 TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES 50 C 666 LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES 51 C 666 SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES 52 C 666 ILE VAL THR
SEQRES 1 D 666 SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES 2 D 666 LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES 3 D 666 ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES 4 D 666 PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES 5 D 666 GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES 6 D 666 GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES 7 D 666 PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES 8 D 666 TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES 9 D 666 ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES 10 D 666 SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES 11 D 666 LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES 12 D 666 HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES 13 D 666 ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES 14 D 666 THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES 15 D 666 LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES 16 D 666 ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES 17 D 666 VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES 18 D 666 GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES 19 D 666 LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES 20 D 666 SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES 21 D 666 THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES 22 D 666 GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES 23 D 666 THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES 24 D 666 GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES 25 D 666 PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES 26 D 666 GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES 27 D 666 CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES 28 D 666 ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES 29 D 666 ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES 30 D 666 PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES 31 D 666 LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES 32 D 666 ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES 33 D 666 TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES 34 D 666 ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES 35 D 666 ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES 36 D 666 SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES 37 D 666 TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES 38 D 666 PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES 39 D 666 LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES 40 D 666 MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES 41 D 666 ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES 42 D 666 PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES 43 D 666 GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES 44 D 666 ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES 45 D 666 MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES 46 D 666 THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES 47 D 666 GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES 48 D 666 LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES 49 D 666 TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES 50 D 666 LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES 51 D 666 SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES 52 D 666 ILE VAL THR
