HEADER VIRAL PROTEIN 15-DEC-03 1RVZ
TITLE 1934 H1 HEMAGGLUTININ IN COMPLEX WITH LSTC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMAGGLUTININ;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 OTHER_DETAILS: HEMAGGLUTININ HA1 CHAIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMAGGLUTININ;
COMPND 7 CHAIN: B, D, F, H, J, L;
COMPND 8 OTHER_DETAILS: HEMAGGLUTININ HA2 CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/PUERTO RICO/8/34(H1N1));
SOURCE 3 ORGANISM_TAXID: 211044;
SOURCE 4 STRAIN: A-PUERTO RICO-8-34;
SOURCE 5 OTHER_DETAILS: BROMELAIN DIGESTION;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/PUERTO RICO/8/34(H1N1));
SOURCE 8 ORGANISM_TAXID: 211044;
SOURCE 9 STRAIN: A-PUERTO RICO-8-34;
SOURCE 10 OTHER_DETAILS: BROMELAIN DIGESTION
KEYWDS HEMAGGLUTININ, INFLUENZA A VIRUS, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.GAMBLIN,L.F.HAIRE,R.J.RUSSELL,D.J.STEVENS,B.XIAO,Y.HA,N.VASISHT,
AUTHOR 2 D.A.STEINHAUER,R.S.DANIELS,A.ELLIOT,D.C.WILEY,J.J.SKEHEL
REVDAT 6 23-AUG-23 1RVZ 1 HETSYN
REVDAT 5 29-JUL-20 1RVZ 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 01-FEB-17 1RVZ 1 AUTHOR
REVDAT 3 13-JUL-11 1RVZ 1 VERSN
REVDAT 2 24-FEB-09 1RVZ 1 VERSN
REVDAT 1 30-MAR-04 1RVZ 0
JRNL AUTH S.J.GAMBLIN,L.F.HAIRE,R.J.RUSSELL,D.J.STEVENS,B.XIAO,Y.HA,
JRNL AUTH 2 N.VASISHT,D.A.STEINHAUER,R.S.DANIELS,A.ELLIOT,D.C.WILEY,
JRNL AUTH 3 J.J.SKEHEL
JRNL TITL THE STRUCTURE AND RECEPTOR BINDING PROPERTIES OF THE 1918
JRNL TITL 2 INFLUENZA HEMAGGLUTININ.
JRNL REF SCIENCE V. 303 1838 2004
JRNL REFN ISSN 0036-8075
JRNL PMID 14764886
JRNL DOI 10.1126/SCIENCE.1093155
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 206016
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 10169
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23039
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 315
REMARK 3 SOLVENT ATOMS : 2098
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RVZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 206016
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 11.60
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 52.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1RU7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, TRISHCL, KSCN, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 113.79150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.76100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 113.79150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 65.76100
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 32060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, M, N, O
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L, P, Q, R
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 ALA A 1
REMARK 465 THR A 2
REMARK 465 ASN A 3
REMARK 465 ALA A 4
REMARK 465 ALA C 1
REMARK 465 THR C 2
REMARK 465 ASN C 3
REMARK 465 ALA C 4
REMARK 465 ALA E 1
REMARK 465 THR E 2
REMARK 465 ASN E 3
REMARK 465 ALA E 4
REMARK 465 ALA G 1
REMARK 465 THR G 2
REMARK 465 ASN G 3
REMARK 465 ALA G 4
REMARK 465 ALA I 1
REMARK 465 THR I 2
REMARK 465 ASN I 3
REMARK 465 ALA I 4
REMARK 465 ALA K 1
REMARK 465 THR K 2
REMARK 465 ASN K 3
REMARK 465 ALA K 4
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ALA A 288 CB
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 O4 NAG R 1 O5 GAL R 2 1.93
REMARK 500 O4 NAG N 1 O5 GAL N 2 1.93
REMARK 500 O4 NAG Q 1 O5 GAL Q 2 1.93
REMARK 500 O4 NAG M 1 O5 GAL M 2 1.94
REMARK 500 O4 NAG P 1 O5 GAL P 2 2.01
REMARK 500 O4 NAG O 1 O5 GAL O 2 2.02
REMARK 500 O HOH A 3354 O HOH A 3355 2.07
REMARK 500 NE2 HIS A 141 O HOH A 3354 2.10
REMARK 500 O HOH A 3354 O HOH A 3356 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH K 3421 O HOH K 3421 2555 2.14
REMARK 500 ND1 HIS G 276 O HOH A 3354 2555 2.15
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 CYS J 644 CA - CB - SG ANGL. DEV. = 7.2 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 ASN A 14 -163.53 -163.30
REMARK 500 ASN A 88 30.40 -97.56
REMARK 500 ASN A 91 84.66 -58.35
REMARK 500 TRP A 127 67.52 -118.44
REMARK 500 SER A 146 -158.84 -146.75
REMARK 500 GLN A 196 -56.43 66.27
REMARK 500 ASN A 199 60.96 -114.52
REMARK 500 ALA A 218 149.99 -173.73
REMARK 500 ASN A 250 -2.70 59.43
REMARK 500 ALA B 505 -77.84 -79.41
REMARK 500 ALA B 507 17.36 59.88
REMARK 500 ILE B 510 79.28 -114.44
REMARK 500 ILE B 518 30.59 -144.03
REMARK 500 GLN B 530 5.16 -68.57
REMARK 500 SER B 532 -159.68 -89.47
REMARK 500 LYS B 627 -95.85 49.49
REMARK 500 ILE B 633 -90.29 -115.46
REMARK 500 ASN B 635 111.67 56.85
REMARK 500 LYS B 643 125.60 61.63
REMARK 500 ASN B 654 22.24 -77.52
REMARK 500 THR B 656 -139.32 -80.86
REMARK 500 TYR B 657 89.60 61.96
REMARK 500 ASP B 658 67.22 -116.66
REMARK 500 ASN C 27 65.52 39.60
REMARK 500 SER C 114 163.13 179.89
REMARK 500 SER C 146 -156.96 -146.57
REMARK 500 GLN C 196 -51.71 69.97
REMARK 500 ALA C 218 149.77 -171.55
REMARK 500 ASN C 250 -0.67 62.79
REMARK 500 MET D 559 53.40 -98.30
REMARK 500 ILE D 561 138.34 -33.41
REMARK 500 THR D 564 121.81 -36.16
REMARK 500 LYS D 627 -83.64 -17.59
REMARK 500 ILE D 633 -112.23 -112.66
REMARK 500 ASN D 635 111.22 52.86
REMARK 500 LYS D 643 117.66 62.87
REMARK 500 ASP D 645 -151.85 -43.71
REMARK 500 ASN D 654 24.86 -79.67
REMARK 500 THR D 656 -122.96 -92.89
REMARK 500 TYR D 657 81.04 56.46
REMARK 500 ASP D 658 73.07 -105.04
REMARK 500 ASN E 14 -166.80 -164.29
REMARK 500 LYS E 45 130.11 67.55
REMARK 500 SER E 125 -23.59 123.33
REMARK 500 TRP E 127 73.50 -119.57
REMARK 500 SER E 146 -155.69 -133.36
REMARK 500 GLN E 196 -56.77 62.67
REMARK 500 ASN E 199 68.29 -116.21
REMARK 500 ASN E 250 -2.44 63.83
REMARK 500 ALA F 505 -81.20 -71.20
REMARK 500
REMARK 500 THIS ENTRY HAS 128 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG M 1
REMARK 610 NAG N 1
REMARK 610 NAG O 1
REMARK 610 NAG P 1
REMARK 610 NAG Q 1
REMARK 610 NAG R 1
REMARK 630
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE GLYCAN COMPONENT
REMARK 630 MOLECULE NAME: 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 NAG A 3321
REMARK 630 NAG E 3311
REMARK 630 NAG F 3331
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: OLIGOSACCHARIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RU7 RELATED DB: PDB
REMARK 900 1934 H1 HEMAGGLUTININ
REMARK 900 RELATED ID: 1RUY RELATED DB: PDB
REMARK 900 1930 H1 HEMAGGLUTININ
REMARK 900 RELATED ID: 1RUZ RELATED DB: PDB
REMARK 900 1918 H1 HEMAGGLUTININ
REMARK 900 RELATED ID: 1RV0 RELATED DB: PDB
REMARK 900 1930 H1 HEMAGGLUTININ IN COMPLEX WITH LSTA
REMARK 900 RELATED ID: 1RVT RELATED DB: PDB
REMARK 900 1930 H1 HEMAGGLUTININ IN COMPLEX WITH LSTC
REMARK 900 RELATED ID: 1RVX RELATED DB: PDB
REMARK 900 1934 H1 HEMAGGLUTININ IN COMPLEX WITH LSTA
REMARK 999
REMARK 999 SEQUENCE AUTHOR STATES THAT THE SEQUENCE OF THIS PROTEIN IS
REMARK 999 CORRECT AND THERE IS NO MATCHED SEQUENCE DATABASE AVAILABLE.
