HEADER CELL ADHESION 07-JUL-04 1TYE
TITLE STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING OF LIGAND-
TITLE 2 MIMETIC THERAPEUTICS TO THE PLATELET RECEPTOR FOR FIBRINOGEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB;
COMPND 3 CHAIN: A, C, E;
COMPND 4 FRAGMENT: RESIDUES 1-452;
COMPND 5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB; GPALPHA IIB; GPIIB; CD41
COMPND 6 ANTIGEN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTEGRIN BETA-3;
COMPND 10 CHAIN: B, D, F;
COMPND 11 FRAGMENT: RESIDUES 1-440;
COMPND 12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA; GPIIIA; CD61 ANTIGEN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ITGAB;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: LEC 3.2.8.1;
SOURCE 10 EXPRESSION_SYSTEM_CELL: HAMPSTER OVARY CELLS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: ITGAB;
SOURCE 17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: LEC 3.2.8.1;
SOURCE 21 EXPRESSION_SYSTEM_CELL: HAMPSTER OVARY CELLS;
SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS CRYSTAL STRUCTURE; PLATELET INTEGRIN ALPHAIIBBETA3; FIBRINOGEN
KEYWDS 2 BINDING; ALLOSTERY; THERAPEUTIC ANTAGONISM, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER
REVDAT 4 13-JUL-11 1TYE 1 VERSN
REVDAT 3 24-FEB-09 1TYE 1 VERSN
REVDAT 2 09-NOV-04 1TYE 1 JRNL
REVDAT 1 12-OCT-04 1TYE 0
JRNL AUTH T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER
JRNL TITL STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING TO
JRNL TITL 2 FIBRINOGEN-MIMETIC THERAPEUTICS
JRNL REF NATURE V. 432 59 2004
JRNL REFN ISSN 0028-0836
JRNL PMID 15378069
JRNL DOI DOI:10.1038/NATURE02976
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 118381
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5971
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 : 20604
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 295
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 74.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21500
REMARK 3 B22 (A**2) : 0.21500
REMARK 3 B33 (A**2) : -0.43000
REMARK 3 B12 (A**2) : -10.34300
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.42
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1TYE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-04.
REMARK 100 THE RCSB ID CODE IS RCSB023029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9760
REMARK 200 MONOCHROMATOR : RH-COATED SI
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121498
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 10.000
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.60200
REMARK 200 R SYM FOR SHELL (I) : 0.60200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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 1TVX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.4 M MAGNESIUM ACETATE,
REMARK 280 0.1 M SODIUM CACODYLATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.85867
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.42933
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 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 58.85867
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 29.42933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 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 C SER B 84 CD PRO B 85 1.51
REMARK 500 O SER C 101 N ASP C 102 1.56
REMARK 500 O GLU E 123 N LYS E 124 1.62
REMARK 500 O ALA A 122 N GLU A 123 1.77
REMARK 500 O TRP E 100 N SER E 101 1.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 28 CB ASP A 28 CG -0.130
REMARK 500 SER A 101 CB SER A 101 OG 0.287
REMARK 500 GLU A 123 CB GLU A 123 CG 0.324
REMARK 500 ALA A 122 C GLU A 123 N -0.292
REMARK 500 GLU A 123 C LYS A 124 N 0.157
REMARK 500 TRP C 100 C SER C 101 N -0.244
REMARK 500 SER C 101 C ASP C 102 N -0.271
REMARK 500 GLU C 117 CA GLU C 117 C 0.317
REMARK 500 LYS C 118 N LYS C 118 CA -0.162
REMARK 500 ALA C 122 C ALA C 122 O -0.119
REMARK 500 GLU C 123 N GLU C 123 CA 0.129
REMARK 500 ARG D 8 CB ARG D 8 CG -0.181
REMARK 500 THR D 7 C ARG D 8 N -0.142
REMARK 500 PRO D 85 CD PRO D 85 N 0.395
REMARK 500 SER D 84 C PRO D 85 N -0.173
REMARK 500 TRP E 100 C SER E 101 N -0.271
REMARK 500 ALA E 122 C GLU E 123 N 0.300
REMARK 500 GLU E 123 C LYS E 124 N -0.377
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 102 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 ASP A 102 N - CA - C ANGL. DEV. = 20.2 DEGREES
REMARK 500 ALA A 122 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 ALA A 122 CA - C - O ANGL. DEV. = -12.8 DEGREES
REMARK 500 ALA A 122 CA - C - N ANGL. DEV. = 33.9 DEGREES
REMARK 500 ALA A 122 O - C - N ANGL. DEV. = -25.0 DEGREES
REMARK 500 GLU A 123 C - N - CA ANGL. DEV. = 25.4 DEGREES
REMARK 500 PRO A 334 N - CA - CB ANGL. DEV. = 8.0 DEGREES
REMARK 500 PRO A 337 CA - N - CD ANGL. DEV. = -15.6 DEGREES
REMARK 500 PRO A 452 C - N - CD ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG B 8 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 GLN B 79 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 PRO B 85 C - N - CD ANGL. DEV. = -65.2 DEGREES
REMARK 500 GLU B 409 N - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 TRP C 100 CA - C - N ANGL. DEV. = 15.4 DEGREES
REMARK 500 TRP C 100 O - C - N ANGL. DEV. = -19.0 DEGREES
REMARK 500 SER C 101 C - N - CA ANGL. DEV. = 25.1 DEGREES
REMARK 500 ASP C 102 N - CA - C ANGL. DEV. = 19.6 DEGREES
REMARK 500 SER C 101 CA - C - N ANGL. DEV. = 31.6 DEGREES
REMARK 500 SER C 101 O - C - N ANGL. DEV. = -39.9 DEGREES
REMARK 500 ASP C 102 C - N - CA ANGL. DEV. = 24.5 DEGREES
REMARK 500 GLU C 117 O - C - N ANGL. DEV. = 16.0 DEGREES
REMARK 500 ALA C 122 CB - CA - C ANGL. DEV. = 14.8 DEGREES
REMARK 500 ALA C 122 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 ALA C 122 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 GLU C 123 C - N - CA ANGL. DEV. = 17.4 DEGREES
REMARK 500 GLU C 123 O - C - N ANGL. DEV. = -11.4 DEGREES
REMARK 500 PRO C 334 CA - N - CD ANGL. DEV. = -22.8 DEGREES
REMARK 500 PRO C 337 CA - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500 PRO C 337 C - N - CD ANGL. DEV. = -25.4 DEGREES
REMARK 500 PRO D 85 CA - N - CD ANGL. DEV. = -20.1 DEGREES
REMARK 500 PRO D 85 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO D 85 N - CD - CG ANGL. DEV. = -11.7 DEGREES
REMARK 500 SER D 84 CA - C - N ANGL. DEV. = 20.2 DEGREES
REMARK 500 SER D 84 O - C - N ANGL. DEV. = -20.3 DEGREES
REMARK 500 PRO D 85 C - N - CA ANGL. DEV. = 30.5 DEGREES
REMARK 500 PRO D 85 C - N - CD ANGL. DEV. = -18.4 DEGREES
REMARK 500 SER E 101 N - CA - CB ANGL. DEV. = -13.1 DEGREES
REMARK 500 TRP E 100 CA - C - N ANGL. DEV. = 18.0 DEGREES
REMARK 500 TRP E 100 O - C - N ANGL. DEV. = -20.3 DEGREES
REMARK 500 SER E 101 C - N - CA ANGL. DEV. = 30.5 DEGREES
REMARK 500 GLU E 123 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 ALA E 122 CA - C - N ANGL. DEV. = -14.5 DEGREES
REMARK 500 ALA E 122 O - C - N ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU E 123 CA - C - N ANGL. DEV. = 24.8 DEGREES
REMARK 500 GLU E 123 O - C - N ANGL. DEV. = -29.6 DEGREES
