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HEADER COMPLEX (HYDROLASE/INHIBITOR) 07-JUN-05 2BUA
TITLE CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE IV (CD26)
TITLE 2 IN COMPLEX WITH A LOW MOLECULAR WEIGHT INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 39-766;
COMPND 6 EC: 3.4.14.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGAN: KIDNEY CORTEX
KEYWDS DPP-IV, DIABETES MELLITUS, DRUG DESIGN, HYDROLASE, SERINE
KEYWDS 2 PROTEASE, AMINOPEPTIDASE, GLYCOPROTEIN, PROTEASE,
KEYWDS 3 SIGNAL-ANCHOR, TRANSMEMBRANE, COMPLEX
KEYWDS 4 (HYDROLASE/INHIBITOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NORDHOFF,S.CEREZO-GALVEZ,A.FEURER,O.HILL,V.G.MATASSA,
AUTHOR 2 G.METZ,C.RUMMEY,M.THIEMANN,P.J.EDWARDS
REVDAT 1 23-JAN-06 2BUA 0
JRNL AUTH S.NORDHOFF,S.CEREZO-GALVEZ,A.FEURER,O.HILL,
JRNL AUTH 2 V.G.MATASSA,G.METZ,C.RUMMEY,M.THIEMANN,P.J.EDWARDS
JRNL TITL THE REVERSED BINDING OF B-PHENETHYLAMINE
JRNL TITL 2 INHIBITORS OF DPP-IV. X-RAY STRUCTURES AND
JRNL TITL 3 PROPERTIES OF NOVEL FRAGMENT AND ELABORATED
JRNL TITL 4 INHIBITORS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 2002
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 10000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 109530
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) : 0.2197
REMARK 3 FREE R VALUE : 0.2557
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2191
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 REFLECTION 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 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 : 23864
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 554
REMARK 3 SOLVENT ATOMS : 826
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) : -0.134
REMARK 3 B22 (A**2) : -0.001
REMARK 3 B33 (A**2) : 0.135
REMARK 3 B12 (A**2) : 0.069
REMARK 3 B13 (A**2) : 0.059
REMARK 3 B23 (A**2) : 0.002
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) : 0.007271
REMARK 3 BOND ANGLES (DEGREES) : 1.33695
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 MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.324626
REMARK 3 BSOL : 31.9216
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 GROUP 2 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 3 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 4 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 4 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 PARAMETER FILE 2 : INH.PAR
REMARK 3 TOPOLOGY FILE 2 : INH.TOP
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BUA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 9-JUN-2005.
REMARK 100 THE EBI ID CODE IS EBI-24384.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.912
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109530
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.56
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.2
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 1.97
REMARK 200 R MERGE (I) : 0.00
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: DIMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN A 150 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 GLU A 206 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 ILE A 236 N - CA - C ANGL. DEV. = -10.4 DEGREES
REMARK 500 PHE A 240 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 PRO A 255 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 LEU A 300 N - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 GLN A 388 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 GLU A 448 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 SER A 458 N - CA - C ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG A 492 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ILE A 529 N - CA - C ANGL. DEV. = -10.8 DEGREES
REMARK 500 TYR A 547 N - CA - C ANGL. DEV. = -10.5 DEGREES
REMARK 500 LEU A 561 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 GLY A 617 N - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 VAL A 656 N - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 VAL A 711 N - CA - C ANGL. DEV. = -10.3 DEGREES
REMARK 500 ILE A 742 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ALA A 743 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASN B 150 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 GLU B 206 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 ILE B 236 N - CA - C ANGL. DEV. = -10.6 DEGREES
REMARK 500 PHE B 240 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 PRO B 255 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 LEU B 300 N - CA - C ANGL. DEV. = -11.4 DEGREES
REMARK 500 GLN B 388 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 GLU B 448 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 SER B 458 N - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG B 492 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 ILE B 529 N - CA - C ANGL. DEV. = -10.5 DEGREES