REMARK 999 RESIDUE (E ASN 42 ) AND RESIDUE (E GLY 44 ) ARE NOT LINKED,
REMARK 999 DISTANCE OF C-N BOND IS 2.61.
DBREF 1RVZ A 4 325 UNP Q82766 Q82766_9INFA 17 338
DBREF 1RVZ B 501 660 UNP Q82766 Q82766_9INFA 344 503
DBREF 1RVZ C 4 325 UNP Q82766 Q82766_9INFA 17 338
DBREF 1RVZ D 501 660 UNP Q82766 Q82766_9INFA 344 503
DBREF 1RVZ E 4 325 UNP Q82766 Q82766_9INFA 17 338
DBREF 1RVZ F 501 660 UNP Q82766 Q82766_9INFA 344 503
DBREF 1RVZ G 4 325 UNP Q82766 Q82766_9INFA 17 338
DBREF 1RVZ H 501 660 UNP Q82766 Q82766_9INFA 344 503
DBREF 1RVZ I 4 325 UNP Q82766 Q82766_9INFA 17 338
DBREF 1RVZ J 501 660 UNP Q82766 Q82766_9INFA 344 503
DBREF 1RVZ K 4 325 UNP Q82766 Q82766_9INFA 17 338
DBREF 1RVZ L 501 660 UNP Q82766 Q82766_9INFA 344 503
SEQRES 1 A 327 ALA THR ASN ALA ASP THR ILE CYS ILE GLY TYR HIS ALA
SEQRES 2 A 327 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS
SEQRES 3 A 327 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP
SEQRES 4 A 327 SER HIS ASN GLY LYS LEU CYS ARG LEU LYS GLY ILE ALA
SEQRES 5 A 327 PRO LEU GLN LEU GLY LYS CYS ASN ILE ALA GLY TRP LEU
SEQRES 6 A 327 LEU GLY ASN PRO GLU CYS ASP PRO LEU LEU PRO VAL ARG
SEQRES 7 A 327 SER TRP SER TYR ILE VAL GLU THR PRO ASN SER GLU ASN
SEQRES 8 A 327 GLY ILE CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU
SEQRES 9 A 327 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG
SEQRES 10 A 327 PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN HIS
SEQRES 11 A 327 ASN THR ASN GLY VAL THR ALA ALA CYS SER HIS GLU GLY
SEQRES 12 A 327 LYS SER SER PHE TYR ARG ASN LEU LEU TRP LEU THR GLU
SEQRES 13 A 327 LYS GLU GLY SER TYR PRO LYS LEU LYS ASN SER TYR VAL
SEQRES 14 A 327 ASN LYS LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE
SEQRES 15 A 327 HIS HIS PRO PRO ASN SER LYS GLU GLN GLN ASN LEU TYR
SEQRES 16 A 327 GLN ASN GLU ASN ALA TYR VAL SER VAL VAL THR SER ASN
SEQRES 17 A 327 TYR ASN ARG ARG PHE THR PRO GLU ILE ALA GLU ARG PRO
SEQRES 18 A 327 LYS VAL ARG ASP GLN ALA GLY ARG MET ASN TYR TYR TRP
SEQRES 19 A 327 THR LEU LEU LYS PRO GLY ASP THR ILE ILE PHE GLU ALA
SEQRES 20 A 327 ASN GLY ASN LEU ILE ALA PRO MET TYR ALA PHE ALA LEU
SEQRES 21 A 327 ARG ARG GLY PHE GLY SER GLY ILE ILE THR SER ASN ALA
SEQRES 22 A 327 SER MET HIS GLU CYS ASN THR LYS CYS GLN THR PRO LEU
SEQRES 23 A 327 GLY ALA ILE ASN SER SER LEU PRO TYR GLN ASN ILE HIS
SEQRES 24 A 327 PRO VAL THR ILE GLY GLU CYS PRO LYS TYR VAL ARG SER
SEQRES 25 A 327 ALA LYS LEU ARG MET VAL THR GLY LEU ARG ASN ILE PRO
SEQRES 26 A 327 ALA ARG
SEQRES 1 B 160 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY
SEQRES 2 B 160 TRP THR GLY MET ILE ASP GLY TRP TYR GLY TYR HIS HIS
SEQRES 3 B 160 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS
SEQRES 4 B 160 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL
SEQRES 5 B 160 ASN SER VAL ILE GLU LYS MET ASN ILE GLN PHE THR ALA
SEQRES 6 B 160 VAL GLY LYS GLU PHE ASN LYS LEU GLU LYS ARG MET GLU
SEQRES 7 B 160 ASN LEU ASN ASN LYS VAL ASP ASP GLY PHE LEU ASP ILE
SEQRES 8 B 160 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN
SEQRES 9 B 160 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN
SEQRES 10 B 160 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA
SEQRES 11 B 160 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS
SEQRES 12 B 160 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR
SEQRES 13 B 160 TYR ASP TYR PRO
SEQRES 1 C 327 ALA THR ASN ALA ASP THR ILE CYS ILE GLY TYR HIS ALA
SEQRES 2 C 327 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS
SEQRES 3 C 327 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP
SEQRES 4 C 327 SER HIS ASN GLY LYS LEU CYS ARG LEU LYS GLY ILE ALA
SEQRES 5 C 327 PRO LEU GLN LEU GLY LYS CYS ASN ILE ALA GLY TRP LEU
SEQRES 6 C 327 LEU GLY ASN PRO GLU CYS ASP PRO LEU LEU PRO VAL ARG
SEQRES 7 C 327 SER TRP SER TYR ILE VAL GLU THR PRO ASN SER GLU ASN
SEQRES 8 C 327 GLY ILE CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU
SEQRES 9 C 327 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG
SEQRES 10 C 327 PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN HIS
SEQRES 11 C 327 ASN THR ASN GLY VAL THR ALA ALA CYS SER HIS GLU GLY
SEQRES 12 C 327 LYS SER SER PHE TYR ARG ASN LEU LEU TRP LEU THR GLU
SEQRES 13 C 327 LYS GLU GLY SER TYR PRO LYS LEU LYS ASN SER TYR VAL
SEQRES 14 C 327 ASN LYS LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE
SEQRES 15 C 327 HIS HIS PRO PRO ASN SER LYS GLU GLN GLN ASN LEU TYR
SEQRES 16 C 327 GLN ASN GLU ASN ALA TYR VAL SER VAL VAL THR SER ASN
SEQRES 17 C 327 TYR ASN ARG ARG PHE THR PRO GLU ILE ALA GLU ARG PRO
SEQRES 18 C 327 LYS VAL ARG ASP GLN ALA GLY ARG MET ASN TYR TYR TRP