REMARK 500 PRO E 334 CA - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 PRO E 334 C - N - CD ANGL. DEV. = -14.2 DEGREES
REMARK 500 PRO E 337 CA - N - CD ANGL. DEV. = -9.7 DEGREES
REMARK 500 PRO E 337 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 58 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 VAL A 6 -47.87 -131.24
REMARK 500 GLN A 7 34.83 -90.60
REMARK 500 HIS A 30 -98.45 -92.66
REMARK 500 ARG A 32 -178.45 -66.22
REMARK 500 PRO A 40 1.79 -65.47
REMARK 500 PRO A 45 -9.44 -58.10
REMARK 500 ARG A 59 115.31 -165.57
REMARK 500 SER A 96 115.77 -163.08
REMARK 500 SER A 101 -97.77 3.03
REMARK 500 LYS A 118 -126.25 64.75
REMARK 500 ALA A 122 -70.33 -124.79
REMARK 500 GLU A 168 40.72 70.62
REMARK 500 SER A 218 32.56 -92.72
REMARK 500 SER A 222 -168.94 -65.61
REMARK 500 SER A 261 65.69 38.50
REMARK 500 TYR A 288 43.63 70.98
REMARK 500 THR A 296 160.04 179.95
REMARK 500 ASP A 319 35.59 84.79
REMARK 500 PRO A 337 59.44 -61.13
REMARK 500 ALA A 342 170.67 -56.74
REMARK 500 GLN A 395 -148.08 -100.99
REMARK 500 PRO A 412 -167.96 -70.56
REMARK 500 SER B 11 -16.72 -168.41
REMARK 500 CYS B 26 103.32 -165.61
REMARK 500 SER B 27 32.23 -90.78
REMARK 500 ALA B 30 3.62 -60.03
REMARK 500 LEU B 33 48.43 -70.00
REMARK 500 PRO B 51 9.97 -57.90
REMARK 500 GLU B 60 -51.20 -128.11
REMARK 500 ALA B 61 90.20 61.17
REMARK 500 LEU B 64 -78.06 -77.84
REMARK 500 ASP B 66 70.86 -162.06
REMARK 500 PRO B 68 167.07 -48.26
REMARK 500 ASP B 76 112.92 -170.10
REMARK 500 GLN B 79 115.88 -167.58
REMARK 500 VAL B 157 -68.52 -141.57
REMARK 500 ASP B 158 -178.90 177.86
REMARK 500 PRO B 160 63.16 -67.78
REMARK 500 SER B 213 -164.06 -125.67
REMARK 500 CYS B 232 73.88 -100.97
REMARK 500 ASP B 233 -73.89 -40.45
REMARK 500 ASN B 240 -40.08 -27.80
REMARK 500 LYS B 253 -175.42 -62.46
REMARK 500 LEU B 258 -5.71 86.05
REMARK 500 SER B 334 -168.71 -168.89
REMARK 500 ASP B 361 74.96 43.33
REMARK 500 GLU B 365 31.33 -86.82
REMARK 500 CYS B 374 -151.63 -76.35
REMARK 500 ASN B 376 3.14 -65.63
REMARK 500 ASN B 377 17.10 57.83
REMARK 500
REMARK 500 THIS ENTRY HAS 172 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 122 GLU A 123 127.70
REMARK 500 TRP C 100 SER C 101 -131.39
REMARK 500 SER C 101 ASP C 102 118.79
REMARK 500 SER D 84 PRO D 85 -142.84
REMARK 500 TRP E 100 SER E 101 -132.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 28 -11.71
REMARK 500 TRP A 100 -11.88
REMARK 500 ALA A 122 24.43
REMARK 500 TRP C 100 -12.88
REMARK 500 SER C 101 32.04
REMARK 500 GLU C 123 -16.11
REMARK 500 SER D 11 -10.36
REMARK 500 SER D 84 -14.66
REMARK 500 TRP E 100 -11.14
REMARK 500 GLU E 123 -19.66
REMARK 500 ASP F 361 -10.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PRO B 2 46.8 L L OUTSIDE RANGE
REMARK 500 ASP C 102 16.9 L L OUTSIDE RANGE
REMARK 500 PHE C 191 24.2 L L OUTSIDE RANGE
REMARK 500 THR F 7 25.0 L L OUTSIDE RANGE
REMARK 500 SER F 11 23.4 L L OUTSIDE RANGE
REMARK 500 LYS F 72 23.6 L L OUTSIDE RANGE
REMARK 500 ASP F 361 20.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 243 OE1
REMARK 620 2 ASP A 247 O 75.0
REMARK 620 3 THR A 250 O 71.9 90.6
REMARK 620 4 ASP A 245 OD1 119.8 102.3 164.4
REMARK 620 5 THR A 250 OG1 143.9 84.7 79.0 93.2
REMARK 620 6 GLU A 252 OE1 120.0 163.5 88.4 76.7 79.0
REMARK 620 7 GLU A 252 OE2 82.8 152.8 97.5 75.1 122.4 43.4
REMARK 620 8 GLU A 243 OE2 51.0 80.7 122.6 69.0 153.7 113.6 73.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1405 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 299 OD1
REMARK 620 2 ASP A 305 OD1 117.0
REMARK 620 3 ASP A 305 OD2 89.3 53.0
REMARK 620 4 ASP A 297 OD1 72.1 135.5 85.5
REMARK 620 5 ASP A 301 OD1 74.1 143.9 160.7 80.1
REMARK 620 6 ASP A 301 OD2 53.5 112.5 131.3 107.0 44.0
REMARK 620 7 ARG A 303 O 148.6 93.1 103.3 80.2 87.0 125.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1406 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 373 OD1
REMARK 620 2 ASP A 367 OD1 97.9
REMARK 620 3 ASP A 365 OD1 147.0 98.7
REMARK 620 4 TYR A 371 O 87.4 164.0 84.4
REMARK 620 5 ASP A 373 OD2 48.1 104.0 100.1 90.7
REMARK 620 6 ASP A 369 OD1 124.2 72.4 88.0 92.1 171.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1407 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 434 OD1
REMARK 620 2 ASP A 428 OD1 103.2
REMARK 620 3 ASP A 434 OD2 49.3 91.6
REMARK 620 4 ASP A 426 OD1 141.6 72.0 92.3
REMARK 620 5 ASP A 428 OD2 74.9 45.1 98.7 116.1
REMARK 620 6 ASN A 430 OD1 139.7 81.3 169.6 78.4 81.6
REMARK 620 7 TYR A 432 O 103.8 141.7 86.0 69.9 172.0 95.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC B1301 O2
REMARK 620 2 HOH B1405 O 152.7
REMARK 620 3 GLU B 220 OE1 99.1 104.4
REMARK 620 4 HOH B1404 O 100.6 95.7 83.9
REMARK 620 5 SER B 121 OG 82.5 84.8 87.4 171.1
REMARK 620 6 SER B 123 OG 75.4 88.4 155.1 73.5 115.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 127 OD1
REMARK 620 2 ASP B 127 OD2 40.8
REMARK 620 3 SER B 123 O 80.4 118.4
REMARK 620 4 ASP B 126 OD1 99.4 97.5 70.9
REMARK 620 5 ASP B 126 OD2 92.9 65.7 113.0 44.3
REMARK 620 6 ASP B 251 OD2 88.5 112.5 72.7 140.8 174.3
REMARK 620 7 HOH B1406 O 156.1 160.8 80.8 88.1 107.9 72.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 158 OD2
REMARK 620 2 ASN B 215 OD1 96.3
REMARK 620 3 ASP B 217 O 170.5 90.8
REMARK 620 4 ASP B 217 OD1 99.0 95.4 74.1
REMARK 620 5 GLU B 220 OE2 89.8 78.4 97.7 169.8
REMARK 620 6 PRO B 219 O 92.6 159.0 82.7 101.9 82.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1411 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 252 OE1
REMARK 620 2 ASP C 245 OD1 73.9
REMARK 620 3 ASP C 247 O 150.9 100.4
REMARK 620 4 THR C 250 OG1 75.6 80.1 75.3
REMARK 620 5 GLU C 243 OE1 118.2 89.9 89.9 160.2
REMARK 620 6 GLU C 243 OE2 115.7 141.3 86.9 137.9 51.9
REMARK 620 7 THR C 250 O 84.4 148.7 87.8 72.8 120.5 68.6
REMARK 620 8 GLU C 252 OE2 39.5 88.9 167.9 114.2 82.4 81.1 88.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1412 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 305 OD2
REMARK 620 2 ASN C 299 OD1 81.7
REMARK 620 3 ASP C 301 OD2 155.6 82.6
REMARK 620 4 ASP C 301 OD1 142.4 70.5 44.8
REMARK 620 5 ASP C 297 OD1 75.1 68.7 116.0 71.5
REMARK 620 6 ASP C 305 OD1 56.2 109.2 112.7 157.4 130.3
REMARK 620 7 ARG C 303 O 96.4 140.3 107.6 89.7 72.5 102.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1413 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 365 OD1
REMARK 620 2 ASP C 367 OD1 92.3
REMARK 620 3 ASP C 369 OD1 84.9 73.8
REMARK 620 4 TYR C 371 O 91.1 162.0 88.9
REMARK 620 5 ASP C 373 OD2 103.9 84.5 157.0 111.7
REMARK 620 6 ASP C 373 OD1 146.7 102.4 127.8 84.0 49.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1414 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 434 OD1
REMARK 620 2 ASP C 434 OD2 48.8
REMARK 620 3 TYR C 432 O 98.3 96.1
REMARK 620 4 ASN C 430 OD1 143.4 160.7 95.8
REMARK 620 5 ASP C 428 OD1 100.1 85.0 156.3 78.1
REMARK 620 6 ASP C 426 OD1 136.7 87.9 84.3 78.2 72.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1408 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC D1302 O2
REMARK 620 2 SER D 123 OG 80.6
REMARK 620 3 SER D 121 OG 71.7 96.5