REMARK 500 TYR B 547 N - CA - C ANGL. DEV. = -12.0 DEGREES
REMARK 500 ALA B 548 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 LEU B 561 N - CA - C ANGL. DEV. = -10.7 DEGREES
REMARK 500 GLY B 617 N - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 VAL B 656 N - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 VAL B 711 N - CA - C ANGL. DEV. = -10.3 DEGREES
REMARK 500 ILE B 742 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 ALA B 743 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASN C 150 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 GLU C 206 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 ILE C 236 N - CA - C ANGL. DEV. = -10.4 DEGREES
REMARK 500 PHE C 240 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 LEU C 300 N - CA - C ANGL. DEV. = -11.6 DEGREES
REMARK 500 GLN C 388 N - CA - C ANGL. DEV. = -10.0 DEGREES
REMARK 500 GLU C 448 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 SER C 458 N - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 ARG C 492 CD - NE - CZ ANGL. DEV. = 10.7 DEGREES
REMARK 500 ILE C 529 N - CA - C ANGL. DEV. = -10.6 DEGREES
REMARK 500 TYR C 547 N - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 ALA C 548 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU C 561 N - CA - C ANGL. DEV. = -10.5 DEGREES
REMARK 500 GLY C 617 N - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500 VAL C 656 N - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 VAL C 711 N - CA - C ANGL. DEV. = -10.5 DEGREES
REMARK 500 ILE C 742 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 ALA C 743 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASN D 150 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 GLU D 206 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 ILE D 236 N - CA - C ANGL. DEV. = -10.2 DEGREES
REMARK 500 PHE D 240 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 PRO D 255 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 LEU D 300 N - CA - C ANGL. DEV. = -11.6 DEGREES
REMARK 500 GLN D 388 N - CA - C ANGL. DEV. = -10.4 DEGREES
REMARK 500 GLU D 448 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 SER D 458 N - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 ARG D 492 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ILE D 529 N - CA - C ANGL. DEV. = -11.0 DEGREES
REMARK 500 TYR D 547 N - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 LEU D 561 N - CA - C ANGL. DEV. = -10.5 DEGREES
REMARK 500 GLY D 617 N - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 VAL D 656 N - CA - C ANGL. DEV. = -11.4 DEGREES
REMARK 500 VAL D 711 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ILE D 742 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 ALA D 743 N - CA - C ANGL. DEV. = 9.1 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 630 -111.08 55.66
REMARK 500 SER B 630 -115.63 60.66
REMARK 500 SER D 630 -112.01 51.64
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 525 C X
REMARK 525 D W
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 SITE_DESCRIPTION: 007 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 SITE_DESCRIPTION: 007 BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 SITE_DESCRIPTION: 007 BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 SITE_DESCRIPTION: 007 BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN D
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ORV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL
REMARK 900 PEPTIDASE IV (CD26)
REMARK 900 RELATED ID: 1ORW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL
REMARK 900 PEPTIDASE IV (CD26)IN COMPLEX WITH A
REMARK 900 PEPTIDOMIMETIC INHIBITOR
REMARK 900 RELATED ID: 2BUC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL
REMARK 900 PEPDIDASE IV (CD26) IN COMPLEX WITH A
REMARK 900 TETRAHYDROISOQUINOLINE INHIBITOR
DBREF 2BUA A 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2BUA B 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2BUA C 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2BUA D 39 766 UNP P22411 DPP4_PIG 39 766
SEQRES 1 A 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 A 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 A 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
SEQRES 7 A 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 A 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 728 ASN ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER
SEQRES 12 A 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 A 728 TYR ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 728 GLN TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 A 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 A 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 A 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 A 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 A 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 A 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP
SEQRES 29 A 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 728 TYR TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS
SEQRES 32 A 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 728 GLN TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 A 728 HIS GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG
SEQRES 46 A 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 728 SER MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR
SEQRES 49 A 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 728 PRO GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL
SEQRES 51 A 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 728 GLN SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 A 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 B 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 B 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
SEQRES 7 B 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 B 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 728 ASN ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER
SEQRES 12 B 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 B 728 TYR ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 728 GLN TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 B 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 B 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 B 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 B 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 B 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 B 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP
SEQRES 29 B 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 728 TYR TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS
SEQRES 32 B 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 728 GLN TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 B 728 HIS GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG
SEQRES 46 B 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 728 SER MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR
SEQRES 49 B 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 728 PRO GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL
SEQRES 51 B 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 728 GLN SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 B 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 C 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 C 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 C 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 C 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 C 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
SEQRES 7 C 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 C 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 C 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 C 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 C 728 ASN ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER
SEQRES 12 C 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 C 728 TYR ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 C 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 C 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 C 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 C 728 GLN TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA
SEQRES 18 C 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 C 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 C 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 C 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 C 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 C 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 C 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 C 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 C 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 C 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 C 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP
SEQRES 29 C 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 C 728 TYR TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY
SEQRES 31 C 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS
SEQRES 32 C 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 C 728 GLN TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 C 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 C 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 C 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 C 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 C 728 HIS GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 C 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU
SEQRES 40 C 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 C 728 PHE ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 C 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 C 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 C 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR
SEQRES 45 C 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG
SEQRES 46 C 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 C 728 SER MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 C 728 GLY ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR
SEQRES 49 C 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 C 728 PRO GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL
SEQRES 51 C 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 C 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 C 728 GLN SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 C 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 C 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 C 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 D 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 D 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 D 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 D 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 D 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
SEQRES 7 D 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 D 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 D 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 D 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 D 728 ASN ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER
SEQRES 12 D 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 D 728 TYR ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 D 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 D 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 D 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 D 728 GLN TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA
SEQRES 18 D 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 D 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 D 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 D 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 D 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 D 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 D 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 D 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 D 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 D 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 D 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP
SEQRES 29 D 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 D 728 TYR TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY
SEQRES 31 D 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS
SEQRES 32 D 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 D 728 GLN TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 D 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 D 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 D 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 D 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 D 728 HIS GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 D 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU
SEQRES 40 D 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 D 728 PHE ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 D 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 D 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 D 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR
SEQRES 45 D 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG
SEQRES 46 D 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 D 728 SER MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 D 728 GLY ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR
SEQRES 49 D 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 D 728 PRO GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL
SEQRES 51 D 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 D 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 D 728 GLN SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 D 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 D 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 D 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
HET NAG A1085 14
HET NDG A1092 14
HET NAG A1229 14
HET NAG A1230 14
HET NAG A1279 14
HET NAG A1321 14
HET NDG A1685 14
HET NDG A1686 14
HET NAG B1085 14
HET NDG B1092 14
HET NAG B1093 14
HET NAG B1229 14
HET NAG B1279 14
HET NAG B1321 14
HET NAG B1685 14
HET NAG B1686 14
HET NAG C1085 14
HET NDG C1092 14
HET NAG C1229 14
HET NAG C1279 14
HET NAG C1321 14
HET NAG C1685 14
HET NDG C1686 14
HET NDG D1085 14
HET NDG D1092 14
HET NAG D1093 14
HET NDG D1229 14
HET NAG D1230 14
HET NAG D1279 14
HET NDG D1321 14
HET NDG D1322 14
HET NAG D1685 14
HET NAG D1686 14
HET 007 A1767 13
HET 007 B1767 13
HET 007 C1767 13
HET 007 D1767 13
HET SO4 A1768 5
HET SO4 B1768 5
HET SO4 C1768 5
HET SO4 D1768 5
HET SO4 A1769 5
HET SO4 B1769 5