SEQRES 19 C 327 THR LEU LEU LYS PRO GLY ASP THR ILE ILE PHE GLU ALA
SEQRES 20 C 327 ASN GLY ASN LEU ILE ALA PRO MET TYR ALA PHE ALA LEU
SEQRES 21 C 327 ARG ARG GLY PHE GLY SER GLY ILE ILE THR SER ASN ALA
SEQRES 22 C 327 SER MET HIS GLU CYS ASN THR LYS CYS GLN THR PRO LEU
SEQRES 23 C 327 GLY ALA ILE ASN SER SER LEU PRO TYR GLN ASN ILE HIS
SEQRES 24 C 327 PRO VAL THR ILE GLY GLU CYS PRO LYS TYR VAL ARG SER
SEQRES 25 C 327 ALA LYS LEU ARG MET VAL THR GLY LEU ARG ASN ILE PRO
SEQRES 26 C 327 ALA ARG
SEQRES 1 D 160 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY
SEQRES 2 D 160 TRP THR GLY MET ILE ASP GLY TRP TYR GLY TYR HIS HIS
SEQRES 3 D 160 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS
SEQRES 4 D 160 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL
SEQRES 5 D 160 ASN SER VAL ILE GLU LYS MET ASN ILE GLN PHE THR ALA
SEQRES 6 D 160 VAL GLY LYS GLU PHE ASN LYS LEU GLU LYS ARG MET GLU
SEQRES 7 D 160 ASN LEU ASN ASN LYS VAL ASP ASP GLY PHE LEU ASP ILE
SEQRES 8 D 160 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN
SEQRES 9 D 160 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN
SEQRES 10 D 160 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA
SEQRES 11 D 160 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS
SEQRES 12 D 160 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR
SEQRES 13 D 160 TYR ASP TYR PRO
SEQRES 1 E 327 ALA THR ASN ALA ASP THR ILE CYS ILE GLY TYR HIS ALA
SEQRES 2 E 327 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS
SEQRES 3 E 327 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP
SEQRES 4 E 327 SER HIS ASN GLY LYS LEU CYS ARG LEU LYS GLY ILE ALA
SEQRES 5 E 327 PRO LEU GLN LEU GLY LYS CYS ASN ILE ALA GLY TRP LEU
SEQRES 6 E 327 LEU GLY ASN PRO GLU CYS ASP PRO LEU LEU PRO VAL ARG
SEQRES 7 E 327 SER TRP SER TYR ILE VAL GLU THR PRO ASN SER GLU ASN
SEQRES 8 E 327 GLY ILE CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU
SEQRES 9 E 327 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG
SEQRES 10 E 327 PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN HIS
SEQRES 11 E 327 ASN THR ASN GLY VAL THR ALA ALA CYS SER HIS GLU GLY
SEQRES 12 E 327 LYS SER SER PHE TYR ARG ASN LEU LEU TRP LEU THR GLU
SEQRES 13 E 327 LYS GLU GLY SER TYR PRO LYS LEU LYS ASN SER TYR VAL
SEQRES 14 E 327 ASN LYS LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE
SEQRES 15 E 327 HIS HIS PRO PRO ASN SER LYS GLU GLN GLN ASN LEU TYR
SEQRES 16 E 327 GLN ASN GLU ASN ALA TYR VAL SER VAL VAL THR SER ASN
SEQRES 17 E 327 TYR ASN ARG ARG PHE THR PRO GLU ILE ALA GLU ARG PRO
SEQRES 18 E 327 LYS VAL ARG ASP GLN ALA GLY ARG MET ASN TYR TYR TRP
SEQRES 19 E 327 THR LEU LEU LYS PRO GLY ASP THR ILE ILE PHE GLU ALA
SEQRES 20 E 327 ASN GLY ASN LEU ILE ALA PRO MET TYR ALA PHE ALA LEU
SEQRES 21 E 327 ARG ARG GLY PHE GLY SER GLY ILE ILE THR SER ASN ALA
SEQRES 22 E 327 SER MET HIS GLU CYS ASN THR LYS CYS GLN THR PRO LEU
SEQRES 23 E 327 GLY ALA ILE ASN SER SER LEU PRO TYR GLN ASN ILE HIS
SEQRES 24 E 327 PRO VAL THR ILE GLY GLU CYS PRO LYS TYR VAL ARG SER
SEQRES 25 E 327 ALA LYS LEU ARG MET VAL THR GLY LEU ARG ASN ILE PRO
SEQRES 26 E 327 ALA ARG
SEQRES 1 F 160 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY
SEQRES 2 F 160 TRP THR GLY MET ILE ASP GLY TRP TYR GLY TYR HIS HIS
SEQRES 3 F 160 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS
SEQRES 4 F 160 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL
SEQRES 5 F 160 ASN SER VAL ILE GLU LYS MET ASN ILE GLN PHE THR ALA
SEQRES 6 F 160 VAL GLY LYS GLU PHE ASN LYS LEU GLU LYS ARG MET GLU
SEQRES 7 F 160 ASN LEU ASN ASN LYS VAL ASP ASP GLY PHE LEU ASP ILE
SEQRES 8 F 160 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN
SEQRES 9 F 160 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN
SEQRES 10 F 160 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA
SEQRES 11 F 160 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS
SEQRES 12 F 160 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR
SEQRES 13 F 160 TYR ASP TYR PRO
SEQRES 1 G 327 ALA THR ASN ALA ASP THR ILE CYS ILE GLY TYR HIS ALA
SEQRES 2 G 327 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS
SEQRES 3 G 327 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP
SEQRES 4 G 327 SER HIS ASN GLY LYS LEU CYS ARG LEU LYS GLY ILE ALA
SEQRES 5 G 327 PRO LEU GLN LEU GLY LYS CYS ASN ILE ALA GLY TRP LEU
SEQRES 6 G 327 LEU GLY ASN PRO GLU CYS ASP PRO LEU LEU PRO VAL ARG
SEQRES 7 G 327 SER TRP SER TYR ILE VAL GLU THR PRO ASN SER GLU ASN
SEQRES 8 G 327 GLY ILE CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU
SEQRES 9 G 327 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG
SEQRES 10 G 327 PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN HIS
SEQRES 11 G 327 ASN THR ASN GLY VAL THR ALA ALA CYS SER HIS GLU GLY
SEQRES 12 G 327 LYS SER SER PHE TYR ARG ASN LEU LEU TRP LEU THR GLU
SEQRES 13 G 327 LYS GLU GLY SER TYR PRO LYS LEU LYS ASN SER TYR VAL
SEQRES 14 G 327 ASN LYS LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE
SEQRES 15 G 327 HIS HIS PRO PRO ASN SER LYS GLU GLN GLN ASN LEU TYR
SEQRES 16 G 327 GLN ASN GLU ASN ALA TYR VAL SER VAL VAL THR SER ASN
SEQRES 17 G 327 TYR ASN ARG ARG PHE THR PRO GLU ILE ALA GLU ARG PRO
SEQRES 18 G 327 LYS VAL ARG ASP GLN ALA GLY ARG MET ASN TYR TYR TRP
SEQRES 19 G 327 THR LEU LEU LYS PRO GLY ASP THR ILE ILE PHE GLU ALA
SEQRES 20 G 327 ASN GLY ASN LEU ILE ALA PRO MET TYR ALA PHE ALA LEU
SEQRES 21 G 327 ARG ARG GLY PHE GLY SER GLY ILE ILE THR SER ASN ALA
SEQRES 22 G 327 SER MET HIS GLU CYS ASN THR LYS CYS GLN THR PRO LEU
SEQRES 23 G 327 GLY ALA ILE ASN SER SER LEU PRO TYR GLN ASN ILE HIS
SEQRES 24 G 327 PRO VAL THR ILE GLY GLU CYS PRO LYS TYR VAL ARG SER
SEQRES 25 G 327 ALA LYS LEU ARG MET VAL THR GLY LEU ARG ASN ILE PRO
SEQRES 26 G 327 ALA ARG
SEQRES 1 H 160 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY
SEQRES 2 H 160 TRP THR GLY MET ILE ASP GLY TRP TYR GLY TYR HIS HIS
SEQRES 3 H 160 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS
SEQRES 4 H 160 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL
SEQRES 5 H 160 ASN SER VAL ILE GLU LYS MET ASN ILE GLN PHE THR ALA
SEQRES 6 H 160 VAL GLY LYS GLU PHE ASN LYS LEU GLU LYS ARG MET GLU
SEQRES 7 H 160 ASN LEU ASN ASN LYS VAL ASP ASP GLY PHE LEU ASP ILE
SEQRES 8 H 160 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN
SEQRES 9 H 160 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN
SEQRES 10 H 160 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA
SEQRES 11 H 160 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS
SEQRES 12 H 160 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR
SEQRES 13 H 160 TYR ASP TYR PRO
SEQRES 1 I 327 ALA THR ASN ALA ASP THR ILE CYS ILE GLY TYR HIS ALA
SEQRES 2 I 327 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS
SEQRES 3 I 327 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP
SEQRES 4 I 327 SER HIS ASN GLY LYS LEU CYS ARG LEU LYS GLY ILE ALA
SEQRES 5 I 327 PRO LEU GLN LEU GLY LYS CYS ASN ILE ALA GLY TRP LEU
SEQRES 6 I 327 LEU GLY ASN PRO GLU CYS ASP PRO LEU LEU PRO VAL ARG
SEQRES 7 I 327 SER TRP SER TYR ILE VAL GLU THR PRO ASN SER GLU ASN
SEQRES 8 I 327 GLY ILE CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU
SEQRES 9 I 327 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG
SEQRES 10 I 327 PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN HIS
SEQRES 11 I 327 ASN THR ASN GLY VAL THR ALA ALA CYS SER HIS GLU GLY
SEQRES 12 I 327 LYS SER SER PHE TYR ARG ASN LEU LEU TRP LEU THR GLU
SEQRES 13 I 327 LYS GLU GLY SER TYR PRO LYS LEU LYS ASN SER TYR VAL
SEQRES 14 I 327 ASN LYS LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE
SEQRES 15 I 327 HIS HIS PRO PRO ASN SER LYS GLU GLN GLN ASN LEU TYR
SEQRES 16 I 327 GLN ASN GLU ASN ALA TYR VAL SER VAL VAL THR SER ASN
SEQRES 17 I 327 TYR ASN ARG ARG PHE THR PRO GLU ILE ALA GLU ARG PRO
SEQRES 18 I 327 LYS VAL ARG ASP GLN ALA GLY ARG MET ASN TYR TYR TRP
SEQRES 19 I 327 THR LEU LEU LYS PRO GLY ASP THR ILE ILE PHE GLU ALA
SEQRES 20 I 327 ASN GLY ASN LEU ILE ALA PRO MET TYR ALA PHE ALA LEU
SEQRES 21 I 327 ARG ARG GLY PHE GLY SER GLY ILE ILE THR SER ASN ALA
SEQRES 22 I 327 SER MET HIS GLU CYS ASN THR LYS CYS GLN THR PRO LEU
SEQRES 23 I 327 GLY ALA ILE ASN SER SER LEU PRO TYR GLN ASN ILE HIS
SEQRES 24 I 327 PRO VAL THR ILE GLY GLU CYS PRO LYS TYR VAL ARG SER
SEQRES 25 I 327 ALA LYS LEU ARG MET VAL THR GLY LEU ARG ASN ILE PRO
SEQRES 26 I 327 ALA ARG
SEQRES 1 J 160 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY
SEQRES 2 J 160 TRP THR GLY MET ILE ASP GLY TRP TYR GLY TYR HIS HIS
SEQRES 3 J 160 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS
SEQRES 4 J 160 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL
SEQRES 5 J 160 ASN SER VAL ILE GLU LYS MET ASN ILE GLN PHE THR ALA
SEQRES 6 J 160 VAL GLY LYS GLU PHE ASN LYS LEU GLU LYS ARG MET GLU
SEQRES 7 J 160 ASN LEU ASN ASN LYS VAL ASP ASP GLY PHE LEU ASP ILE
SEQRES 8 J 160 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN
SEQRES 9 J 160 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN
SEQRES 10 J 160 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA
SEQRES 11 J 160 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS
SEQRES 12 J 160 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR
SEQRES 13 J 160 TYR ASP TYR PRO
SEQRES 1 K 327 ALA THR ASN ALA ASP THR ILE CYS ILE GLY TYR HIS ALA
SEQRES 2 K 327 ASN ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS
SEQRES 3 K 327 ASN VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP
SEQRES 4 K 327 SER HIS ASN GLY LYS LEU CYS ARG LEU LYS GLY ILE ALA
SEQRES 5 K 327 PRO LEU GLN LEU GLY LYS CYS ASN ILE ALA GLY TRP LEU
SEQRES 6 K 327 LEU GLY ASN PRO GLU CYS ASP PRO LEU LEU PRO VAL ARG
SEQRES 7 K 327 SER TRP SER TYR ILE VAL GLU THR PRO ASN SER GLU ASN
SEQRES 8 K 327 GLY ILE CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU
SEQRES 9 K 327 LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG
SEQRES 10 K 327 PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN HIS
SEQRES 11 K 327 ASN THR ASN GLY VAL THR ALA ALA CYS SER HIS GLU GLY
SEQRES 12 K 327 LYS SER SER PHE TYR ARG ASN LEU LEU TRP LEU THR GLU
SEQRES 13 K 327 LYS GLU GLY SER TYR PRO LYS LEU LYS ASN SER TYR VAL
SEQRES 14 K 327 ASN LYS LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE
SEQRES 15 K 327 HIS HIS PRO PRO ASN SER LYS GLU GLN GLN ASN LEU TYR
SEQRES 16 K 327 GLN ASN GLU ASN ALA TYR VAL SER VAL VAL THR SER ASN
SEQRES 17 K 327 TYR ASN ARG ARG PHE THR PRO GLU ILE ALA GLU ARG PRO
SEQRES 18 K 327 LYS VAL ARG ASP GLN ALA GLY ARG MET ASN TYR TYR TRP
SEQRES 19 K 327 THR LEU LEU LYS PRO GLY ASP THR ILE ILE PHE GLU ALA
SEQRES 20 K 327 ASN GLY ASN LEU ILE ALA PRO MET TYR ALA PHE ALA LEU
SEQRES 21 K 327 ARG ARG GLY PHE GLY SER GLY ILE ILE THR SER ASN ALA
SEQRES 22 K 327 SER MET HIS GLU CYS ASN THR LYS CYS GLN THR PRO LEU
SEQRES 23 K 327 GLY ALA ILE ASN SER SER LEU PRO TYR GLN ASN ILE HIS
SEQRES 24 K 327 PRO VAL THR ILE GLY GLU CYS PRO LYS TYR VAL ARG SER
SEQRES 25 K 327 ALA LYS LEU ARG MET VAL THR GLY LEU ARG ASN ILE PRO
SEQRES 26 K 327 ALA ARG
SEQRES 1 L 160 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY
SEQRES 2 L 160 TRP THR GLY MET ILE ASP GLY TRP TYR GLY TYR HIS HIS
SEQRES 3 L 160 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS
SEQRES 4 L 160 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL
SEQRES 5 L 160 ASN SER VAL ILE GLU LYS MET ASN ILE GLN PHE THR ALA
SEQRES 6 L 160 VAL GLY LYS GLU PHE ASN LYS LEU GLU LYS ARG MET GLU
SEQRES 7 L 160 ASN LEU ASN ASN LYS VAL ASP ASP GLY PHE LEU ASP ILE
SEQRES 8 L 160 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN
SEQRES 9 L 160 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN
SEQRES 10 L 160 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA
SEQRES 11 L 160 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS
SEQRES 12 L 160 CYS ASP ASN GLU CYS MET GLU SER VAL ARG ASN GLY THR
SEQRES 13 L 160 TYR ASP TYR PRO
HET NAG M 1 14
HET GAL M 2 11
HET SIA M 3 20
HET NAG N 1 14
HET GAL N 2 11
HET SIA N 3 20
HET NAG O 1 14
HET GAL O 2 11
HET SIA O 3 20
HET NAG P 1 14
HET GAL P 2 11
HET SIA P 3 20
HET NAG Q 1 14
HET GAL Q 2 11
HET SIA Q 3 20
HET NAG R 1 14
HET GAL R 2 11
HET SIA R 3 20
HET NAG A3321 15
HET NAG E3311 15
HET NAG F3331 15
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC
HETSYN 2 SIA ACID; O-SIALIC ACID
FORMUL 13 NAG 9(C8 H15 N O6)
FORMUL 13 GAL 6(C6 H12 O6)
FORMUL 13 SIA 6(C11 H19 N O9)
FORMUL 22 HOH *2098(H2 O)
HELIX 1 1 ASN A 60 GLY A 67 1 8
HELIX 2 2 ASN A 68 LEU A 75 5 8
HELIX 3 3 ASP A 101 SER A 110 1 10
HELIX 4 4 PRO A 122 TRP A 127 1 6
HELIX 5 5 ASN A 187 GLN A 196 1 10
HELIX 6 6 ASP B 537 MET B 559 1 23
HELIX 7 7 GLU B 574 LYS B 627 1 54
HELIX 8 8 ASP B 645 ASN B 654 1 10
HELIX 9 9 ASN C 60 GLY C 67 1 8
HELIX 10 10 ASN C 68 LEU C 75 5 8
HELIX 11 11 ASP C 101 SER C 110 1 10
HELIX 12 12 PRO C 122 TRP C 127 1 6
HELIX 13 13 ASN C 187 GLN C 196 1 10
HELIX 14 14 ASP D 537 MET D 559 1 23
HELIX 15 15 GLU D 574 SER D 624 1 51
HELIX 16 16 ASN D 646 ASN D 654 1 9
HELIX 17 17 ASN E 60 GLY E 67 1 8
HELIX 18 18 ASN E 68 LEU E 75 5 8
HELIX 19 19 ASP E 101 SER E 110 1 10
HELIX 20 20 PRO E 122 TRP E 127 1 6
HELIX 21 21 ASN E 187 GLN E 196 1 10
HELIX 22 22 ASP F 537 MET F 559 1 23
HELIX 23 23 GLU F 574 LYS F 627 1 54
HELIX 24 24 ASP F 645 ASN F 654 1 10
HELIX 25 25 ASN G 60 GLY G 67 1 8
HELIX 26 26 ASN G 68 LEU G 75 5 8
HELIX 27 27 ASP G 101 SER G 110 1 10
HELIX 28 28 PRO G 122 TRP G 127 1 6
HELIX 29 29 ASN G 187 GLN G 196 1 10
HELIX 30 30 ASP H 537 MET H 559 1 23
HELIX 31 31 GLU H 574 LEU H 626 1 53
HELIX 32 32 ASN H 646 ASN H 654 1 9
HELIX 33 33 ASN I 60 GLY I 67 1 8
HELIX 34 34 ASN I 68 LEU I 75 5 8
HELIX 35 35 ASP I 101 SER I 110 1 10
HELIX 36 36 PRO I 122 TRP I 127 1 6
HELIX 37 37 ASN I 187 GLN I 196 1 10