REMARK 620 4 GLU D 220 OE1 93.7 163.7 96.2
REMARK 620 5 HOH D1412 O 154.0 83.0 90.4 107.1
REMARK 620 6 HOH D1411 O 105.3 82.4 177.0 84.5 92.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D1409 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 126 OD1
REMARK 620 2 ASP D 126 OD2 43.7
REMARK 620 3 SER D 123 O 76.2 118.5
REMARK 620 4 ASP D 127 OD1 88.2 102.0 84.5
REMARK 620 5 ASP D 251 OD2 148.3 167.1 72.3 85.5
REMARK 620 6 HOH D1413 O 122.8 106.6 94.3 147.9 63.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D1410 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 220 OE2
REMARK 620 2 ASN D 215 OD1 84.8
REMARK 620 3 ASP D 217 O 97.6 93.3
REMARK 620 4 PRO D 219 O 92.3 169.9 77.5
REMARK 620 5 ASP D 217 OD1 163.3 86.9 68.4 93.4
REMARK 620 6 ASP D 158 OD2 98.0 102.9 158.4 87.1 98.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1418 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 250 OG1
REMARK 620 2 GLU E 243 OE1 145.9
REMARK 620 3 ASP E 247 O 91.1 70.4
REMARK 620 4 THR E 250 O 77.2 72.3 82.8
REMARK 620 5 ASP E 245 OD1 87.7 124.5 106.6 162.4
REMARK 620 6 GLU E 243 OE2 157.0 51.4 82.8 123.6 73.1
REMARK 620 7 GLU E 252 OE2 110.2 88.0 157.8 95.7 81.1 79.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1419 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 299 OD1
REMARK 620 2 ASP E 305 OD2 85.9
REMARK 620 3 ASP E 297 OD1 72.3 82.8
REMARK 620 4 ASP E 305 OD1 109.2 57.3 139.3
REMARK 620 5 ASP E 301 OD2 81.9 153.1 115.8 104.5
REMARK 620 6 ARG E 303 O 153.5 99.8 82.7 95.4 101.8
REMARK 620 7 ASP E 301 OD1 73.6 150.7 71.3 149.4 44.9 90.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1420 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 373 OD2
REMARK 620 2 ASP E 365 OD1 97.7
REMARK 620 3 TYR E 371 O 104.2 94.1
REMARK 620 4 ASP E 369 OD1 167.2 78.0 88.3
REMARK 620 5 ASP E 367 OD1 91.1 76.8 163.3 76.2
REMARK 620 6 ASP E 373 OD1 50.7 148.2 91.6 133.5 103.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1421 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 426 OD1
REMARK 620 2 ASP E 428 OD1 92.9
REMARK 620 3 ASN E 430 OD1 80.6 79.8
REMARK 620 4 TYR E 432 O 70.2 162.9 94.4
REMARK 620 5 ASP E 434 OD1 146.5 99.3 132.1 96.5
REMARK 620 6 ASP E 434 OD2 95.9 92.0 170.9 92.3 53.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F1415 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC F1303 O2
REMARK 620 2 HOH F1419 O 151.8
REMARK 620 3 GLU F 220 OE1 104.4 103.7
REMARK 620 4 SER F 123 OG 76.3 80.7 150.6
REMARK 620 5 SER F 121 OG 81.9 90.1 100.9 108.2
REMARK 620 6 HOH F1418 O 97.5 91.5 77.0 73.9 177.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F1416 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 126 OD1
REMARK 620 2 SER F 123 O 94.2
REMARK 620 3 ASP F 127 OD1 93.8 82.6
REMARK 620 4 ASP F 251 OD2 155.3 62.5 75.9
REMARK 620 5 HOH F1420 O 101.3 82.7 159.6 84.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F1417 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 217 O
REMARK 620 2 ASP F 217 OD1 72.0
REMARK 620 3 PRO F 219 O 82.5 93.1
REMARK 620 4 ASP F 158 OD2 159.8 89.7 90.3
REMARK 620 5 GLU F 220 OE2 103.6 173.1 91.4 95.4
REMARK 620 6 ASN F 215 OD1 93.4 86.4 175.8 93.8 88.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1013
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 1014
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 1015
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 1016
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 1017
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN F 1018
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA F 1019
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 1020
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC D 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC F 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1405
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1406
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1407
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 1409
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 1410
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1411
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1412
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1413
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1414
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 1415
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 1416
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 1417
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1419
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1420
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1421
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TXV RELATED DB: PDB
REMARK 900 NON-DRUG BOUND HIGHER RESOLUTION STRUCTURE COMPLEXED WITH
REMARK 900 10E5 FAB
REMARK 900 RELATED ID: 1TY3 RELATED DB: PDB
REMARK 900 NON-DRUG BOUND STRUCTURE COMPLEXED WITH 10E5 FAB
REMARK 900 RELATED ID: 1TY5 RELATED DB: PDB
REMARK 900 TIROFIBAN BOUND STRUCTURE COMPLEXED WITH 10E5 FAB
REMARK 900 RELATED ID: 1TY6 RELATED DB: PDB
REMARK 900 EPTIFIBATIDE BOUND STRUCTURE COMPLEXED WITH 10E5 FAB
REMARK 900 RELATED ID: 1TY7 RELATED DB: PDB
REMARK 900 MERCK COMPOUND L739758 BOUND STRUCTURE COMPLEXED WITH 10E5
REMARK 900 FAB
DBREF 1TYE A 1 452 UNP P08514 ITAB_HUMAN 32 483
DBREF 1TYE C 1 452 UNP P08514 ITAB_HUMAN 32 483
DBREF 1TYE E 1 452 UNP P08514 ITAB_HUMAN 32 483
DBREF 1TYE B 1 440 UNP P05106 ITB3_HUMAN 27 466
DBREF 1TYE D 1 440 UNP P05106 ITB3_HUMAN 27 466
DBREF 1TYE F 1 440 UNP P05106 ITB3_HUMAN 27 466
SEQRES 1 A 452 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 A 452 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 A 452 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 A 452 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 A 452 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 A 452 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 A 452 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 A 452 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 A 452 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 A 452 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 A 452 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 A 452 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 A 452 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 A 452 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 A 452 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 A 452 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 A 452 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 A 452 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 A 452 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 A 452 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 A 452 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 A 452 TYR GLN ARG LEU HIS ARG LEU ARG ALA GLU GLN MET ALA