SEQRES 1 E 666 SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES 2 E 666 LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES 3 E 666 ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES 4 E 666 PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES 5 E 666 GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES 6 E 666 GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES 7 E 666 PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES 8 E 666 TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES 9 E 666 ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES 10 E 666 SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES 11 E 666 LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES 12 E 666 HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES 13 E 666 ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES 14 E 666 THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES 15 E 666 LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES 16 E 666 ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES 17 E 666 VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES 18 E 666 GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES 19 E 666 LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES 20 E 666 SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES 21 E 666 THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES 22 E 666 GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES 23 E 666 THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES 24 E 666 GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES 25 E 666 PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES 26 E 666 GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES 27 E 666 CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES 28 E 666 ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES 29 E 666 ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES 30 E 666 PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES 31 E 666 LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES 32 E 666 ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES 33 E 666 TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES 34 E 666 ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES 35 E 666 ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES 36 E 666 SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES 37 E 666 TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES 38 E 666 PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES 39 E 666 LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES 40 E 666 MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES 41 E 666 ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES 42 E 666 PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES 43 E 666 GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES 44 E 666 ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES 45 E 666 MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES 46 E 666 THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES 47 E 666 GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES 48 E 666 LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES 49 E 666 TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES 50 E 666 LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES 51 E 666 SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES 52 E 666 ILE VAL THR
SEQRES 1 F 666 SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES 2 F 666 LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES 3 F 666 ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES 4 F 666 PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES 5 F 666 GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES 6 F 666 GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES 7 F 666 PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES 8 F 666 TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES 9 F 666 ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES 10 F 666 SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES 11 F 666 LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES 12 F 666 HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES 13 F 666 ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES 14 F 666 THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES 15 F 666 LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES 16 F 666 ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES 17 F 666 VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES 18 F 666 GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES 19 F 666 LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES 20 F 666 SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES 21 F 666 THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES 22 F 666 GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES 23 F 666 THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES 24 F 666 GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES 25 F 666 PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES 26 F 666 GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES 27 F 666 CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES 28 F 666 ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES 29 F 666 ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES 30 F 666 PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES 31 F 666 LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES 32 F 666 ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES 33 F 666 TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES 34 F 666 ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES 35 F 666 ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES 36 F 666 SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES 37 F 666 TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES 38 F 666 PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES 39 F 666 LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES 40 F 666 MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES 41 F 666 ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES 42 F 666 PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES 43 F 666 GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES 44 F 666 ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES 45 F 666 MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES 46 F 666 THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES 47 F 666 GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES 48 F 666 LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES 49 F 666 TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES 50 F 666 LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES 51 F 666 SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES 52 F 666 ILE VAL THR
HET SIA G 1 21
HET SIA G 2 20
HET SIA H 1 21
HET SIA H 2 20
HET SIA I 1 21
HET SIA I 2 20
HET SLB A1685 21
HET PO4 A1686 5
HET SLB B1685 21
HET PO4 B1686 5
HET SLB C1685 21
HET PO4 C1687 5
HET SLB D1685 21
HET PO4 D1687 5
HET SLB E1685 21
HET SLB F1685 21
HET PO4 F1686 5
HET PO4 F1687 5
HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID
HETNAM SLB N-ACETYL-BETA-NEURAMINIC ACID
HETNAM PO4 PHOSPHATE ION
HETSYN SLB BETA-SIALIC ACID
FORMUL 7 SIA 6(C11 H19 N O9)
FORMUL 10 SLB 6(C11 H19 N O9)
FORMUL 11 PO4 6(O4 P 3-)
FORMUL 22 HOH *921(H2 O)
HELIX 1 1 ASP A 254 THR A 265 1 12
HELIX 2 2 ASP A 285 SER A 287 5 3
HELIX 3 3 PRO A 572 GLU A 576 5 5
HELIX 4 4 ASN A 832 GLY A 835 5 4
HELIX 5 5 SER A 847 THR A 850 5 4
HELIX 6 6 ASP B 254 THR B 265 1 12
HELIX 7 7 ASP B 285 SER B 287 5 3
HELIX 8 8 PRO B 572 GLU B 576 5 5
HELIX 9 9 ASN B 832 GLY B 835 5 4
HELIX 10 10 SER B 847 THR B 850 5 4
HELIX 11 11 ASP C 254 THR C 265 1 12
HELIX 12 12 ASP C 285 SER C 287 5 3
HELIX 13 13 PRO C 572 GLU C 576 5 5
HELIX 14 14 ASN C 832 GLY C 835 5 4
HELIX 15 15 SER C 847 THR C 850 5 4
HELIX 16 16 ASP D 254 THR D 265 1 12
HELIX 17 17 ASP D 285 SER D 287 5 3
HELIX 18 18 PRO D 572 GLU D 576 5 5
HELIX 19 19 ASN D 832 GLY D 835 5 4
HELIX 20 20 SER D 847 THR D 850 5 4
HELIX 21 21 ASP E 254 THR E 265 1 12
HELIX 22 22 ASP E 285 SER E 287 5 3
HELIX 23 23 PRO E 572 GLU E 576 5 5
HELIX 24 24 ASN E 832 GLY E 835 5 4
HELIX 25 25 SER E 847 THR E 850 5 4
HELIX 26 26 ASP F 254 THR F 265 1 12
HELIX 27 27 ASP F 285 SER F 287 5 3
HELIX 28 28 PRO F 572 GLU F 576 5 5
HELIX 29 29 ASN F 832 GLY F 835 5 4
HELIX 30 30 SER F 847 THR F 850 5 4
SHEET 1 AA 8 ASP A 249 ASP A 253 0
SHEET 2 AA 8 THR A 277 VAL A 280 1 O THR A 277 N GLY A 250
SHEET 3 AA 8 ARG A 293 TYR A 296 1 O ARG A 293 N TYR A 278
SHEET 4 AA 8 LEU A 304 ALA A 307 -1 O LEU A 304 N TYR A 296
SHEET 5 AA 8 VAL A 686 ASP A 690 1 O ASN A 687 N ALA A 307
SHEET 6 AA 8 ARG A 667 ASN A 674 -1 O THR A 668 N ILE A 688
SHEET 7 AA 8 ASP A 639 SER A 645 -1 O LEU A 640 N LEU A 673
SHEET 8 AA 8 PHE A 633 VAL A 636 -1 O ALA A 634 N ILE A 641
SHEET 1 AB 2 ILE A 271 ASN A 272 0