HELIX 38 38 ASP J 537 MET J 559 1 23
HELIX 39 39 GLU J 574 LYS J 627 1 54
HELIX 40 40 ASP J 645 ASN J 654 1 10
HELIX 41 41 ASN K 60 GLY K 67 1 8
HELIX 42 42 ASN K 68 LEU K 75 5 8
HELIX 43 43 ASP K 101 SER K 110 1 10
HELIX 44 44 PRO K 122 TRP K 127 1 6
HELIX 45 45 ASN K 187 GLN K 196 1 10
HELIX 46 46 ASP L 537 MET L 559 1 23
HELIX 47 47 GLU L 574 LYS L 627 1 54
HELIX 48 48 ASP L 645 ASN L 654 1 10
SHEET 1 A 5 GLY B 533 ALA B 536 0
SHEET 2 A 5 TYR B 522 HIS B 526 -1 N TYR B 524 O ALA B 535
SHEET 3 A 5 THR A 6 TYR A 11 -1 N GLY A 10 O GLY B 523
SHEET 4 A 5 CYS B 637 PHE B 640 -1 O PHE B 638 N ILE A 7
SHEET 5 A 5 ALA B 630 GLU B 632 -1 N LYS B 631 O GLU B 639
SHEET 1 B 2 THR A 19 VAL A 20 0
SHEET 2 B 2 VAL A 28 THR A 29 -1 O VAL A 28 N VAL A 20
SHEET 1 C 2 SER A 33 ASN A 35 0
SHEET 2 C 2 ARG A 316 VAL A 318 -1 O MET A 317 N VAL A 34
SHEET 1 D 3 LEU A 37 GLU A 38 0
SHEET 2 D 3 TYR A 295 GLN A 296 1 O TYR A 295 N GLU A 38
SHEET 3 D 3 LYS A 308 TYR A 309 1 O LYS A 308 N GLN A 296
SHEET 1 E 2 LYS A 45 LEU A 49 0
SHEET 2 E 2 SER A 274 THR A 280 1 O SER A 274 N LEU A 46
SHEET 1 F 3 LEU A 54 GLY A 57 0
SHEET 2 F 3 ILE A 83 GLU A 85 1 O VAL A 84 N LEU A 54
SHEET 3 F 3 ILE A 268 THR A 270 1 O ILE A 269 N GLU A 85
SHEET 1 G 5 VAL A 112 GLU A 119 0
SHEET 2 G 5 TYR A 256 ARG A 262 -1 O ARG A 261 N SER A 114
SHEET 3 G 5 VAL A 176 HIS A 184 -1 N LEU A 177 O PHE A 258
SHEET 4 G 5 LEU A 251 PRO A 254 -1 O ILE A 252 N GLY A 181
SHEET 5 G 5 LEU A 151 TRP A 153 -1 N LEU A 152 O ALA A 253
SHEET 1 H 4 VAL A 112 GLU A 119 0
SHEET 2 H 4 TYR A 256 ARG A 262 -1 O ARG A 261 N SER A 114
SHEET 3 H 4 VAL A 176 HIS A 184 -1 N LEU A 177 O PHE A 258
SHEET 4 H 4 ARG A 229 LEU A 237 -1 O ARG A 229 N HIS A 184
SHEET 1 I 2 THR A 136 HIS A 141 0
SHEET 2 I 2 LYS A 144 SER A 146 -1 O LYS A 144 N HIS A 141
SHEET 1 J 4 LEU A 164 VAL A 169 0
SHEET 2 J 4 THR A 242 ALA A 247 -1 O ALA A 247 N LEU A 164
SHEET 3 J 4 VAL A 202 VAL A 205 -1 N SER A 203 O GLU A 246
SHEET 4 J 4 ASN A 210 PHE A 213 -1 O PHE A 213 N VAL A 202
SHEET 1 K 4 GLY A 287 ILE A 289 0
SHEET 2 K 4 CYS A 282 THR A 284 -1 N CYS A 282 O ILE A 289
SHEET 3 K 4 THR A 302 CYS A 306 -1 O ILE A 303 N GLN A 283
SHEET 4 K 4 GLN B 562 ALA B 565 -1 O GLN B 562 N CYS A 306
SHEET 1 L 5 GLY D 531 ALA D 536 0
SHEET 2 L 5 TYR D 522 ASN D 528 -1 N TYR D 524 O ALA D 535
SHEET 3 L 5 THR C 6 TYR C 11 -1 N GLY C 10 O GLY D 523
SHEET 4 L 5 CYS D 637 PHE D 640 -1 O PHE D 638 N ILE C 7
SHEET 5 L 5 ALA D 630 GLU D 632 -1 N LYS D 631 O GLU D 639
SHEET 1 M 2 THR C 19 VAL C 20 0
SHEET 2 M 2 VAL C 28 THR C 29 -1 O VAL C 28 N VAL C 20
SHEET 1 N 2 SER C 33 ASN C 35 0
SHEET 2 N 2 ARG C 316 VAL C 318 -1 O MET C 317 N VAL C 34
SHEET 1 O 3 LEU C 37 GLU C 38 0
SHEET 2 O 3 TYR C 295 GLN C 296 1 O TYR C 295 N GLU C 38
SHEET 3 O 3 LYS C 308 TYR C 309 1 O LYS C 308 N GLN C 296
SHEET 1 P 2 LEU C 46 LEU C 49 0
SHEET 2 P 2 MET C 275 THR C 280 1 O CYS C 278 N ARG C 48
SHEET 1 Q 3 LEU C 54 GLN C 55 0
SHEET 2 Q 3 ILE C 83 GLU C 85 1 O VAL C 84 N LEU C 54
SHEET 3 Q 3 ILE C 268 THR C 270 1 O ILE C 269 N GLU C 85
SHEET 1 R 5 VAL C 112 GLU C 119 0
SHEET 2 R 5 TYR C 256 ARG C 262 -1 O ALA C 257 N PHE C 118
SHEET 3 R 5 VAL C 176 HIS C 184 -1 N LEU C 177 O PHE C 258
SHEET 4 R 5 LEU C 251 PRO C 254 -1 O ILE C 252 N GLY C 181
SHEET 5 R 5 LEU C 151 TRP C 153 -1 N LEU C 152 O ALA C 253
SHEET 1 S 4 VAL C 112 GLU C 119 0
SHEET 2 S 4 TYR C 256 ARG C 262 -1 O ALA C 257 N PHE C 118
SHEET 3 S 4 VAL C 176 HIS C 184 -1 N LEU C 177 O PHE C 258
SHEET 4 S 4 ARG C 229 LEU C 237 -1 O ARG C 229 N HIS C 184
SHEET 1 T 2 THR C 136 HIS C 141 0
SHEET 2 T 2 LYS C 144 SER C 146 -1 O LYS C 144 N HIS C 141
SHEET 1 U 4 LEU C 164 VAL C 169 0
SHEET 2 U 4 THR C 242 ALA C 247 -1 O ALA C 247 N LEU C 164
SHEET 3 U 4 VAL C 202 VAL C 205 -1 N SER C 203 O GLU C 246
SHEET 4 U 4 ASN C 210 PHE C 213 -1 O PHE C 213 N VAL C 202
SHEET 1 V 4 ALA C 288 ILE C 289 0
SHEET 2 V 4 CYS C 282 GLN C 283 -1 N CYS C 282 O ILE C 289
SHEET 3 V 4 THR C 302 CYS C 306 -1 O ILE C 303 N GLN C 283
SHEET 4 V 4 GLN D 562 ALA D 565 -1 O GLN D 562 N CYS C 306
SHEET 1 W 5 TYR F 534 ALA F 536 0
SHEET 2 W 5 TYR F 522 HIS F 526 -1 N TYR F 524 O ALA F 535
SHEET 3 W 5 THR E 6 TYR E 11 -1 N CYS E 8 O HIS F 525
SHEET 4 W 5 CYS F 637 PHE F 640 -1 O PHE F 638 N ILE E 7
SHEET 5 W 5 ALA F 630 GLU F 632 -1 N LYS F 631 O GLU F 639
SHEET 1 X 2 ASP E 18 VAL E 20 0
SHEET 2 X 2 VAL E 28 VAL E 30 -1 O VAL E 28 N VAL E 20
SHEET 1 Y 2 SER E 33 ASN E 35 0
SHEET 2 Y 2 ARG E 316 VAL E 318 -1 O MET E 317 N VAL E 34
SHEET 1 Z 3 LEU E 37 GLU E 38 0
SHEET 2 Z 3 TYR E 295 GLN E 296 1 O TYR E 295 N GLU E 38