HET SO4 C1769 5
HET SO4 D1769 5
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM 007 1-METHYLAMINE-1-BENZYL-CYCLOPENTANE
HETSYN 007 1-(1-PHENYLCYCLOPENTYL)METHANAMINE
FORMUL 5 007 4(C12 H17 N1)
FORMUL 6 SO4 8(O4 S1 2-)
FORMUL 7 NAG 22(C8 H15 N1 O6)
FORMUL 8 NDG 11(C8 H15 N1 O6)
FORMUL 9 HOH *826(H2 O1)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 ASP A 200 GLU A 206 1 7
HELIX 3 3 ARG A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 SER A 340 ALA A 342 5 3
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 463 ALA A 465 5 3
HELIX 8 8 ASN A 497 GLN A 505 1 9
HELIX 9 9 SER A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 MET A 616 1 17
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 LYS A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 ASN A 685 1 7
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 HIS A 712 ALA A 726 1 15
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 THR B 44 LYS B 50 1 7
HELIX 21 21 ASP B 200 GLU B 206 1 7
HELIX 22 22 ARG B 274 LEU B 276 5 3
HELIX 23 23 PRO B 290 ILE B 295 1 6
HELIX 24 24 SER B 340 ALA B 342 5 3
HELIX 25 25 GLU B 421 MET B 425 5 5
HELIX 26 26 ASN B 463 ALA B 465 5 3
HELIX 27 27 ASN B 497 GLN B 505 1 9
HELIX 28 28 SER B 562 THR B 570 1 9
HELIX 29 29 GLY B 587 HIS B 592 1 6
HELIX 30 30 ALA B 593 ASN B 595 5 3
HELIX 31 31 THR B 600 MET B 616 1 17
HELIX 32 32 SER B 630 GLY B 641 1 12
HELIX 33 33 LYS B 658 TYR B 662 5 5
HELIX 34 34 ASP B 663 GLY B 672 1 10
HELIX 35 35 ASN B 679 ASN B 685 1 7
HELIX 36 36 VAL B 688 VAL B 698 5 11
HELIX 37 37 HIS B 712 ALA B 726 1 15
HELIX 38 38 SER B 744 PHE B 763 1 20
HELIX 39 39 THR C 44 LYS C 50 1 7
HELIX 40 40 ASP C 200 GLU C 206 1 7
HELIX 41 41 ARG C 274 LEU C 276 5 3
HELIX 42 42 PRO C 290 ILE C 295 1 6
HELIX 43 43 SER C 340 ALA C 342 5 3
HELIX 44 44 GLU C 421 MET C 425 5 5
HELIX 45 45 ASN C 463 ALA C 465 5 3
HELIX 46 46 ASN C 497 GLN C 505 1 9
HELIX 47 47 SER C 562 THR C 570 1 9
HELIX 48 48 GLY C 587 HIS C 592 1 6
HELIX 49 49 ALA C 593 ASN C 595 5 3
HELIX 50 50 THR C 600 MET C 616 1 17
HELIX 51 51 SER C 630 GLY C 641 1 12
HELIX 52 52 LYS C 658 TYR C 662 5 5
HELIX 53 53 ASP C 663 GLY C 672 1 10
HELIX 54 54 ASN C 679 ASN C 685 1 7
HELIX 55 55 VAL C 688 VAL C 698 5 11
HELIX 56 56 HIS C 712 ALA C 726 1 15
HELIX 57 57 SER C 744 PHE C 763 1 20
HELIX 58 58 THR D 44 LYS D 50 1 7
HELIX 59 59 ASP D 200 GLU D 206 1 7
HELIX 60 60 ARG D 274 LEU D 276 5 3
HELIX 61 61 PRO D 290 ILE D 295 1 6
HELIX 62 62 SER D 340 ALA D 342 5 3
HELIX 63 63 GLU D 421 MET D 425 5 5
HELIX 64 64 ASN D 463 ALA D 465 5 3
HELIX 65 65 ASN D 497 GLN D 505 1 9
HELIX 66 66 SER D 562 THR D 570 1 9
HELIX 67 67 GLY D 587 HIS D 592 1 6
HELIX 68 68 ALA D 593 ASN D 595 5 3
HELIX 69 69 THR D 600 MET D 616 1 17
HELIX 70 70 SER D 630 GLY D 641 1 12
HELIX 71 71 LYS D 658 TYR D 662 5 5
HELIX 72 72 ASP D 663 GLY D 672 1 10
HELIX 73 73 ASN D 679 ASN D 685 1 7
HELIX 74 74 VAL D 688 VAL D 698 5 11
HELIX 75 75 HIS D 712 ALA D 726 1 15
HELIX 76 76 SER D 744 PHE D 763 1 20
SHEET 1 AA 2 ARG A 41 THR A 42 0
SHEET 2 AA 2 VAL A 507 GLN A 508 1 N GLN A 508 O ARG A 41
SHEET 1 AB 4 LEU A 60 TRP A 62 0
SHEET 2 AB 4 GLU A 67 GLN A 72 -1 O LEU A 69 N GLN A 61
SHEET 3 AB 4 ASN A 75 ASN A 80 -1 O ASN A 75 N GLN A 72
SHEET 4 AB 4 SER A 86 LEU A 90 -1 O SER A 87 N LEU A 78
SHEET 1 AC 4 ASP A 104 VAL A 107 0
SHEET 2 AC 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AC 4 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 4 AC 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AD 4 THR A 152 TRP A 157 0
SHEET 2 AD 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 AD 4 ASP A 171 LYS A 175 -1 O ASP A 171 N TRP A 168
SHEET 4 AD 4 GLN A 183 ARG A 184 -1 O GLN A 183 N VAL A 174
SHEET 1 AE 3 ILE A 194 ASN A 196 0
SHEET 2 AE 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AE 3 LEU A 214 TRP A 216 -1 O TRP A 215 N ALA A 224
SHEET 1 AF 4 ILE A 194 ASN A 196 0
SHEET 2 AF 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AF 4 THR A 265 ASP A 272 -1 O THR A 265 N ASN A 229
SHEET 4 AF 4 SER A 284 ILE A 287 -1 O TYR A 285 N VAL A 270
SHEET 1 AG 2 LEU A 235 PHE A 240 0
SHEET 2 AG 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AH 4 HIS A 298 THR A 307 0
SHEET 2 AH 4 ARG A 310 ARG A 317 -1 O ARG A 310 N VAL A 306
SHEET 3 AH 4 TYR A 322 TYR A 330 -1 O TYR A 322 N ARG A 317
SHEET 4 AH 4 GLN A 344 ILE A 348 -1 O HIS A 345 N ILE A 325
SHEET 1 AI 4 HIS A 298 THR A 307 0
SHEET 2 AI 4 ARG A 310 ARG A 317 -1 O ARG A 310 N VAL A 306
SHEET 3 AI 4 TYR A 322 TYR A 330 -1 O TYR A 322 N ARG A 317
SHEET 4 AI 4 TRP A 337 ILE A 338 -1 O ILE A 338 N ASP A 329
SHEET 1 AJ 4 HIS A 363 PHE A 364 0
SHEET 2 AJ 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AJ 4 LYS A 382 GLN A 388 -1 O HIS A 383 N ILE A 375
SHEET 4 AJ 4 CYS A 394 PHE A 396 -1 O THR A 395 N HIS A 386
SHEET 1 AK 4 VAL A 404 LEU A 410 0