SEQRES 23 A 452 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 A 452 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 A 452 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 A 452 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 A 452 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 A 452 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 A 452 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 A 452 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 A 452 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 A 452 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 A 452 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 A 452 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 A 452 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO
SEQRES 1 B 440 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 B 440 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 B 440 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 B 440 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 B 440 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 B 440 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 B 440 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 B 440 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 B 440 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 B 440 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 B 440 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 B 440 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 B 440 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 B 440 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 B 440 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 B 440 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 B 440 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 B 440 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 B 440 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 B 440 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 B 440 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 B 440 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 B 440 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 B 440 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 B 440 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 B 440 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 B 440 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 B 440 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 B 440 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 B 440 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 B 440 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 B 440 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 B 440 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 B 440 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN
SEQRES 1 C 452 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 C 452 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 C 452 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 C 452 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 C 452 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 C 452 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 C 452 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 C 452 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 C 452 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 C 452 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 C 452 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 C 452 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 C 452 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 C 452 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 C 452 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 C 452 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 C 452 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 C 452 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 C 452 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 C 452 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 C 452 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 C 452 TYR GLN ARG LEU HIS ARG LEU ARG ALA GLU GLN MET ALA
SEQRES 23 C 452 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 C 452 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 C 452 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 C 452 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 C 452 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 C 452 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 C 452 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 C 452 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 C 452 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 C 452 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 C 452 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 C 452 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 C 452 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO
SEQRES 1 D 440 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 D 440 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 D 440 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 D 440 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 D 440 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 D 440 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 D 440 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 D 440 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 D 440 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 D 440 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 D 440 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 D 440 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 D 440 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 D 440 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 D 440 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 D 440 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 D 440 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 D 440 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 D 440 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 D 440 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 D 440 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 D 440 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 D 440 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 D 440 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 D 440 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 D 440 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 D 440 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 D 440 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 D 440 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 D 440 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 D 440 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 D 440 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 D 440 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 D 440 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN
SEQRES 1 E 452 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 E 452 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 E 452 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 E 452 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 E 452 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 E 452 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 E 452 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 E 452 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 E 452 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 E 452 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 E 452 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 E 452 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 E 452 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 E 452 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 E 452 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 E 452 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 E 452 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 E 452 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 E 452 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 E 452 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 E 452 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 E 452 TYR GLN ARG LEU HIS ARG LEU ARG ALA GLU GLN MET ALA
SEQRES 23 E 452 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 E 452 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 E 452 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 E 452 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 E 452 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 E 452 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 E 452 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 E 452 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 E 452 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 E 452 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 E 452 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 E 452 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 E 452 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO
SEQRES 1 F 440 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 F 440 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 F 440 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 F 440 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 F 440 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 F 440 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 F 440 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 F 440 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 F 440 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 F 440 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 F 440 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 F 440 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 F 440 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 F 440 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 F 440 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 F 440 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 F 440 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 F 440 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 F 440 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 F 440 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 F 440 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 F 440 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 F 440 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 F 440 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 F 440 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 F 440 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 F 440 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 F 440 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 F 440 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 F 440 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 F 440 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 F 440 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 F 440 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 F 440 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN
MODRES 1TYE ASN B 99 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN B 320 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN B 371 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN D 99 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN D 320 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN D 371 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN E 15 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN F 99 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN F 320 ASN GLYCOSYLATION SITE
MODRES 1TYE ASN F 371 ASN GLYCOSYLATION SITE
HET NAG B1001 14
HET NAG B1002 14
HET NAG B1003 14
HET MAN B1004 11
HET BMA B1005 11
HET NAG B1006 14
HET NAG D1007 14
HET NAG D1008 14
HET NAG D1009 14
HET MAN D1010 11
HET BMA D1011 11
HET MAN D1012 11
HET NAG D1013 14
HET NAG E1014 14
HET NAG F1015 14
HET NAG F1016 14
HET NAG F1017 14
HET MAN F1018 11
HET BMA F1019 11
HET NAG F1020 14
HET CAC B1301 5
HET CAC D1302 5
HET CAC F1303 5
HET MG B1401 1
HET CA B1402 1
HET CA B1403 1
HET CA A1404 1
HET CA A1405 1
HET CA A1406 1
HET CA A1407 1
HET MG D1408 1
HET CA D1409 1
HET CA D1410 1
HET CA C1411 1
HET CA C1412 1
HET CA C1413 1
HET CA C1414 1
HET MG F1415 1
HET CA F1416 1
HET CA F1417 1
HET CA E1418 1
HET CA E1419 1
HET CA E1420 1
HET CA E1421 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM BMA BETA-D-MANNOSE
HETNAM CAC CACODYLATE ION
HETNAM MG MAGNESIUM ION
HETNAM CA CALCIUM ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 7 NAG 13(C8 H15 N O6)
FORMUL 8 MAN 4(C6 H12 O6)
FORMUL 8 BMA 3(C6 H12 O6)
FORMUL 17 CAC 3(C2 H6 AS O2 1-)
FORMUL 20 MG 3(MG 2+)
FORMUL 21 CA 18(CA 2+)
FORMUL 41 HOH *120(H2 O)
HELIX 1 1 LEU A 151 ASP A 159 1 9
HELIX 2 2 GLY A 187 LEU A 192 1 6
HELIX 3 3 VAL A 200 TYR A 207 1 8
HELIX 4 4 ASN A 227 PHE A 231 5 5
HELIX 5 5 THR A 259 LEU A 264 1 6
HELIX 6 6 TYR A 440 ALA A 442 5 3
HELIX 7 7 SER B 12 ALA B 18 1 7
HELIX 8 8 LEU B 40 ASP B 47 1 8
HELIX 9 9 SER B 121 ASP B 126 5 6
HELIX 10 10 ASP B 127 THR B 146 1 20
HELIX 11 11 PRO B 169 GLU B 174 5 6
HELIX 12 12 ASN B 175 LYS B 181 5 7
HELIX 13 13 GLN B 199 LYS B 208 1 10
HELIX 14 14 GLY B 221 CYS B 232 1 12
HELIX 15 15 CYS B 232 GLY B 237 1 6
HELIX 16 16 LEU B 258 GLY B 264 5 7
HELIX 17 17 TYR B 281 THR B 286 5 6
HELIX 18 18 SER B 291 LYS B 302 1 12
HELIX 19 19 VAL B 314 LEU B 324 1 11
HELIX 20 20 SER B 337 LYS B 350 1 14
HELIX 21 21 LEU C 151 ASP C 159 1 9
HELIX 22 22 GLY C 187 LEU C 192 1 6
HELIX 23 23 VAL C 200 TYR C 207 1 8
HELIX 24 24 THR C 259 LEU C 264 1 6
HELIX 25 25 SER D 12 SER D 20 1 9
HELIX 26 26 LYS D 41 ASP D 47 1 7
HELIX 27 27 ALA D 50 GLU D 52 5 3
HELIX 28 28 SER D 121 LYS D 125 5 5
HELIX 29 29 ASP D 127 LYS D 144 1 18
HELIX 30 30 PRO D 169 GLU D 174 5 6
HELIX 31 31 CYS D 177 LYS D 181 5 5
HELIX 32 32 GLN D 199 LYS D 209 1 11
HELIX 33 33 GLY D 221 CYS D 232 1 12
HELIX 34 34 CYS D 232 GLY D 237 1 6
HELIX 35 35 ASP D 259 GLY D 264 5 6
HELIX 36 36 TYR D 281 THR D 286 5 6
HELIX 37 37 SER D 291 LYS D 302 1 12
HELIX 38 38 VAL D 314 GLU D 323 1 10