SHEET 3 Z 3 LYS E 308 TYR E 309 1 O LYS E 308 N GLN E 296
SHEET 1 AA 2 LEU E 46 LEU E 49 0
SHEET 2 AA 2 MET E 275 THR E 280 1 O CYS E 278 N ARG E 48
SHEET 1 AB 3 LEU E 54 GLY E 57 0
SHEET 2 AB 3 ILE E 83 GLU E 85 1 O VAL E 84 N LEU E 54
SHEET 3 AB 3 ILE E 268 THR E 270 1 O ILE E 269 N GLU E 85
SHEET 1 AC 5 VAL E 112 GLU E 119 0
SHEET 2 AC 5 TYR E 256 ARG E 262 -1 O ALA E 257 N PHE E 118
SHEET 3 AC 5 VAL E 176 HIS E 184 -1 N LEU E 177 O PHE E 258
SHEET 4 AC 5 LEU E 251 PRO E 254 -1 O ILE E 252 N GLY E 181
SHEET 5 AC 5 LEU E 151 TRP E 153 -1 N LEU E 152 O ALA E 253
SHEET 1 AD 4 VAL E 112 GLU E 119 0
SHEET 2 AD 4 TYR E 256 ARG E 262 -1 O ALA E 257 N PHE E 118
SHEET 3 AD 4 VAL E 176 HIS E 184 -1 N LEU E 177 O PHE E 258
SHEET 4 AD 4 ARG E 229 LEU E 237 -1 O ARG E 229 N HIS E 184
SHEET 1 AE 2 THR E 136 HIS E 141 0
SHEET 2 AE 2 LYS E 144 SER E 146 -1 O SER E 146 N THR E 136
SHEET 1 AF 4 LEU E 164 VAL E 169 0
SHEET 2 AF 4 THR E 242 ALA E 247 -1 O ALA E 247 N LEU E 164
SHEET 3 AF 4 VAL E 202 VAL E 205 -1 N SER E 203 O GLU E 246
SHEET 4 AF 4 ASN E 210 PHE E 213 -1 O PHE E 213 N VAL E 202
SHEET 1 AG 3 ALA E 288 ILE E 289 0
SHEET 2 AG 3 CYS E 282 GLN E 283 -1 N CYS E 282 O ILE E 289
SHEET 3 AG 3 ILE E 303 GLY E 304 -1 O ILE E 303 N GLN E 283
SHEET 1 AH 5 TYR H 534 ALA H 536 0
SHEET 2 AH 5 TYR H 522 GLN H 527 -1 N TYR H 524 O ALA H 535
SHEET 3 AH 5 THR G 6 TYR G 11 -1 N THR G 6 O GLN H 527
SHEET 4 AH 5 CYS H 637 PHE H 640 -1 O PHE H 638 N ILE G 7
SHEET 5 AH 5 ALA H 630 GLU H 632 -1 N LYS H 631 O GLU H 639
SHEET 1 AI 2 ASP G 18 VAL G 20 0
SHEET 2 AI 2 VAL G 28 VAL G 30 -1 O VAL G 28 N VAL G 20
SHEET 1 AJ 2 SER G 33 ASN G 35 0
SHEET 2 AJ 2 ARG G 316 VAL G 318 -1 O MET G 317 N VAL G 34
SHEET 1 AK 3 LEU G 37 GLU G 38 0
SHEET 2 AK 3 TYR G 295 GLN G 296 1 O TYR G 295 N GLU G 38
SHEET 3 AK 3 LYS G 308 TYR G 309 1 O LYS G 308 N GLN G 296
SHEET 1 AL 2 LEU G 46 LEU G 49 0
SHEET 2 AL 2 MET G 275 THR G 280 1 O CYS G 278 N ARG G 48
SHEET 1 AM 3 LEU G 54 GLY G 57 0
SHEET 2 AM 3 ILE G 83 GLU G 85 1 O VAL G 84 N LEU G 54
SHEET 3 AM 3 ILE G 268 THR G 270 1 O ILE G 269 N GLU G 85
SHEET 1 AN 5 VAL G 112 GLU G 119 0
SHEET 2 AN 5 TYR G 256 ARG G 262 -1 O ARG G 261 N SER G 114
SHEET 3 AN 5 VAL G 176 HIS G 184 -1 N LEU G 177 O PHE G 258
SHEET 4 AN 5 LEU G 251 PRO G 254 -1 O ILE G 252 N GLY G 181
SHEET 5 AN 5 LEU G 151 TRP G 153 -1 N LEU G 152 O ALA G 253
SHEET 1 AO 4 VAL G 112 GLU G 119 0
SHEET 2 AO 4 TYR G 256 ARG G 262 -1 O ARG G 261 N SER G 114
SHEET 3 AO 4 VAL G 176 HIS G 184 -1 N LEU G 177 O PHE G 258
SHEET 4 AO 4 ARG G 229 LEU G 237 -1 O ARG G 229 N HIS G 184
SHEET 1 AP 2 THR G 136 HIS G 141 0
SHEET 2 AP 2 LYS G 144 SER G 146 -1 O LYS G 144 N HIS G 141
SHEET 1 AQ 4 LEU G 164 VAL G 169 0
SHEET 2 AQ 4 THR G 242 ALA G 247 -1 O ALA G 247 N LEU G 164
SHEET 3 AQ 4 VAL G 202 VAL G 205 -1 N SER G 203 O GLU G 246
SHEET 4 AQ 4 ASN G 210 PHE G 213 -1 O PHE G 213 N VAL G 202
SHEET 1 AR 4 ALA G 288 ILE G 289 0
SHEET 2 AR 4 CYS G 282 GLN G 283 -1 N CYS G 282 O ILE G 289
SHEET 3 AR 4 THR G 302 CYS G 306 -1 O ILE G 303 N GLN G 283
SHEET 4 AR 4 GLN H 562 ALA H 565 -1 O GLN H 562 N CYS G 306
SHEET 1 AS 5 TYR J 534 ALA J 536 0
SHEET 2 AS 5 TYR J 522 HIS J 525 -1 N TYR J 524 O ALA J 535
SHEET 3 AS 5 THR I 6 TYR I 11 -1 N GLY I 10 O GLY J 523
SHEET 4 AS 5 CYS J 637 PHE J 640 -1 O PHE J 638 N ILE I 7
SHEET 5 AS 5 ALA J 630 GLU J 632 -1 N LYS J 631 O GLU J 639
SHEET 1 AT 2 THR I 19 VAL I 20 0
SHEET 2 AT 2 VAL I 28 THR I 29 -1 O VAL I 28 N VAL I 20
SHEET 1 AU 2 SER I 33 ASN I 35 0
SHEET 2 AU 2 ARG I 316 VAL I 318 -1 O MET I 317 N VAL I 34
SHEET 1 AV 3 LEU I 37 GLU I 38 0
SHEET 2 AV 3 TYR I 295 GLN I 296 1 O TYR I 295 N GLU I 38
SHEET 3 AV 3 LYS I 308 TYR I 309 1 O LYS I 308 N GLN I 296
SHEET 1 AW 2 LEU I 46 LEU I 49 0
SHEET 2 AW 2 MET I 275 THR I 280 1 O CYS I 278 N ARG I 48
SHEET 1 AX 3 LEU I 54 GLY I 57 0
SHEET 2 AX 3 ILE I 83 GLU I 85 1 O VAL I 84 N LEU I 54
SHEET 3 AX 3 ILE I 268 THR I 270 1 O ILE I 269 N GLU I 85
SHEET 1 AY 5 VAL I 112 GLU I 119 0
SHEET 2 AY 5 TYR I 256 ARG I 262 -1 O ALA I 257 N PHE I 118
SHEET 3 AY 5 VAL I 176 HIS I 184 -1 N LEU I 177 O PHE I 258
SHEET 4 AY 5 LEU I 251 PRO I 254 -1 O ILE I 252 N GLY I 181
SHEET 5 AY 5 LEU I 151 TRP I 153 -1 N LEU I 152 O ALA I 253
SHEET 1 AZ 4 VAL I 112 GLU I 119 0
SHEET 2 AZ 4 TYR I 256 ARG I 262 -1 O ALA I 257 N PHE I 118
SHEET 3 AZ 4 VAL I 176 HIS I 184 -1 N LEU I 177 O PHE I 258
SHEET 4 AZ 4 ARG I 229 LEU I 237 -1 O ARG I 229 N HIS I 184
SHEET 1 BA 2 THR I 136 HIS I 141 0
SHEET 2 BA 2 LYS I 144 SER I 146 -1 O LYS I 144 N HIS I 141
SHEET 1 BB 4 LEU I 164 VAL I 169 0
SHEET 2 BB 4 THR I 242 ALA I 247 -1 O ALA I 247 N LEU I 164