SHEET 2 AB 2 PHE A 289 ILE A 290 1 N ILE A 290 O ILE A 271
SHEET 1 AC 5 GLY A 703 LYS A 710 0
SHEET 2 AC 5 TYR A 713 GLY A 720 -1 O TYR A 713 N LYS A 710
SHEET 3 AC 5 ASP A 746 LYS A 753 -1 O ASP A 746 N GLY A 720
SHEET 4 AC 5 GLY A 314 LYS A 318 -1 O GLU A 315 N LYS A 751
SHEET 5 AC 5 ARG B 765 TYR B 766 1 O ARG B 765 N LYS A 318
SHEET 1 AD 3 TYR A 325 ALA A 327 0
SHEET 2 AD 3 VAL A 339 SER A 347 -1 O MET A 345 N ALA A 327
SHEET 3 AD 3 PHE A 334 TYR A 336 -1 O PHE A 334 N TYR A 341
SHEET 1 AE 4 TYR A 325 ALA A 327 0
SHEET 2 AE 4 VAL A 339 SER A 347 -1 O MET A 345 N ALA A 327
SHEET 3 AE 4 HIS A 356 SER A 362 -1 O HIS A 356 N GLY A 346
SHEET 4 AE 4 GLU A 373 TRP A 374 -1 O GLU A 373 N TRP A 359
SHEET 1 AF 3 VAL A 385 HIS A 388 0
SHEET 2 AF 3 ARG A 398 THR A 407 -1 O GLU A 404 N HIS A 388
SHEET 3 AF 3 MET A 392 CYS A 395 -1 O GLY A 393 N PHE A 400
SHEET 1 AG 4 VAL A 385 HIS A 388 0
SHEET 2 AG 4 ARG A 398 THR A 407 -1 O GLU A 404 N HIS A 388
SHEET 3 AG 4 LEU A 413 PRO A 422 -1 N THR A 414 O THR A 405
SHEET 4 AG 4 ARG A 513 ASP A 516 -1 O ARG A 513 N ASP A 420
SHEET 1 AH 4 SER A 426 THR A 430 0
SHEET 2 AH 4 ASN A 500 THR A 505 -1 O TRP A 501 N LEU A 429
SHEET 3 AH 4 PHE A 456 SER A 460 -1 O ASN A 458 N GLY A 504
SHEET 4 AH 4 GLY A 469 THR A 472 -1 O GLY A 469 N PHE A 459
SHEET 1 AI 5 THR A 475 ASP A 478 0
SHEET 2 AI 5 ASN A 481 LEU A 485 -1 O ASN A 481 N ASP A 478
SHEET 3 AI 5 TYR A 441 HIS A 445 -1 O ALA A 442 N VAL A 484
SHEET 4 AI 5 ILE A 433 LYS A 435 -1 O THR A 434 N THR A 443
SHEET 5 AI 5 LEU A 494 ASN A 495 -1 O LEU A 494 N LYS A 435
SHEET 1 AJ 4 GLU A 525 THR A 531 0
SHEET 2 AJ 4 PHE A 537 GLN A 543 -1 O ALA A 538 N ALA A 530
SHEET 3 AJ 4 GLU A 550 PHE A 556 -1 O GLU A 550 N GLN A 543
SHEET 4 AJ 4 VAL A 567 GLN A 570 -1 O VAL A 567 N TYR A 555
SHEET 1 AK 4 ALA A 579 TYR A 587 0
SHEET 2 AK 4 VAL A 590 GLY A 597 -1 O VAL A 590 N TYR A 587
SHEET 3 AK 4 SER A 606 SER A 610 -1 O SER A 606 N THR A 595
SHEET 4 AK 4 GLU A 618 ARG A 621 -1 O GLU A 618 N ARG A 609
SHEET 1 AL 5 ARG A 765 TYR A 766 0
SHEET 2 AL 5 GLY C 314 LYS C 318 1 O LEU C 316 N ARG A 765
SHEET 3 AL 5 ASP C 746 LYS C 753 -1 O CYS C 749 N PHE C 317
SHEET 4 AL 5 TYR C 713 GLY C 720 -1 O ILE C 714 N MET C 752
SHEET 5 AL 5 GLY C 703 LYS C 710 -1 O GLY C 703 N GLY C 719
SHEET 1 AM12 PHE A 777 PHE A 778 0
SHEET 2 AM12 ARG A 784 VAL A 786 -1 O THR A 785 N PHE A 777
SHEET 3 AM12 MET C 790 PHE C 792 1 O GLU C 791 N VAL A 786
SHEET 4 AM12 LEU B 796 LEU B 798 1 O GLY B 797 N PHE C 792
SHEET 5 AM12 VAL A 801 ILE A 803 1 O THR A 802 N LEU B 798
SHEET 6 AM12 ARG C 812 MET C 817 1 O GLU C 814 N VAL A 801
SHEET 7 AM12 TYR B 821 LYS B 826 1 O TYR B 821 N SER C 813
SHEET 8 AM12 ARG A 837 CYS A 841 1 O ARG A 837 N GLY B 822
SHEET 9 AM12 GLN A 853 TYR A 857 -1 O ILE A 854 N PHE A 840
SHEET 10 AM12 ARG A 866 ASN A 870 -1 O ARG A 866 N TYR A 857
SHEET 11 AM12 GLU C 873 GLN C 877 1 O GLU C 873 N ILE A 867
SHEET 12 AM12 VAL B 881 PRO B 883 1 O LYS B 882 N PHE C 876
SHEET 1 BA12 PHE B 777 PHE B 778 0
SHEET 2 BA12 ARG B 784 VAL B 786 -1 O THR B 785 N PHE B 777
SHEET 3 BA12 MET A 790 PHE A 792 1 O GLU A 791 N VAL B 786
SHEET 4 BA12 LEU C 796 LEU C 798 1 O GLY C 797 N PHE A 792
SHEET 5 BA12 VAL B 801 ILE B 803 1 O THR B 802 N LEU C 798
SHEET 6 BA12 ARG A 812 MET A 817 1 O GLU A 814 N VAL B 801
SHEET 7 BA12 TYR C 821 LYS C 826 1 O TYR C 821 N SER A 813
SHEET 8 BA12 ARG B 837 CYS B 841 1 O ARG B 837 N GLY C 822
SHEET 9 BA12 GLN B 853 TYR B 857 -1 O ILE B 854 N PHE B 840
SHEET 10 BA12 ARG B 866 ASN B 870 -1 O ARG B 866 N TYR B 857
SHEET 11 BA12 GLU A 873 GLN A 877 1 O GLU A 873 N ILE B 867
SHEET 12 BA12 VAL C 881 PRO C 883 1 O LYS C 882 N PHE A 876
SHEET 1 AN12 VAL A 881 PRO A 883 0
SHEET 2 AN12 GLU B 873 GLN B 877 1 O HIS B 874 N LYS A 882
SHEET 3 AN12 ARG C 866 ASN C 870 1 O ILE C 867 N LEU B 875
SHEET 4 AN12 GLN C 853 TYR C 857 -1 O GLN C 853 N ASN C 870
SHEET 5 AN12 ARG C 837 CYS C 841 -1 O ILE C 838 N LEU C 856
SHEET 6 AN12 TYR A 821 LYS A 826 1 O GLY A 822 N ILE C 839
SHEET 7 AN12 ARG B 812 MET B 817 1 O SER B 813 N PHE A 823
SHEET 8 AN12 VAL C 801 ILE C 803 1 O VAL C 801 N LEU B 816
SHEET 9 AN12 LEU A 796 LEU A 798 1 O LEU A 796 N THR C 802