HELIX 39 39 SER D 337 GLY D 349 1 13
HELIX 40 40 GLY E 44 GLU E 48 5 5
HELIX 41 41 LEU E 151 ASP E 159 1 9
HELIX 42 42 GLY E 187 LEU E 192 1 6
HELIX 43 43 VAL E 200 TYR E 207 1 8
HELIX 44 44 ASN E 227 PHE E 231 5 5
HELIX 45 45 THR E 259 LEU E 264 1 6
HELIX 46 46 ASN F 3 ARG F 8 1 6
HELIX 47 47 SER F 12 LEU F 17 1 6
HELIX 48 48 SER F 121 ASP F 126 5 6
HELIX 49 49 ASP F 127 LYS F 144 1 18
HELIX 50 50 PRO F 169 GLU F 174 5 6
HELIX 51 51 CYS F 177 LYS F 181 5 5
HELIX 52 52 GLN F 199 LYS F 208 1 10
HELIX 53 53 GLY F 221 CYS F 232 1 12
HELIX 54 54 CYS F 232 GLY F 237 1 6
HELIX 55 55 LEU F 258 GLY F 264 5 7
HELIX 56 56 SER F 291 LYS F 302 1 12
HELIX 57 57 VAL F 314 ILE F 325 1 12
HELIX 58 58 SER F 337 GLY F 349 1 13
SHEET 1 A 5 GLY A 62 GLY A 63 0
SHEET 2 A 5 THR A 9 ALA A 12 1 N PHE A 10 O GLY A 63
SHEET 3 A 5 GLN A 444 TYR A 448 -1 O VAL A 447 N THR A 9
SHEET 4 A 5 ASP A 434 ALA A 439 -1 N VAL A 437 O ALA A 446
SHEET 5 A 5 SER A 420 VAL A 425 -1 N ARG A 422 O ILE A 436
SHEET 1 B 4 LEU A 23 HIS A 26 0
SHEET 2 B 4 ALA A 34 ALA A 39 -1 O ALA A 34 N HIS A 26
SHEET 3 B 4 GLY A 52 PRO A 57 -1 O PHE A 54 N VAL A 37
SHEET 4 B 4 SER A 67 LEU A 68 -1 O LEU A 68 N VAL A 53
SHEET 1 C 4 GLU A 75 VAL A 79 0
SHEET 2 C 4 GLN A 82 PHE A 87 -1 O LEU A 84 N ARG A 77
SHEET 3 C 4 HIS A 112 GLU A 117 -1 O ASN A 114 N GLN A 85
SHEET 4 C 4 GLU A 120 GLU A 121 -1 O GLU A 120 N GLU A 117
SHEET 1 D 4 GLU A 75 VAL A 79 0
SHEET 2 D 4 GLN A 82 PHE A 87 -1 O LEU A 84 N ARG A 77
SHEET 3 D 4 HIS A 112 GLU A 117 -1 O ASN A 114 N GLN A 85
SHEET 4 D 4 THR A 125 PRO A 126 -1 O THR A 125 N TRP A 113
SHEET 1 E 4 VAL A 97 TRP A 100 0
SHEET 2 E 4 VAL A 103 ALA A 108 -1 O VAL A 103 N TRP A 100
SHEET 3 E 4 SER A 129 GLN A 134 -1 O PHE A 131 N ALA A 106
SHEET 4 E 4 ARG A 139 TYR A 143 -1 O TYR A 143 N CYS A 130
SHEET 1 F 4 SER A 172 VAL A 175 0
SHEET 2 F 4 GLU A 180 ALA A 185 -1 O VAL A 182 N VAL A 174
SHEET 3 F 4 LEU A 194 PRO A 199 -1 O ALA A 196 N LEU A 183
SHEET 4 F 4 SER A 220 LEU A 221 -1 O SER A 220 N GLN A 197
SHEET 1 G 4 VAL A 239 GLY A 242 0
SHEET 2 G 4 GLU A 252 ALA A 257 -1 O VAL A 254 N ALA A 240
SHEET 3 G 4 ALA A 266 LEU A 270 -1 O LEU A 270 N TYR A 253
SHEET 4 G 4 ARG A 276 ARG A 281 -1 O LEU A 277 N ILE A 269
SHEET 1 H 4 VAL A 293 THR A 296 0
SHEET 2 H 4 ASP A 305 GLY A 309 -1 O LEU A 307 N ALA A 294
SHEET 3 H 4 ARG A 327 PHE A 331 -1 O PHE A 331 N LEU A 306
SHEET 4 H 4 LEU A 345 THR A 348 -1 O LEU A 347 N VAL A 328
SHEET 1 I 2 MET A 314 ARG A 317 0
SHEET 2 I 2 LYS A 321 GLU A 324 -1 O ALA A 323 N GLU A 315
SHEET 1 J 4 ILE A 360 PRO A 362 0
SHEET 2 J 4 ILE A 374 ALA A 378 -1 O ALA A 375 N ALA A 361
SHEET 3 J 4 GLN A 388 PHE A 392 -1 O LEU A 390 N VAL A 376
SHEET 4 J 4 GLN A 405 ASP A 408 -1 O GLN A 405 N VAL A 391
SHEET 1 K 6 ARG B 62 GLU B 65 0
SHEET 2 K 6 ARG B 87 LEU B 92 -1 O ALA B 89 N ARG B 62
SHEET 3 K 6 LEU B 425 PHE B 431 1 O GLN B 428 N LEU B 90
SHEET 4 K 6 GLU B 411 PRO B 418 -1 N PHE B 414 O VAL B 427
SHEET 5 K 6 SER B 353 ARG B 360 -1 N ARG B 360 O THR B 415
SHEET 6 K 6 SER B 385 LEU B 389 -1 O LEU B 389 N SER B 353
SHEET 1 L 4 SER B 97 ARG B 105 0
SHEET 2 L 4 THR B 394 VAL B 403 -1 O VAL B 395 N VAL B 104
SHEET 3 L 4 LEU B 366 THR B 373 -1 N SER B 367 O LYS B 402
SHEET 4 L 4 VAL B 379 PRO B 381 -1 O ILE B 380 N ALA B 372
SHEET 1 M 6 TYR B 190 THR B 197 0
SHEET 2 M 6 LEU B 149 PHE B 156 -1 N ALA B 155 O LYS B 191
SHEET 3 M 6 VAL B 112 ASP B 119 1 N MET B 118 O GLY B 154
SHEET 4 M 6 SER B 243 THR B 250 1 O LEU B 245 N ASP B 113
SHEET 5 M 6 ILE B 304 VAL B 310 1 O ALA B 309 N PHE B 248
SHEET 6 M 6 THR B 329 VAL B 332 1 O GLY B 331 N PHE B 308
SHEET 1 N 4 LEU C 8 ALA C 12 0
SHEET 2 N 4 GLN C 444 TYR C 448 -1 O VAL C 445 N TYR C 11
SHEET 3 N 4 ASP C 434 ALA C 439 -1 N LEU C 435 O TYR C 448
SHEET 4 N 4 SER C 420 VAL C 425 -1 N ARG C 422 O ILE C 436
SHEET 1 O 3 LEU C 23 LYS C 27 0
SHEET 2 O 3 VAL C 33 GLY C 38 -1 O VAL C 36 N ASP C 24
SHEET 3 O 3 VAL C 53 PRO C 57 -1 O CYS C 56 N ILE C 35
SHEET 1 P 4 THR C 76 VAL C 79 0
SHEET 2 P 4 GLN C 82 PHE C 87 -1 O LEU C 84 N ARG C 77
SHEET 3 P 4 HIS C 112 GLU C 117 -1 O HIS C 112 N PHE C 87
SHEET 4 P 4 GLU C 120 GLU C 121 -1 O GLU C 120 N GLU C 117
SHEET 1 Q 4 VAL C 97 TRP C 100 0
SHEET 2 Q 4 VAL C 103 ALA C 108 -1 O VAL C 105 N VAL C 98
SHEET 3 Q 4 SER C 129 ALA C 133 -1 O PHE C 131 N ALA C 106
SHEET 4 Q 4 ARG C 140 TYR C 143 -1 O ALA C 141 N LEU C 132
SHEET 1 R 4 SER C 172 VAL C 175 0
SHEET 2 R 4 GLU C 180 ALA C 185 -1 O VAL C 182 N VAL C 174
SHEET 3 R 4 LEU C 194 PRO C 199 -1 O ALA C 196 N LEU C 183
SHEET 4 R 4 SER C 220 LEU C 221 -1 O SER C 220 N GLN C 197
SHEET 1 S 4 VAL C 239 GLY C 242 0
SHEET 2 S 4 GLU C 252 ALA C 257 -1 O VAL C 254 N ALA C 240
SHEET 3 S 4 ALA C 266 ASP C 271 -1 O LEU C 270 N TYR C 253
SHEET 4 S 4 ARG C 276 ARG C 281 -1 O LEU C 277 N ILE C 269
SHEET 1 T 4 VAL C 293 THR C 296 0
SHEET 2 T 4 ASP C 305 ALA C 310 -1 O ASP C 305 N THR C 296
SHEET 3 T 4 ARG C 327 PHE C 331 -1 O PHE C 331 N LEU C 306
SHEET 4 T 4 LEU C 345 THR C 348 -1 O LEU C 347 N VAL C 328
SHEET 1 U 2 MET C 314 ARG C 317 0
SHEET 2 U 2 LYS C 321 GLU C 324 -1 O ALA C 323 N GLU C 315
SHEET 1 V 4 ILE C 360 PRO C 362 0
SHEET 2 V 4 ILE C 374 ALA C 378 -1 O ALA C 375 N ALA C 361
SHEET 3 V 4 GLN C 388 PHE C 392 -1 O LEU C 390 N VAL C 376
SHEET 4 V 4 VAL C 406 ASP C 408 -1 O LEU C 407 N VAL C 389
SHEET 1 W 2 GLY C 394 GLN C 395 0
SHEET 2 W 2 GLY C 398 LEU C 399 -1 O GLY C 398 N GLN C 395
SHEET 1 X 3 CYS D 38 LEU D 40 0
SHEET 2 X 3 CYS D 23 CYS D 26 -1 N ALA D 24 O ASP D 39
SHEET 3 X 3 ILE D 54 GLU D 55 -1 O GLU D 55 N TRP D 25
SHEET 1 Y 6 ARG D 62 GLU D 65 0
SHEET 2 Y 6 ARG D 87 LEU D 92 -1 O ALA D 89 N ARG D 62
SHEET 3 Y 6 LEU D 425 PHE D 431 1 O GLN D 428 N ILE D 88
SHEET 4 Y 6 GLU D 411 PRO D 418 -1 N PHE D 414 O VAL D 427
SHEET 5 Y 6 SER D 353 ARG D 360 -1 N ARG D 360 O THR D 415
SHEET 6 Y 6 SER D 385 LEU D 389 -1 O LEU D 389 N SER D 353
SHEET 1 Z 4 SER D 97 ARG D 105 0
SHEET 2 Z 4 THR D 394 VAL D 403 -1 O VAL D 395 N VAL D 104
SHEET 3 Z 4 LEU D 366 THR D 373 -1 N SER D 367 O LYS D 402
SHEET 4 Z 4 VAL D 379 PRO D 381 -1 O ILE D 380 N ALA D 372
SHEET 1 AA 6 TYR D 190 THR D 197 0
SHEET 2 AA 6 LEU D 149 PHE D 156 -1 N ILE D 151 O THR D 197
SHEET 3 AA 6 VAL D 112 ASP D 119 1 N MET D 118 O GLY D 154
SHEET 4 AA 6 SER D 243 THR D 250 1 O SER D 243 N ASP D 113
SHEET 5 AA 6 ILE D 304 THR D 311 1 O ALA D 309 N PHE D 248
SHEET 6 AA 6 THR D 329 LEU D 333 1 O THR D 329 N PHE D 308
SHEET 1 AB 5 GLY E 63 GLN E 64 0
SHEET 2 AB 5 THR E 9 ALA E 12 1 N PHE E 10 O GLY E 63
SHEET 3 AB 5 GLN E 444 TYR E 448 -1 O VAL E 447 N THR E 9
SHEET 4 AB 5 ASP E 434 ALA E 439 -1 N LEU E 435 O TYR E 448
SHEET 5 AB 5 SER E 420 VAL E 425 -1 N ARG E 422 O ILE E 436
SHEET 1 AC 3 LEU E 23 LYS E 27 0
SHEET 2 AC 3 VAL E 33 GLY E 38 -1 O ALA E 34 N HIS E 26
SHEET 3 AC 3 VAL E 53 PRO E 57 -1 O CYS E 56 N ILE E 35
SHEET 1 AD 4 GLU E 75 VAL E 79 0
SHEET 2 AD 4 GLN E 82 PHE E 87 -1 O LEU E 84 N ARG E 77
SHEET 3 AD 4 HIS E 112 GLU E 117 -1 O HIS E 112 N PHE E 87
SHEET 4 AD 4 GLU E 120 GLU E 121 -1 O GLU E 120 N GLU E 117
SHEET 1 AE 4 GLU E 75 VAL E 79 0