SHEET 3 BB 4 VAL I 202 VAL I 205 -1 N SER I 203 O GLU I 246
SHEET 4 BB 4 ASN I 210 PHE I 213 -1 O PHE I 213 N VAL I 202
SHEET 1 BC 4 ALA I 288 ILE I 289 0
SHEET 2 BC 4 CYS I 282 GLN I 283 -1 N CYS I 282 O ILE I 289
SHEET 3 BC 4 THR I 302 CYS I 306 -1 O ILE I 303 N GLN I 283
SHEET 4 BC 4 GLN J 562 ALA J 565 -1 O GLN J 562 N CYS I 306
SHEET 1 BD 5 TYR L 534 ALA L 536 0
SHEET 2 BD 5 TYR L 522 HIS L 526 -1 N TYR L 524 O ALA L 535
SHEET 3 BD 5 THR K 6 TYR K 11 -1 N GLY K 10 O GLY L 523
SHEET 4 BD 5 CYS L 637 PHE L 640 -1 O PHE L 638 N ILE K 7
SHEET 5 BD 5 ALA L 630 GLU L 632 -1 N LYS L 631 O GLU L 639
SHEET 1 BE 2 THR K 19 VAL K 20 0
SHEET 2 BE 2 VAL K 28 THR K 29 -1 O VAL K 28 N VAL K 20
SHEET 1 BF 2 SER K 33 ASN K 35 0
SHEET 2 BF 2 ARG K 316 VAL K 318 -1 O MET K 317 N VAL K 34
SHEET 1 BG 3 LEU K 37 GLU K 38 0
SHEET 2 BG 3 TYR K 295 GLN K 296 1 O TYR K 295 N GLU K 38
SHEET 3 BG 3 LYS K 308 TYR K 309 1 O LYS K 308 N GLN K 296
SHEET 1 BH 2 LYS K 45 LEU K 49 0
SHEET 2 BH 2 SER K 274 THR K 280 1 O CYS K 278 N ARG K 48
SHEET 1 BI 3 LEU K 54 GLN K 55 0
SHEET 2 BI 3 ILE K 83 GLU K 85 1 O VAL K 84 N LEU K 54
SHEET 3 BI 3 ILE K 268 THR K 270 1 O ILE K 269 N GLU K 85
SHEET 1 BJ 5 VAL K 112 GLU K 119 0
SHEET 2 BJ 5 TYR K 256 ARG K 262 -1 O ARG K 261 N SER K 114
SHEET 3 BJ 5 VAL K 176 HIS K 184 -1 N LEU K 177 O PHE K 258
SHEET 4 BJ 5 LEU K 251 PRO K 254 -1 O ILE K 252 N GLY K 181
SHEET 5 BJ 5 LEU K 151 TRP K 153 -1 N LEU K 152 O ALA K 253
SHEET 1 BK 4 VAL K 112 GLU K 119 0
SHEET 2 BK 4 TYR K 256 ARG K 262 -1 O ARG K 261 N SER K 114
SHEET 3 BK 4 VAL K 176 HIS K 184 -1 N LEU K 177 O PHE K 258
SHEET 4 BK 4 ARG K 229 LEU K 237 -1 O ARG K 229 N HIS K 184
SHEET 1 BL 2 THR K 136 HIS K 141 0
SHEET 2 BL 2 LYS K 144 SER K 146 -1 O LYS K 144 N HIS K 141
SHEET 1 BM 4 LEU K 164 VAL K 169 0
SHEET 2 BM 4 THR K 242 ALA K 247 -1 O ALA K 247 N LEU K 164
SHEET 3 BM 4 VAL K 202 VAL K 205 -1 N SER K 203 O GLU K 246
SHEET 4 BM 4 ASN K 210 PHE K 213 -1 O PHE K 213 N VAL K 202
SHEET 1 BN 4 GLY K 287 ILE K 289 0
SHEET 2 BN 4 CYS K 282 THR K 284 -1 N CYS K 282 O ILE K 289
SHEET 3 BN 4 THR K 302 CYS K 306 -1 O ILE K 303 N GLN K 283
SHEET 4 BN 4 GLN L 562 ALA L 565 -1 O GLN L 562 N CYS K 306
SSBOND 1 CYS A 8 CYS B 637 1555 1555 2.04
SSBOND 2 CYS A 47 CYS A 278 1555 1555 2.05
SSBOND 3 CYS A 59 CYS A 71 1555 1555 2.04
SSBOND 4 CYS A 94 CYS A 139 1555 1555 2.05
SSBOND 5 CYS A 282 CYS A 306 1555 1555 2.03
SSBOND 6 CYS B 644 CYS B 648 1555 1555 2.03
SSBOND 7 CYS C 8 CYS D 637 1555 1555 2.04
SSBOND 8 CYS C 47 CYS C 278 1555 1555 2.05
SSBOND 9 CYS C 59 CYS C 71 1555 1555 2.04
SSBOND 10 CYS C 94 CYS C 139 1555 1555 2.05
SSBOND 11 CYS C 282 CYS C 306 1555 1555 2.04
SSBOND 12 CYS D 644 CYS D 648 1555 1555 2.03
SSBOND 13 CYS E 8 CYS F 637 1555 1555 2.04
SSBOND 14 CYS E 47 CYS E 278 1555 1555 2.05
SSBOND 15 CYS E 59 CYS E 71 1555 1555 2.04
SSBOND 16 CYS E 94 CYS E 139 1555 1555 2.05
SSBOND 17 CYS E 282 CYS E 306 1555 1555 2.03
SSBOND 18 CYS F 644 CYS F 648 1555 1555 2.03
SSBOND 19 CYS G 8 CYS H 637 1555 1555 2.04
SSBOND 20 CYS G 47 CYS G 278 1555 1555 2.04
SSBOND 21 CYS G 59 CYS G 71 1555 1555 2.04
SSBOND 22 CYS G 94 CYS G 139 1555 1555 2.05
SSBOND 23 CYS G 282 CYS G 306 1555 1555 2.03
SSBOND 24 CYS H 644 CYS H 648 1555 1555 2.03
SSBOND 25 CYS I 8 CYS J 637 1555 1555 2.04
SSBOND 26 CYS I 47 CYS I 278 1555 1555 2.04
SSBOND 27 CYS I 59 CYS I 71 1555 1555 2.04
SSBOND 28 CYS I 94 CYS I 139 1555 1555 2.05
SSBOND 29 CYS I 282 CYS I 306 1555 1555 2.04
SSBOND 30 CYS J 644 CYS J 648 1555 1555 2.03
SSBOND 31 CYS K 8 CYS L 637 1555 1555 2.04
SSBOND 32 CYS K 47 CYS K 278 1555 1555 2.04
SSBOND 33 CYS K 59 CYS K 71 1555 1555 2.05
SSBOND 34 CYS K 94 CYS K 139 1555 1555 2.05
SSBOND 35 CYS K 282 CYS K 306 1555 1555 2.04
SSBOND 36 CYS L 644 CYS L 648 1555 1555 2.03
LINK O4 NAG M 1 C1 GAL M 2 1555 1555 1.29
LINK O6 GAL M 2 C2 SIA M 3 1555 1555 1.44
LINK O4 NAG N 1 C1 GAL N 2 1555 1555 1.27
LINK O6 GAL N 2 C2 SIA N 3 1555 1555 1.44
LINK O4 NAG O 1 C1 GAL O 2 1555 1555 1.30
LINK O6 GAL O 2 C2 SIA O 3 1555 1555 1.45
LINK O4 NAG P 1 C1 GAL P 2 1555 1555 1.29
LINK O6 GAL P 2 C2 SIA P 3 1555 1555 1.44
LINK O4 NAG Q 1 C1 GAL Q 2 1555 1555 1.28
LINK O6 GAL Q 2 C2 SIA Q 3 1555 1555 1.44
LINK O4 NAG R 1 C1 GAL R 2 1555 1555 1.27
LINK O6 GAL R 2 C2 SIA R 3 1555 1555 1.44
CRYST1 227.583 131.522 175.017 90.00 110.07 90.00 C 1 2 1 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 0.004394 0.000000 0.001605 0.00000
SCALE2 0.000000 0.007603 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006083 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