SHEET 10 AN12 MET B 790 PHE B 792 1 O MET B 790 N GLY A 797
SHEET 11 AN12 ARG C 784 VAL C 786 1 O ARG C 784 N GLU B 791
SHEET 12 AN12 PHE C 777 PHE C 778 -1 O PHE C 777 N THR C 785
SHEET 1 AO 2 TYR A 902 LEU A 903 0
SHEET 2 AO 2 ILE C 908 VAL C 909 1 O ILE C 908 N LEU A 903
SHEET 1 AP 2 ILE A 908 VAL A 909 0
SHEET 2 AP 2 TYR B 902 LEU B 903 1 N LEU B 903 O ILE A 908
SHEET 1 BB 2 ILE B 271 ASN B 272 0
SHEET 2 BB 2 PHE B 289 ILE B 290 1 N ILE B 290 O ILE B 271
SHEET 1 BC 7 THR B 277 VAL B 280 0
SHEET 2 BC 7 ARG B 293 TYR B 296 1 O ARG B 293 N TYR B 278
SHEET 3 BC 7 LEU B 304 ALA B 307 -1 O LEU B 304 N TYR B 296
SHEET 4 BC 7 VAL B 686 ASP B 690 1 O ASN B 687 N ALA B 307
SHEET 5 BC 7 ARG B 667 ASN B 674 -1 O THR B 668 N ILE B 688
SHEET 6 BC 7 ASP B 639 SER B 645 -1 O LEU B 640 N LEU B 673
SHEET 7 BC 7 PHE B 633 VAL B 636 -1 O ALA B 634 N ILE B 641
SHEET 1 BD 5 GLY B 703 LYS B 710 0
SHEET 2 BD 5 TYR B 713 GLY B 720 -1 O TYR B 713 N LYS B 710
SHEET 3 BD 5 ASP B 746 LYS B 753 -1 O ASP B 746 N GLY B 720
SHEET 4 BD 5 GLY B 314 LYS B 318 -1 O GLU B 315 N LYS B 751
SHEET 5 BD 5 ARG C 765 TYR C 766 1 O ARG C 765 N LYS B 318
SHEET 1 BE 3 TYR B 325 ALA B 327 0
SHEET 2 BE 3 VAL B 339 SER B 347 -1 O MET B 345 N ALA B 327
SHEET 3 BE 3 PHE B 334 TYR B 336 -1 O PHE B 334 N TYR B 341
SHEET 1 BF 4 TYR B 325 ALA B 327 0
SHEET 2 BF 4 VAL B 339 SER B 347 -1 O MET B 345 N ALA B 327
SHEET 3 BF 4 HIS B 356 SER B 362 -1 O HIS B 356 N GLY B 346
SHEET 4 BF 4 GLU B 373 TRP B 374 -1 O GLU B 373 N TRP B 359
SHEET 1 BG 7 VAL B 385 HIS B 388 0
SHEET 2 BG 7 ARG B 398 THR B 407 -1 O GLU B 404 N HIS B 388
SHEET 3 BG 7 MET B 392 CYS B 395 -1 O GLY B 393 N PHE B 400
SHEET 4 BG 7 ARG B 398 THR B 407 -1 O ARG B 398 N CYS B 395
SHEET 5 BG 7 ARG B 513 GLY B 518 0
SHEET 6 BG 7 LEU B 413 PRO B 422 -1 O CYS B 416 N LEU B 517
SHEET 7 BG 7 ARG B 398 THR B 407 -1 O LEU B 399 N ARG B 421
SHEET 1 BH 4 SER B 426 THR B 430 0
SHEET 2 BH 4 ASN B 500 THR B 505 -1 O TRP B 501 N LEU B 429
SHEET 3 BH 4 PHE B 456 SER B 460 -1 O ASN B 458 N GLY B 504
SHEET 4 BH 4 GLY B 469 THR B 472 -1 O GLY B 469 N PHE B 459
SHEET 1 BI 5 THR B 475 ASP B 478 0
SHEET 2 BI 5 ASN B 481 LEU B 485 -1 O ASN B 481 N ASP B 478
SHEET 3 BI 5 TYR B 441 HIS B 445 -1 O ALA B 442 N VAL B 484
SHEET 4 BI 5 ILE B 433 LYS B 435 -1 O THR B 434 N THR B 443
SHEET 5 BI 5 LEU B 494 ASN B 495 -1 O LEU B 494 N LYS B 435
SHEET 1 BJ 4 GLU B 525 THR B 531 0
SHEET 2 BJ 4 PHE B 537 GLN B 543 -1 O ALA B 538 N ALA B 530
SHEET 3 BJ 4 GLU B 550 PHE B 556 -1 O GLU B 550 N GLN B 543
SHEET 4 BJ 4 VAL B 567 GLN B 570 -1 O VAL B 567 N TYR B 555
SHEET 1 BK 4 ALA B 579 TYR B 587 0
SHEET 2 BK 4 VAL B 590 GLY B 597 -1 O VAL B 590 N TYR B 587
SHEET 3 BK 4 SER B 606 SER B 610 -1 O SER B 606 N THR B 595
SHEET 4 BK 4 GLU B 618 ARG B 621 -1 O GLU B 618 N ARG B 609
SHEET 1 BL 2 ILE B 908 VAL B 909 0
SHEET 2 BL 2 TYR C 902 LEU C 903 1 N LEU C 903 O ILE B 908
SHEET 1 CA 2 ILE C 271 ASN C 272 0
SHEET 2 CA 2 PHE C 289 ILE C 290 1 N ILE C 290 O ILE C 271
SHEET 1 CB 7 THR C 277 VAL C 280 0
SHEET 2 CB 7 ARG C 293 TYR C 296 1 O ARG C 293 N TYR C 278
SHEET 3 CB 7 LEU C 304 ALA C 307 -1 O LEU C 304 N TYR C 296
SHEET 4 CB 7 VAL C 686 ASP C 690 1 O ASN C 687 N ALA C 307
SHEET 5 CB 7 ARG C 667 ASN C 674 -1 O THR C 668 N ILE C 688
SHEET 6 CB 7 ASP C 639 SER C 645 -1 O LEU C 640 N LEU C 673
SHEET 7 CB 7 PHE C 633 VAL C 636 -1 O ALA C 634 N ILE C 641
SHEET 1 CC 7 TYR C 325 ALA C 327 0
SHEET 2 CC 7 VAL C 339 SER C 347 -1 O MET C 345 N ALA C 327
SHEET 3 CC 7 PHE C 334 TYR C 336 -1 O PHE C 334 N TYR C 341
SHEET 4 CC 7 VAL C 339 SER C 347 -1 O VAL C 339 N TYR C 336
SHEET 5 CC 7 GLU C 373 TRP C 374 0
SHEET 6 CC 7 HIS C 356 SER C 362 -1 O TRP C 359 N GLU C 373
SHEET 7 CC 7 VAL C 339 SER C 347 -1 O ILE C 340 N SER C 362
SHEET 1 CD 7 VAL C 385 HIS C 388 0
SHEET 2 CD 7 ARG C 398 THR C 407 -1 O GLU C 404 N HIS C 388
SHEET 3 CD 7 MET C 392 CYS C 395 -1 O GLY C 393 N PHE C 400
SHEET 4 CD 7 ARG C 398 THR C 407 -1 O ARG C 398 N CYS C 395
SHEET 5 CD 7 ARG C 513 GLY C 518 0
SHEET 6 CD 7 LEU C 413 PRO C 422 -1 O CYS C 416 N LEU C 517
SHEET 7 CD 7 ARG C 398 THR C 407 -1 O LEU C 399 N ARG C 421