SHEET 2 AE 4 GLN E 82 PHE E 87 -1 O LEU E 84 N ARG E 77
SHEET 3 AE 4 HIS E 112 GLU E 117 -1 O HIS E 112 N PHE E 87
SHEET 4 AE 4 THR E 125 PRO E 126 -1 O THR E 125 N TRP E 113
SHEET 1 AF 4 VAL E 97 TRP E 100 0
SHEET 2 AF 4 VAL E 103 ALA E 108 -1 O VAL E 103 N TRP E 100
SHEET 3 AF 4 SER E 129 ALA E 133 -1 O SER E 129 N ALA E 108
SHEET 4 AF 4 ARG E 140 TYR E 143 -1 O ALA E 141 N LEU E 132
SHEET 1 AG 4 SER E 173 VAL E 175 0
SHEET 2 AG 4 GLU E 180 ALA E 185 -1 O VAL E 182 N VAL E 174
SHEET 3 AG 4 LEU E 194 PRO E 199 -1 O ALA E 196 N LEU E 183
SHEET 4 AG 4 SER E 220 LEU E 221 -1 O SER E 220 N GLN E 197
SHEET 1 AH 4 VAL E 239 GLY E 242 0
SHEET 2 AH 4 GLU E 252 ALA E 257 -1 O VAL E 254 N ALA E 240
SHEET 3 AH 4 ALA E 266 LEU E 270 -1 O ALA E 266 N ALA E 257
SHEET 4 AH 4 ARG E 276 ARG E 281 -1 O LEU E 277 N ILE E 269
SHEET 1 AI 4 VAL E 293 THR E 296 0
SHEET 2 AI 4 ASP E 305 ALA E 310 -1 O LEU E 307 N ALA E 294
SHEET 3 AI 4 ARG E 327 PHE E 331 -1 O PHE E 331 N LEU E 306
SHEET 4 AI 4 LEU E 345 THR E 348 -1 O LEU E 347 N VAL E 328
SHEET 1 AJ 2 MET E 314 ARG E 317 0
SHEET 2 AJ 2 LYS E 321 GLU E 324 -1 O ALA E 323 N GLU E 315
SHEET 1 AK 4 ILE E 360 PRO E 362 0
SHEET 2 AK 4 ILE E 374 ALA E 378 -1 O ALA E 375 N ALA E 361
SHEET 3 AK 4 GLN E 388 PHE E 392 -1 O PHE E 392 N ILE E 374
SHEET 4 AK 4 GLN E 405 ASP E 408 -1 O LEU E 407 N VAL E 389
SHEET 1 AL 2 GLY E 394 GLN E 395 0
SHEET 2 AL 2 GLY E 398 LEU E 399 -1 O GLY E 398 N GLN E 395
SHEET 1 AM 6 ARG F 62 GLU F 65 0
SHEET 2 AM 6 ARG F 87 LEU F 92 -1 O ALA F 89 N ARG F 62
SHEET 3 AM 6 ILE F 426 PHE F 431 1 O THR F 430 N LEU F 90
SHEET 4 AM 6 GLU F 411 VAL F 419 -1 N PHE F 414 O VAL F 427
SHEET 5 AM 6 SER F 353 ARG F 360 -1 N GLU F 356 O VAL F 419
SHEET 6 AM 6 SER F 385 LEU F 389 -1 O CYS F 386 N VAL F 355
SHEET 1 AN 4 SER F 97 ARG F 105 0
SHEET 2 AN 4 THR F 394 VAL F 403 -1 O VAL F 395 N VAL F 104
SHEET 3 AN 4 LEU F 366 THR F 373 -1 N THR F 373 O SER F 396
SHEET 4 AN 4 VAL F 379 PRO F 381 -1 O ILE F 380 N ALA F 372
SHEET 1 AO 6 TYR F 190 THR F 197 0
SHEET 2 AO 6 LEU F 149 PHE F 156 -1 N ALA F 155 O LYS F 191
SHEET 3 AO 6 VAL F 112 ASP F 119 1 N TYR F 116 O GLY F 152
SHEET 4 AO 6 SER F 243 THR F 250 1 O SER F 243 N ASP F 113
SHEET 5 AO 6 ASN F 305 THR F 311 1 O ALA F 309 N PHE F 248
SHEET 6 AO 6 THR F 329 LEU F 333 1 O GLY F 331 N PHE F 308
SSBOND 1 CYS A 56 CYS A 65 1555 1555 2.04
SSBOND 2 CYS A 107 CYS A 130 1555 1555 2.05
SSBOND 3 CYS A 146 CYS A 167 1555 1555 2.03
SSBOND 4 CYS B 5 CYS B 23 1555 1555 2.03
SSBOND 5 CYS B 13 CYS B 435 1555 1555 2.04
SSBOND 6 CYS B 16 CYS B 38 1555 1555 2.03
SSBOND 7 CYS B 26 CYS B 49 1555 1555 2.03
SSBOND 8 CYS B 177 CYS B 184 1555 1555 2.04
SSBOND 9 CYS B 232 CYS B 273 1555 1555 2.04
SSBOND 10 CYS B 374 CYS B 386 1555 1555 2.04
SSBOND 11 CYS B 406 CYS B 433 1555 1555 2.06
SSBOND 12 CYS C 56 CYS C 65 1555 1555 2.03
SSBOND 13 CYS C 107 CYS C 130 1555 1555 2.05
SSBOND 14 CYS C 146 CYS C 167 1555 1555 2.04
SSBOND 15 CYS D 5 CYS D 23 1555 1555 2.03
SSBOND 16 CYS D 13 CYS D 435 1555 1555 2.03
SSBOND 17 CYS D 16 CYS D 38 1555 1555 2.04
SSBOND 18 CYS D 26 CYS D 49 1555 1555 2.02
SSBOND 19 CYS D 177 CYS D 184 1555 1555 2.05
SSBOND 20 CYS D 232 CYS D 273 1555 1555 2.04
SSBOND 21 CYS D 374 CYS D 386 1555 1555 2.03
SSBOND 22 CYS D 406 CYS D 433 1555 1555 2.02
SSBOND 23 CYS E 56 CYS E 65 1555 1555 2.03
SSBOND 24 CYS E 107 CYS E 130 1555 1555 2.05
SSBOND 25 CYS E 146 CYS E 167 1555 1555 2.04
SSBOND 26 CYS F 5 CYS F 23 1555 1555 1.96
SSBOND 27 CYS F 13 CYS F 435 1555 1555 2.05
SSBOND 28 CYS F 16 CYS F 38 1555 1555 2.03
SSBOND 29 CYS F 26 CYS F 49 1555 1555 2.03
SSBOND 30 CYS F 177 CYS F 184 1555 1555 2.05
SSBOND 31 CYS F 232 CYS F 273 1555 1555 2.04
SSBOND 32 CYS F 374 CYS F 386 1555 1555 2.04
SSBOND 33 CYS F 406 CYS F 433 1555 1555 2.03
LINK ND2 ASN B 99 C1 NAG B1001 1555 1555 1.45
LINK ND2 ASN B 320 C1 NAG B1002 1555 1555 1.45
LINK ND2 ASN B 371 C1 NAG B1006 1555 1555 1.45
LINK ND2 ASN D 99 C1 NAG D1007 1555 1555 1.45
LINK ND2 ASN D 320 C1 NAG D1008 1555 1555 1.45
LINK ND2 ASN D 371 C1 NAG D1013 1555 1555 1.45
LINK ND2 ASN E 15 C1 NAG E1014 1555 1555 1.45
LINK ND2 ASN F 99 C1 NAG F1015 1555 1555 1.45
LINK ND2 ASN F 320 C1 NAG F1016 1555 1555 1.45
LINK ND2 ASN F 371 C1 NAG F1020 1555 1555 1.45
LINK O4 NAG B1002 C1 NAG B1003 1555 1555 1.39
LINK O4 NAG B1003 C1 MAN B1004 1555 1555 1.40
LINK O3 MAN B1004 C1 BMA B1005 1555 1555 1.40
LINK O4 NAG D1008 C1 NAG D1009 1555 1555 1.38
LINK O4 NAG D1009 C1 MAN D1010 1555 1555 1.39
LINK O3 MAN D1010 C1 BMA D1011 1555 1555 1.40
LINK O6 MAN D1010 C1 MAN D1012 1555 1555 1.41
LINK O4 NAG F1016 C1 NAG F1017 1555 1555 1.38
LINK O4 NAG F1017 C1 MAN F1018 1555 1555 1.40
LINK O3 MAN F1018 C1 BMA F1019 1555 1555 1.40
LINK CA CA A1404 OE1 GLU A 243 1555 1555 2.63
LINK CA CA A1404 O ASP A 247 1555 1555 2.09
LINK CA CA A1404 O THR A 250 1555 1555 2.01
LINK CA CA A1404 OD1 ASP A 245 1555 1555 2.28
LINK CA CA A1404 OG1 THR A 250 1555 1555 2.60
LINK CA CA A1404 OE1 GLU A 252 1555 1555 3.20
LINK CA CA A1404 OE2 GLU A 252 1555 1555 2.27
LINK CA CA A1404 OE2 GLU A 243 1555 1555 2.47
LINK CA CA A1405 OD1 ASN A 299 1555 1555 2.65
LINK CA CA A1405 OD1 ASP A 305 1555 1555 2.53
LINK CA CA A1405 OD2 ASP A 305 1555 1555 2.40
LINK CA CA A1405 OD1 ASP A 297 1555 1555 2.41
LINK CA CA A1405 OD1 ASP A 301 1555 1555 2.38
LINK CA CA A1405 OD2 ASP A 301 1555 1555 3.18
LINK CA CA A1405 O ARG A 303 1555 1555 2.43
LINK CA CA A1406 OD1 ASP A 373 1555 1555 2.64
LINK CA CA A1406 OD1 ASP A 367 1555 1555 2.07
LINK CA CA A1406 OD1 ASP A 365 1555 1555 2.06
LINK CA CA A1406 O TYR A 371 1555 1555 2.12
LINK CA CA A1406 OD2 ASP A 373 1555 1555 2.76
LINK CA CA A1406 OD1 ASP A 369 1555 1555 2.65
LINK CA CA A1407 OD1 ASP A 434 1555 1555 2.67
LINK CA CA A1407 OD1 ASP A 428 1555 1555 2.20
LINK CA CA A1407 OD2 ASP A 434 1555 1555 2.62
LINK CA CA A1407 OD1 ASP A 426 1555 1555 2.67
LINK CA CA A1407 OD2 ASP A 428 1555 1555 3.10
LINK CA CA A1407 OD1 ASN A 430 1555 1555 2.35
LINK CA CA A1407 O TYR A 432 1555 1555 2.12
LINK O2 CAC B1301 MG MG B1401 1555 1555 1.94
LINK MG MG B1401 O HOH B1405 1555 1555 1.92
LINK MG MG B1401 OE1 GLU B 220 1555 1555 2.12
LINK MG MG B1401 O HOH B1404 1555 1555 2.19
LINK MG MG B1401 OG SER B 121 1555 1555 2.17
LINK MG MG B1401 OG SER B 123 1555 1555 2.17
LINK CA CA B1402 OD1 ASP B 127 1555 1555 2.22
LINK CA CA B1402 OD2 ASP B 127 1555 1555 3.33
LINK CA CA B1402 O SER B 123 1555 1555 2.38
LINK CA CA B1402 OD1 ASP B 126 1555 1555 2.70
LINK CA CA B1402 OD2 ASP B 126 1555 1555 3.09
LINK CA CA B1402 OD2 ASP B 251 1555 1555 2.69
LINK CA CA B1402 O HOH B1406 1555 1555 2.29
LINK CA CA B1403 OD2 ASP B 158 1555 1555 1.99
LINK CA CA B1403 OD1 ASN B 215 1555 1555 1.93
LINK CA CA B1403 O ASP B 217 1555 1555 2.20
LINK CA CA B1403 OD1 ASP B 217 1555 1555 2.17
LINK CA CA B1403 OE2 GLU B 220 1555 1555 2.34
LINK CA CA B1403 O PRO B 219 1555 1555 1.99
LINK CA CA C1411 OE1 GLU C 252 1555 1555 3.39
LINK CA CA C1411 OD1 ASP C 245 1555 1555 2.06
LINK CA CA C1411 O ASP C 247 1555 1555 2.14
LINK CA CA C1411 OG1 THR C 250 1555 1555 2.69