SHEET 1 CE 8 SER C 426 THR C 430 0
SHEET 2 CE 8 ASN C 500 THR C 505 -1 O TRP C 501 N LEU C 429
SHEET 3 CE 8 PHE C 456 SER C 460 -1 O ASN C 458 N GLY C 504
SHEET 4 CE 8 GLY C 469 ASP C 478 -1 O GLY C 469 N PHE C 459
SHEET 5 CE 8 ASN C 481 LEU C 485 -1 O ASN C 481 N ASP C 478
SHEET 6 CE 8 TYR C 441 HIS C 445 -1 O ALA C 442 N VAL C 484
SHEET 7 CE 8 ILE C 433 LYS C 435 -1 O THR C 434 N THR C 443
SHEET 8 CE 8 LEU C 494 ASN C 495 -1 O LEU C 494 N LYS C 435
SHEET 1 CF 4 GLU C 525 THR C 531 0
SHEET 2 CF 4 PHE C 537 GLN C 543 -1 O ALA C 538 N ALA C 530
SHEET 3 CF 4 GLU C 550 PHE C 556 -1 O GLU C 550 N GLN C 543
SHEET 4 CF 4 VAL C 567 GLN C 570 -1 O VAL C 567 N TYR C 555
SHEET 1 CG 4 ALA C 579 TYR C 587 0
SHEET 2 CG 4 VAL C 590 GLY C 597 -1 O VAL C 590 N TYR C 587
SHEET 3 CG 4 SER C 606 SER C 610 -1 O SER C 606 N THR C 595
SHEET 4 CG 4 GLU C 618 ARG C 621 -1 O GLU C 618 N ARG C 609
SHEET 1 DA 2 ILE D 271 ASN D 272 0
SHEET 2 DA 2 PHE D 289 ILE D 290 1 N ILE D 290 O ILE D 271
SHEET 1 DB 7 THR D 277 VAL D 280 0
SHEET 2 DB 7 ARG D 293 TYR D 296 1 O ARG D 293 N TYR D 278
SHEET 3 DB 7 LEU D 304 ALA D 307 -1 O LEU D 304 N TYR D 296
SHEET 4 DB 7 VAL D 686 ASP D 690 1 O ASN D 687 N ALA D 307
SHEET 5 DB 7 ARG D 667 ASN D 674 -1 O THR D 668 N ILE D 688
SHEET 6 DB 7 ASP D 639 SER D 645 -1 O LEU D 640 N LEU D 673
SHEET 7 DB 7 PHE D 633 VAL D 636 -1 O ALA D 634 N ILE D 641
SHEET 1 DC 5 GLY D 703 LYS D 710 0
SHEET 2 DC 5 TYR D 713 GLY D 720 -1 O TYR D 713 N LYS D 710
SHEET 3 DC 5 ASP D 746 LYS D 753 -1 O ASP D 746 N GLY D 720
SHEET 4 DC 5 GLY D 314 LYS D 318 -1 O GLU D 315 N LYS D 751
SHEET 5 DC 5 ARG F 765 TYR F 766 1 O ARG F 765 N LYS D 318
SHEET 1 DD 7 TYR D 325 ALA D 327 0
SHEET 2 DD 7 VAL D 339 SER D 347 -1 O MET D 345 N ALA D 327
SHEET 3 DD 7 PHE D 334 TYR D 336 -1 O PHE D 334 N TYR D 341
SHEET 4 DD 7 VAL D 339 SER D 347 -1 O VAL D 339 N TYR D 336
SHEET 5 DD 7 GLU D 373 TRP D 374 0
SHEET 6 DD 7 HIS D 356 SER D 362 -1 O TRP D 359 N GLU D 373
SHEET 7 DD 7 VAL D 339 SER D 347 -1 O ILE D 340 N SER D 362
SHEET 1 DE 7 VAL D 385 HIS D 388 0
SHEET 2 DE 7 ARG D 398 THR D 407 -1 O GLU D 404 N HIS D 388
SHEET 3 DE 7 MET D 392 CYS D 395 -1 O GLY D 393 N PHE D 400
SHEET 4 DE 7 ARG D 398 THR D 407 -1 O ARG D 398 N CYS D 395
SHEET 5 DE 7 ARG D 513 GLY D 518 0
SHEET 6 DE 7 LEU D 413 PRO D 422 -1 O CYS D 416 N LEU D 517
SHEET 7 DE 7 ARG D 398 THR D 407 -1 O LEU D 399 N ARG D 421
SHEET 1 DF 4 SER D 426 THR D 430 0
SHEET 2 DF 4 ASN D 500 THR D 505 -1 O TRP D 501 N LEU D 429
SHEET 3 DF 4 PHE D 456 SER D 460 -1 O ASN D 458 N GLY D 504
SHEET 4 DF 4 GLY D 469 THR D 472 -1 O GLY D 469 N PHE D 459
SHEET 1 DG 5 THR D 475 ASP D 478 0
SHEET 2 DG 5 ASN D 481 LEU D 485 -1 O ASN D 481 N ASP D 478
SHEET 3 DG 5 TYR D 441 HIS D 445 -1 O ALA D 442 N VAL D 484
SHEET 4 DG 5 ILE D 433 LYS D 435 -1 O THR D 434 N THR D 443
SHEET 5 DG 5 LEU D 494 ASN D 495 -1 O LEU D 494 N LYS D 435
SHEET 1 DH 4 GLU D 525 THR D 531 0
SHEET 2 DH 4 PHE D 537 GLN D 543 -1 O ALA D 538 N ALA D 530
SHEET 3 DH 4 GLU D 550 PHE D 556 -1 O GLU D 550 N GLN D 543
SHEET 4 DH 4 VAL D 567 GLN D 570 -1 O VAL D 567 N TYR D 555
SHEET 1 DI 4 ALA D 579 TYR D 587 0
SHEET 2 DI 4 VAL D 590 GLY D 597 -1 O VAL D 590 N TYR D 587
SHEET 3 DI 4 SER D 606 SER D 610 -1 O SER D 606 N THR D 595
SHEET 4 DI 4 GLU D 618 ARG D 621 -1 O GLU D 618 N ARG D 609
SHEET 1 DJ 5 PHE D 764 TYR D 766 0
SHEET 2 DJ 5 GLY E 314 LYS E 318 1 O LEU E 316 N ARG D 765
SHEET 3 DJ 5 ASP E 746 LYS E 753 -1 O CYS E 749 N PHE E 317
SHEET 4 DJ 5 TYR E 713 GLY E 720 -1 O ILE E 714 N MET E 752
SHEET 5 DJ 5 GLY E 703 LYS E 710 -1 O GLY E 703 N GLY E 719
SHEET 1 DK12 PHE D 777 PHE D 778 0
SHEET 2 DK12 ARG D 784 VAL D 786 -1 O THR D 785 N PHE D 777
SHEET 3 DK12 MET E 790 PHE E 792 1 O GLU E 791 N VAL D 786
SHEET 4 DK12 LEU F 796 LEU F 798 1 O GLY F 797 N PHE E 792
SHEET 5 DK12 VAL D 801 ILE D 803 1 O THR D 802 N LEU F 798
SHEET 6 DK12 ARG E 812 MET E 817 1 O GLU E 814 N VAL D 801
SHEET 7 DK12 TYR F 821 LYS F 826 1 O TYR F 821 N SER E 813
SHEET 8 DK12 ARG D 837 CYS D 841 1 O ARG D 837 N GLY F 822
SHEET 9 DK12 GLN D 853 TYR D 857 -1 O ILE D 854 N PHE D 840
SHEET 10 DK12 ARG D 866 ASN D 870 -1 O ARG D 866 N TYR D 857
SHEET 11 DK12 GLU E 873 GLN E 877 1 O GLU E 873 N ILE D 867
SHEET 12 DK12 VAL F 881 PRO F 883 1 O LYS F 882 N PHE E 876
SHEET 1 EA12 VAL E 881 PRO E 883 0
SHEET 2 EA12 GLU D 873 GLN D 877 1 O HIS D 874 N LYS E 882
SHEET 3 EA12 ARG F 866 ASN F 870 1 O ILE F 867 N LEU D 875
SHEET 4 EA12 GLN F 853 TYR F 857 -1 O GLN F 853 N ASN F 870
SHEET 5 EA12 ARG F 837 CYS F 841 -1 O ILE F 838 N LEU F 856
SHEET 6 EA12 TYR E 821 LYS E 826 1 O GLY E 822 N ILE F 839
SHEET 7 EA12 ARG D 812 MET D 817 1 O SER D 813 N PHE E 823
SHEET 8 EA12 VAL F 801 ILE F 803 1 O VAL F 801 N LEU D 816
SHEET 9 EA12 LEU E 796 LEU E 798 1 O LEU E 796 N THR F 802
SHEET 10 EA12 MET D 790 PHE D 792 1 O MET D 790 N GLY E 797
SHEET 11 EA12 ARG F 784 VAL F 786 1 O ARG F 784 N GLU D 791
SHEET 12 EA12 PHE F 777 PHE F 778 -1 O PHE F 777 N THR F 785
SHEET 1 DL12 VAL D 881 PRO D 883 0
SHEET 2 DL12 GLU F 873 GLN F 877 1 O HIS F 874 N LYS D 882
SHEET 3 DL12 ARG E 866 ASN E 870 1 O ILE E 867 N LEU F 875
SHEET 4 DL12 GLN E 853 TYR E 857 -1 O GLN E 853 N ASN E 870
SHEET 5 DL12 ARG E 837 CYS E 841 -1 O ILE E 838 N LEU E 856
SHEET 6 DL12 TYR D 821 LYS D 826 1 O GLY D 822 N ILE E 839
SHEET 7 DL12 ARG F 812 MET F 817 1 O SER F 813 N PHE D 823
SHEET 8 DL12 VAL E 801 ILE E 803 1 O VAL E 801 N LEU F 816
SHEET 9 DL12 LEU D 796 LEU D 798 1 O LEU D 796 N THR E 802
SHEET 10 DL12 MET F 790 PHE F 792 1 O MET F 790 N GLY D 797
SHEET 11 DL12 ARG E 784 VAL E 786 1 O ARG E 784 N GLU F 791
SHEET 12 DL12 PHE E 777 PHE E 778 -1 O PHE E 777 N THR E 785
SHEET 1 DM 2 TYR D 902 LEU D 903 0
SHEET 2 DM 2 ILE E 908 VAL E 909 1 O ILE E 908 N LEU D 903
SHEET 1 DN 2 ILE D 908 VAL D 909 0
SHEET 2 DN 2 TYR F 902 LEU F 903 1 N LEU F 903 O ILE D 908
SHEET 1 EB 2 ILE E 271 ASN E 272 0
SHEET 2 EB 2 PHE E 289 ILE E 290 1 N ILE E 290 O ILE E 271
SHEET 1 EC 7 THR E 277 VAL E 280 0
SHEET 2 EC 7 ARG E 293 TYR E 296 1 O ARG E 293 N TYR E 278
SHEET 3 EC 7 LEU E 304 ALA E 307 -1 O LEU E 304 N TYR E 296
SHEET 4 EC 7 VAL E 686 ASP E 690 1 O ASN E 687 N ALA E 307
SHEET 5 EC 7 ARG E 667 ASN E 674 -1 O THR E 668 N ILE E 688
SHEET 6 EC 7 ASP E 639 SER E 645 -1 O LEU E 640 N LEU E 673
SHEET 7 EC 7 PHE E 633 VAL E 636 -1 O ALA E 634 N ILE E 641
SHEET 1 ED 7 TYR E 325 ALA E 327 0
SHEET 2 ED 7 VAL E 339 SER E 347 -1 O MET E 345 N ALA E 327
SHEET 3 ED 7 PHE E 334 TYR E 336 -1 O PHE E 334 N TYR E 341
SHEET 4 ED 7 VAL E 339 SER E 347 -1 O VAL E 339 N TYR E 336
SHEET 5 ED 7 GLU E 373 TRP E 374 0
SHEET 6 ED 7 HIS E 356 SER E 362 -1 O TRP E 359 N GLU E 373
SHEET 7 ED 7 VAL E 339 SER E 347 -1 O ILE E 340 N SER E 362
SHEET 1 EE 7 VAL E 385 HIS E 388 0
SHEET 2 EE 7 ARG E 398 THR E 407 -1 O GLU E 404 N HIS E 388
SHEET 3 EE 7 MET E 392 CYS E 395 -1 O GLY E 393 N PHE E 400
SHEET 4 EE 7 ARG E 398 THR E 407 -1 O ARG E 398 N CYS E 395
SHEET 5 EE 7 ARG E 513 GLY E 518 0
SHEET 6 EE 7 LEU E 413 PRO E 422 -1 O CYS E 416 N LEU E 517
SHEET 7 EE 7 ARG E 398 THR E 407 -1 O LEU E 399 N ARG E 421
SHEET 1 EF 8 SER E 426 THR E 430 0
SHEET 2 EF 8 ASN E 500 THR E 505 -1 O TRP E 501 N LEU E 429
SHEET 3 EF 8 PHE E 456 SER E 460 -1 O ASN E 458 N GLY E 504
SHEET 4 EF 8 GLY E 469 ASP E 478 -1 O GLY E 469 N PHE E 459
SHEET 5 EF 8 ASN E 481 LEU E 485 -1 O ASN E 481 N ASP E 478
SHEET 6 EF 8 TYR E 441 HIS E 445 -1 O ALA E 442 N VAL E 484
SHEET 7 EF 8 ILE E 433 LYS E 435 -1 O THR E 434 N THR E 443
SHEET 8 EF 8 LEU E 494 ASN E 495 -1 O LEU E 494 N LYS E 435
SHEET 1 EG 4 GLU E 525 THR E 531 0
SHEET 2 EG 4 PHE E 537 GLN E 543 -1 O ALA E 538 N ALA E 530
SHEET 3 EG 4 GLU E 550 PHE E 556 -1 O GLU E 550 N GLN E 543
SHEET 4 EG 4 VAL E 567 GLN E 570 -1 O VAL E 567 N TYR E 555
SHEET 1 EH 4 ALA E 579 TYR E 587 0
SHEET 2 EH 4 VAL E 590 GLY E 597 -1 O VAL E 590 N TYR E 587
SHEET 3 EH 4 SER E 606 SER E 610 -1 O SER E 606 N THR E 595
SHEET 4 EH 4 GLU E 618 ARG E 621 -1 O GLU E 618 N ARG E 609
SHEET 1 EI 5 ARG E 765 TYR E 766 0
SHEET 2 EI 5 GLY F 314 LYS F 318 1 O LEU F 316 N ARG E 765
SHEET 3 EI 5 ASP F 746 LYS F 753 -1 O CYS F 749 N PHE F 317
SHEET 4 EI 5 TYR F 713 GLY F 720 -1 O ILE F 714 N MET F 752
SHEET 5 EI 5 GLY F 703 LYS F 710 -1 O GLY F 703 N GLY F 719
SHEET 1 EJ 2 TYR E 902 LEU E 903 0
SHEET 2 EJ 2 ILE F 908 VAL F 909 1 O ILE F 908 N LEU E 903