LINK CA CA C1411 OE1 GLU C 243 1555 1555 2.73
LINK CA CA C1411 OE2 GLU C 243 1555 1555 2.15
LINK CA CA C1411 O THR C 250 1555 1555 2.45
LINK CA CA C1411 OE2 GLU C 252 1555 1555 2.18
LINK CA CA C1412 OD2 ASP C 305 1555 1555 2.22
LINK CA CA C1412 OD1 ASN C 299 1555 1555 2.22
LINK CA CA C1412 OD2 ASP C 301 1555 1555 3.10
LINK CA CA C1412 OD1 ASP C 301 1555 1555 2.15
LINK CA CA C1412 OD1 ASP C 297 1555 1555 2.35
LINK CA CA C1412 OD1 ASP C 305 1555 1555 2.45
LINK CA CA C1412 O ARG C 303 1555 1555 2.40
LINK CA CA C1413 OD1 ASP C 365 1555 1555 2.32
LINK CA CA C1413 OD1 ASP C 367 1555 1555 2.22
LINK CA CA C1413 OD1 ASP C 369 1555 1555 2.65
LINK CA CA C1413 O TYR C 371 1555 1555 2.08
LINK CA CA C1413 OD2 ASP C 373 1555 1555 2.64
LINK CA CA C1413 OD1 ASP C 373 1555 1555 2.63
LINK CA CA C1414 OD1 ASP C 434 1555 1555 2.68
LINK CA CA C1414 OD2 ASP C 434 1555 1555 2.66
LINK CA CA C1414 O TYR C 432 1555 1555 2.01
LINK CA CA C1414 OD1 ASN C 430 1555 1555 2.28
LINK CA CA C1414 OD1 ASP C 428 1555 1555 2.20
LINK CA CA C1414 OD1 ASP C 426 1555 1555 2.46
LINK O2 CAC D1302 MG MG D1408 1555 1555 1.95
LINK MG MG D1408 OG SER D 123 1555 1555 2.01
LINK MG MG D1408 OG SER D 121 1555 1555 2.25
LINK MG MG D1408 OE1 GLU D 220 1555 1555 2.02
LINK MG MG D1408 O HOH D1412 1555 1555 1.97
LINK MG MG D1408 O HOH D1411 1555 1555 2.03
LINK CA CA D1409 OD1 ASP D 126 1555 1555 2.56
LINK CA CA D1409 OD2 ASP D 126 1555 1555 3.16
LINK CA CA D1409 O SER D 123 1555 1555 2.10
LINK CA CA D1409 OD1 ASP D 127 1555 1555 2.24
LINK CA CA D1409 OD2 ASP D 251 1555 1555 2.69
LINK CA CA D1409 O HOH D1413 1555 1555 2.64
LINK CA CA D1410 OE2 GLU D 220 1555 1555 2.49
LINK CA CA D1410 OD1 ASN D 215 1555 1555 1.98
LINK CA CA D1410 O ASP D 217 1555 1555 2.45
LINK CA CA D1410 O PRO D 219 1555 1555 1.96
LINK CA CA D1410 OD1 ASP D 217 1555 1555 2.37
LINK CA CA D1410 OD2 ASP D 158 1555 1555 2.11
LINK CA CA E1418 OG1 THR E 250 1555 1555 2.46
LINK CA CA E1418 OE1 GLU E 243 1555 1555 2.68
LINK CA CA E1418 O ASP E 247 1555 1555 2.23
LINK CA CA E1418 O THR E 250 1555 1555 2.05
LINK CA CA E1418 OD1 ASP E 245 1555 1555 2.10
LINK CA CA E1418 OE2 GLU E 243 1555 1555 2.34
LINK CA CA E1418 OE2 GLU E 252 1555 1555 2.00
LINK CA CA E1419 OD1 ASN E 299 1555 1555 2.28
LINK CA CA E1419 OD2 ASP E 305 1555 1555 2.10
LINK CA CA E1419 OD1 ASP E 297 1555 1555 2.39
LINK CA CA E1419 OD1 ASP E 305 1555 1555 2.46
LINK CA CA E1419 OD2 ASP E 301 1555 1555 3.10
LINK CA CA E1419 O ARG E 303 1555 1555 2.23
LINK CA CA E1419 OD1 ASP E 301 1555 1555 2.12
LINK CA CA E1420 OD2 ASP E 373 1555 1555 2.61
LINK CA CA E1420 OD1 ASP E 365 1555 1555 2.24
LINK CA CA E1420 O TYR E 371 1555 1555 2.08
LINK CA CA E1420 OD1 ASP E 369 1555 1555 2.46
LINK CA CA E1420 OD1 ASP E 367 1555 1555 2.27
LINK CA CA E1420 OD1 ASP E 373 1555 1555 2.48
LINK CA CA E1421 OD1 ASP E 426 1555 1555 2.54
LINK CA CA E1421 OD1 ASP E 428 1555 1555 2.29
LINK CA CA E1421 OD1 ASN E 430 1555 1555 2.26
LINK CA CA E1421 O TYR E 432 1555 1555 2.26
LINK CA CA E1421 OD1 ASP E 434 1555 1555 2.54
LINK CA CA E1421 OD2 ASP E 434 1555 1555 2.40
LINK O2 CAC F1303 MG MG F1415 1555 1555 2.03
LINK MG MG F1415 O HOH F1419 1555 1555 1.98
LINK MG MG F1415 OE1 GLU F 220 1555 1555 2.02
LINK MG MG F1415 OG SER F 123 1555 1555 2.05
LINK MG MG F1415 OG SER F 121 1555 1555 2.05
LINK MG MG F1415 O HOH F1418 1555 1555 2.11
LINK CA CA F1416 OD1 ASP F 126 1555 1555 2.65
LINK CA CA F1416 O SER F 123 1555 1555 2.23
LINK CA CA F1416 OD1 ASP F 127 1555 1555 2.31
LINK CA CA F1416 OD2 ASP F 251 1555 1555 2.61
LINK CA CA F1416 O HOH F1420 1555 1555 2.51
LINK CA CA F1417 O ASP F 217 1555 1555 2.28
LINK CA CA F1417 OD1 ASP F 217 1555 1555 2.44
LINK CA CA F1417 O PRO F 219 1555 1555 1.99
LINK CA CA F1417 OD2 ASP F 158 1555 1555 2.13
LINK CA CA F1417 OE2 GLU F 220 1555 1555 2.49
LINK CA CA F1417 OD1 ASN F 215 1555 1555 2.00
CISPEP 1 SER B 162 PRO B 163 0 -0.44
CISPEP 2 SER B 168 PRO B 169 0 0.18
CISPEP 3 SER D 162 PRO D 163 0 2.74
CISPEP 4 SER D 168 PRO D 169 0 0.56
CISPEP 5 SER F 162 PRO F 163 0 0.11
CISPEP 6 SER F 168 PRO F 169 0 0.31
SITE 1 AC1 2 ASN B 99 PHE B 100
SITE 1 AC2 4 MET A 285 LEU B 317 ASN B 320 NAG B1003
SITE 1 AC3 3 ARG A 281 NAG B1002 MAN B1004
SITE 1 AC4 2 NAG B1003 BMA B1005
SITE 1 AC5 1 MAN B1004
SITE 1 AC6 4 SER B 369 ASN B 371 SER B 398 GLU B 400
SITE 1 AC7 1 ASN D 99
SITE 1 AC8 5 MET C 285 ASN D 316 LEU D 317 ASN D 320
SITE 2 AC8 5 NAG D1009
SITE 1 AC9 3 ARG C 281 NAG D1008 MAN D1010
SITE 1 BC1 3 NAG D1009 BMA D1011 MAN D1012
SITE 1 BC2 1 MAN D1010
SITE 1 BC3 1 MAN D1010
SITE 1 BC4 3 ASN D 371 SER D 398 GLU D 400
SITE 1 BC5 1 ASN E 15
SITE 1 BC6 3 ASN F 99 PHE F 100 SER F 101
SITE 1 BC7 4 ASN F 316 LEU F 317 ASN F 320 NAG F1017
SITE 1 BC8 3 ARG E 281 NAG F1016 MAN F1018
SITE 1 BC9 2 NAG F1017 BMA F1019
SITE 1 CC1 1 MAN F1018
SITE 1 CC2 3 ASN F 371 SER F 398 GLU F 400
SITE 1 CC3 8 SER B 121 TYR B 122 SER B 123 ARG B 214
SITE 2 CC3 8 ASN B 215 ASP B 217 GLU B 220 MG B1401
SITE 1 CC4 8 SER D 121 TYR D 122 SER D 123 ARG D 214
SITE 2 CC4 8 ASN D 215 ASP D 217 GLU D 220 MG D1408
SITE 1 CC5 8 SER F 121 TYR F 122 SER F 123 ARG F 214
SITE 2 CC5 8 ASN F 215 ASP F 217 GLU F 220 MG F1415
SITE 1 CC6 6 SER B 121 SER B 123 GLU B 220 CAC B1301
SITE 2 CC6 6 HOH B1404 HOH B1405
SITE 1 CC7 5 SER B 123 ASP B 126 ASP B 127 ASP B 251
SITE 2 CC7 5 HOH B1406
SITE 1 CC8 5 ASP B 158 ASN B 215 ASP B 217 PRO B 219
SITE 2 CC8 5 GLU B 220
SITE 1 CC9 5 GLU A 243 ASP A 245 ASP A 247 THR A 250
SITE 2 CC9 5 GLU A 252
SITE 1 DC1 5 ASP A 297 ASN A 299 ASP A 301 ARG A 303
SITE 2 DC1 5 ASP A 305
SITE 1 DC2 5 ASP A 365 ASP A 367 ASP A 369 TYR A 371
SITE 2 DC2 5 ASP A 373
SITE 1 DC3 5 ASP A 426 ASP A 428 ASN A 430 TYR A 432
SITE 2 DC3 5 ASP A 434
SITE 1 DC4 6 SER D 121 SER D 123 GLU D 220 CAC D1302
SITE 2 DC4 6 HOH D1411 HOH D1412
SITE 1 DC5 5 SER D 123 ASP D 126 ASP D 127 ASP D 251
SITE 2 DC5 5 HOH D1413
SITE 1 DC6 5 ASP D 158 ASN D 215 ASP D 217 PRO D 219
SITE 2 DC6 5 GLU D 220
SITE 1 DC7 5 GLU C 243 ASP C 245 ASP C 247 THR C 250
SITE 2 DC7 5 GLU C 252
SITE 1 DC8 5 ASP C 297 ASN C 299 ASP C 301 ARG C 303
SITE 2 DC8 5 ASP C 305
SITE 1 DC9 5 ASP C 365 ASP C 367 ASP C 369 TYR C 371
SITE 2 DC9 5 ASP C 373
SITE 1 EC1 5 ASP C 426 ASP C 428 ASN C 430 TYR C 432
SITE 2 EC1 5 ASP C 434
SITE 1 EC2 6 SER F 121 SER F 123 GLU F 220 CAC F1303
SITE 2 EC2 6 HOH F1418 HOH F1419
SITE 1 EC3 5 SER F 123 ASP F 126 ASP F 127 ASP F 251
SITE 2 EC3 5 HOH F1420
SITE 1 EC4 5 ASP F 158 ASN F 215 ASP F 217 PRO F 219
SITE 2 EC4 5 GLU F 220
SITE 1 EC5 5 GLU E 243 ASP E 245 ASP E 247 THR E 250
SITE 2 EC5 5 GLU E 252
SITE 1 EC6 5 ASP E 297 ASN E 299 ASP E 301 ARG E 303
SITE 2 EC6 5 ASP E 305
SITE 1 EC7 5 ASP E 365 ASP E 367 ASP E 369 TYR E 371
SITE 2 EC7 5 ASP E 373
SITE 1 EC8 5 ASP E 426 ASP E 428 ASN E 430 TYR E 432
SITE 2 EC8 5 ASP E 434
CRYST1 332.093 332.093 88.288 90.00 90.00 120.00 P 62 18
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 0.003011 0.001739 0.000000 0.00000
SCALE2 0.000000 0.003477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011327 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