SHEET 1 FA 2 ILE F 271 ASN F 272 0
SHEET 2 FA 2 PHE F 289 ILE F 290 1 N ILE F 290 O ILE F 271
SHEET 1 FB 7 THR F 277 VAL F 280 0
SHEET 2 FB 7 ARG F 293 TYR F 296 1 O ARG F 293 N TYR F 278
SHEET 3 FB 7 LEU F 304 ALA F 307 -1 O LEU F 304 N TYR F 296
SHEET 4 FB 7 VAL F 686 ASP F 690 1 O ASN F 687 N ALA F 307
SHEET 5 FB 7 ARG F 667 ASN F 674 -1 O THR F 668 N ILE F 688
SHEET 6 FB 7 ASP F 639 SER F 645 -1 O LEU F 640 N LEU F 673
SHEET 7 FB 7 PHE F 633 VAL F 636 -1 O ALA F 634 N ILE F 641
SHEET 1 FC 7 TYR F 325 ALA F 327 0
SHEET 2 FC 7 VAL F 339 SER F 347 -1 O MET F 345 N ALA F 327
SHEET 3 FC 7 PHE F 334 TYR F 336 -1 O PHE F 334 N TYR F 341
SHEET 4 FC 7 VAL F 339 SER F 347 -1 O VAL F 339 N TYR F 336
SHEET 5 FC 7 GLU F 373 TRP F 374 0
SHEET 6 FC 7 HIS F 356 SER F 362 -1 O TRP F 359 N GLU F 373
SHEET 7 FC 7 VAL F 339 SER F 347 -1 O ILE F 340 N SER F 362
SHEET 1 FD 7 VAL F 385 HIS F 388 0
SHEET 2 FD 7 ARG F 398 THR F 407 -1 O GLU F 404 N HIS F 388
SHEET 3 FD 7 MET F 392 CYS F 395 -1 O GLY F 393 N PHE F 400
SHEET 4 FD 7 ARG F 398 THR F 407 -1 O ARG F 398 N CYS F 395
SHEET 5 FD 7 ARG F 513 GLY F 518 0
SHEET 6 FD 7 LEU F 413 PRO F 422 -1 O CYS F 416 N LEU F 517
SHEET 7 FD 7 ARG F 398 THR F 407 -1 O LEU F 399 N ARG F 421
SHEET 1 FE 4 SER F 426 THR F 430 0
SHEET 2 FE 4 ASN F 500 THR F 505 -1 O TRP F 501 N LEU F 429
SHEET 3 FE 4 PHE F 456 SER F 460 -1 O ASN F 458 N GLY F 504
SHEET 4 FE 4 GLY F 469 THR F 472 -1 O GLY F 469 N PHE F 459
SHEET 1 FF 5 THR F 475 ASP F 478 0
SHEET 2 FF 5 ASN F 481 LEU F 485 -1 O ASN F 481 N ASP F 478
SHEET 3 FF 5 TYR F 441 HIS F 445 -1 O ALA F 442 N VAL F 484
SHEET 4 FF 5 ILE F 433 LYS F 435 -1 O THR F 434 N THR F 443
SHEET 5 FF 5 LEU F 494 ASN F 495 -1 O LEU F 494 N LYS F 435
SHEET 1 FG 4 GLU F 525 THR F 531 0
SHEET 2 FG 4 PHE F 537 GLN F 543 -1 O ALA F 538 N ALA F 530
SHEET 3 FG 4 GLU F 550 PHE F 556 -1 O GLU F 550 N GLN F 543
SHEET 4 FG 4 VAL F 567 GLN F 570 -1 O VAL F 567 N TYR F 555
SHEET 1 FH 4 ALA F 579 TYR F 587 0
SHEET 2 FH 4 VAL F 590 GLY F 597 -1 O VAL F 590 N TYR F 587
SHEET 3 FH 4 SER F 606 SER F 610 -1 O SER F 606 N THR F 595
SHEET 4 FH 4 GLU F 618 ARG F 621 -1 O GLU F 618 N ARG F 609
LINK O8 SIA G 1 C2 SIA G 2 1555 1555 1.42
LINK O8 SIA H 1 C2 SIA H 2 1555 1555 1.43
LINK O8 SIA I 1 C2 SIA I 2 1555 1555 1.44
CISPEP 1 GLN A 330 ASP A 331 0 -20.41
CISPEP 2 TYR A 382 PRO A 383 0 4.79
CISPEP 3 MET A 503 GLY A 504 0 3.94
CISPEP 4 ALA A 547 PRO A 548 0 -4.97
CISPEP 5 GLN B 330 ASP B 331 0 -20.78
CISPEP 6 TYR B 382 PRO B 383 0 2.06
CISPEP 7 MET B 503 GLY B 504 0 2.41
CISPEP 8 ALA B 547 PRO B 548 0 -10.73
CISPEP 9 GLN C 330 ASP C 331 0 -22.13
CISPEP 10 TYR C 382 PRO C 383 0 3.96
CISPEP 11 MET C 503 GLY C 504 0 1.99
CISPEP 12 ALA C 547 PRO C 548 0 -0.09
CISPEP 13 GLN D 330 ASP D 331 0 -21.92
CISPEP 14 TYR D 382 PRO D 383 0 7.55
CISPEP 15 MET D 503 GLY D 504 0 -1.03
CISPEP 16 ALA D 547 PRO D 548 0 -17.85
CISPEP 17 GLN E 330 ASP E 331 0 -19.69
CISPEP 18 TYR E 382 PRO E 383 0 1.47
CISPEP 19 MET E 503 GLY E 504 0 2.88
CISPEP 20 ALA E 547 PRO E 548 0 -8.56
CISPEP 21 GLN F 330 ASP F 331 0 -19.77
CISPEP 22 TYR F 382 PRO F 383 0 9.30
CISPEP 23 MET F 503 GLY F 504 0 -3.03
CISPEP 24 ALA F 547 PRO F 548 0 -2.40
CRYST1 99.540 131.400 346.040 90.00 90.00 90.00 P 2 2 21 24
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 0.010046 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002890 0.00000
MTRIX1 1 -0.498000 -0.451000 -0.740000 108.14800 1
MTRIX2 1 0.460000 0.586000 -0.667000 26.54500 1
MTRIX3 1 0.735000 -0.673000 -0.085000 43.72600 1
MTRIX1 2 -0.506000 0.459000 0.730000 10.26200 1
MTRIX2 2 -0.446000 0.586000 -0.677000 62.39800 1
MTRIX3 2 -0.738000 -0.668000 -0.092000 101.80900 1
MTRIX1 3 -1.000000 0.006000 -0.005000 24.28300 1
MTRIX2 3 -0.005000 -0.958000 -0.287000 21.57800 1
MTRIX3 3 -0.006000 -0.287000 0.958000 3.71300 1
MTRIX1 4 0.505000 -0.453000 -0.735000 14.07900 1
MTRIX2 4 0.645000 -0.367000 0.670000 -67.68800 1
MTRIX3 4 -0.573000 -0.812000 0.107000 82.93200 1
MTRIX1 5 0.498000 0.458000 0.737000 -83.85900 1
MTRIX2 5 -0.650000 -0.366000 0.666000 -16.78500 1
MTRIX3 5 0.574000 -0.810000 0.116000 37.34300 1
(ATOM LINES ARE NOT SHOWN.)
END