SHEET 2 AK 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 AK 4 ASN A 430 GLN A 435 -1 O ASN A 430 N SER A 419
SHEET 4 AK 4 VAL A 442 CYS A 444 -1 O THR A 443 N ARG A 433
SHEET 1 AL 4 TYR A 457 PHE A 461 0
SHEET 2 AL 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 AL 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AL 4 GLU A 490 GLU A 495 -1 O ARG A 492 N LEU A 482
SHEET 1 AM 8 SER A 511 LEU A 519 0
SHEET 2 AM 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 AM 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AM 8 TYR A 540 VAL A 546 1 O PRO A 541 N ILE A 574
SHEET 5 AM 8 VAL A 619 TRP A 629 1 N ASP A 620 O TYR A 540
SHEET 6 AM 8 CYS A 649 VAL A 653 1 O CYS A 649 N ILE A 626
SHEET 7 AM 8 GLU A 699 GLY A 705 1 O GLU A 699 N GLY A 650
SHEET 8 AM 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 BA 2 ARG B 41 THR B 42 0
SHEET 2 BA 2 VAL B 507 GLN B 508 1 N GLN B 508 O ARG B 41
SHEET 1 BB 4 LEU B 60 TRP B 62 0
SHEET 2 BB 4 GLU B 67 GLN B 72 -1 O LEU B 69 N GLN B 61
SHEET 3 BB 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 BB 4 SER B 86 LEU B 90 -1 O SER B 87 N LEU B 78
SHEET 1 BC 4 ASP B 104 VAL B 107 0
SHEET 2 BC 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 BC 4 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 4 BC 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 BD 4 THR B 152 TRP B 157 0
SHEET 2 BD 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 BD 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 BD 4 GLN B 183 ARG B 184 -1 O GLN B 183 N VAL B 174
SHEET 1 BE 3 ILE B 194 ASN B 196 0
SHEET 2 BE 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BE 3 LEU B 214 TRP B 216 -1 O TRP B 215 N ALA B 224
SHEET 1 BF 4 ILE B 194 ASN B 196 0
SHEET 2 BF 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BF 4 THR B 265 ASP B 272 -1 O THR B 265 N ASN B 229
SHEET 4 BF 4 SER B 284 ILE B 287 -1 O TYR B 285 N VAL B 270
SHEET 1 BG 2 LEU B 235 PHE B 240 0
SHEET 2 BG 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 BH 7 HIS B 298 THR B 307 0
SHEET 2 BH 7 ARG B 310 ARG B 317 -1 O ARG B 310 N VAL B 306
SHEET 3 BH 7 TYR B 322 TYR B 330 -1 O TYR B 322 N ARG B 317
SHEET 4 BH 7 TRP B 337 ILE B 338 -1 O ILE B 338 N ASP B 329
SHEET 5 BH 7 TYR B 322 TYR B 330 -1 O ASP B 329 N ILE B 338
SHEET 6 BH 7 GLN B 344 ILE B 348 -1 O HIS B 345 N ILE B 325
SHEET 7 BH 7 TYR B 322 TYR B 330 -1 O SER B 323 N GLU B 347
SHEET 1 BI 4 HIS B 363 PHE B 364 0
SHEET 2 BI 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 BI 4 LYS B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 BI 4 CYS B 394 PHE B 396 -1 O THR B 395 N HIS B 386
SHEET 1 BJ 4 VAL B 404 LEU B 410 0
SHEET 2 BJ 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 BJ 4 ASN B 430 GLN B 435 -1 O ASN B 430 N SER B 419
SHEET 4 BJ 4 VAL B 442 CYS B 444 -1 O THR B 443 N ARG B 433
SHEET 1 BK 4 TYR B 457 PHE B 461 0
SHEET 2 BK 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 BK 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 BK 4 GLU B 490 GLU B 495 -1 O ARG B 492 N LEU B 482
SHEET 1 BL 8 SER B 511 LEU B 519 0
SHEET 2 BL 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 BL 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 BL 8 TYR B 540 VAL B 546 1 O PRO B 541 N ILE B 574
SHEET 5 BL 8 VAL B 619 TRP B 629 1 N ASP B 620 O TYR B 540
SHEET 6 BL 8 CYS B 649 VAL B 653 1 O CYS B 649 N ILE B 626
SHEET 7 BL 8 GLU B 699 GLY B 705 1 O GLU B 699 N GLY B 650
SHEET 8 BL 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
SHEET 1 CA 2 ARG C 41 THR C 42 0
SHEET 2 CA 2 VAL C 507 GLN C 508 1 N GLN C 508 O ARG C 41
SHEET 1 CB 4 LEU C 60 TRP C 62 0
SHEET 2 CB 4 GLU C 67 GLN C 72 -1 O LEU C 69 N GLN C 61
SHEET 3 CB 4 ASN C 75 ASN C 80 -1 O ASN C 75 N GLN C 72
SHEET 4 CB 4 SER C 86 LEU C 90 -1 O SER C 87 N LEU C 78
SHEET 1 CC 4 ASP C 104 VAL C 107 0
SHEET 2 CC 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 CC 4 TYR C 128 ASP C 136 -1 O THR C 129 N VAL C 121
SHEET 4 CC 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 CD 4 THR C 152 TRP C 157 0
SHEET 2 CD 4 LEU C 164 TRP C 168 -1 O ALA C 165 N THR C 156
SHEET 3 CD 4 ASP C 171 LYS C 175 -1 O ASP C 171 N TRP C 168
SHEET 4 CD 4 GLN C 183 ARG C 184 -1 O GLN C 183 N VAL C 174
SHEET 1 CE 7 ILE C 194 ASN C 196 0
SHEET 2 CE 7 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 CE 7 LEU C 214 TRP C 216 -1 O TRP C 215 N ALA C 224
SHEET 4 CE 7 PHE C 222 ASN C 229 -1 O ALA C 224 N TRP C 215
SHEET 5 CE 7 SER C 284 ILE C 287
SHEET 6 CE 7 THR C 265 ASP C 272 -1 O PHE C 268 N ILE C 287
SHEET 7 CE 7 PHE C 222 ASN C 229 -1 O LEU C 223 N VAL C 271
SHEET 1 CF 2 LEU C 235 PHE C 240 0
SHEET 2 CF 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 CG 7 HIS C 298 THR C 307 0
SHEET 2 CG 7 ARG C 310 ARG C 317 -1 O ARG C 310 N VAL C 306
SHEET 3 CG 7 TYR C 322 TYR C 330 -1 O TYR C 322 N ARG C 317
SHEET 4 CG 7 TRP C 337 ILE C 338 -1 O ILE C 338 N ASP C 329
SHEET 5 CG 7 TYR C 322 TYR C 330 -1 O ASP C 329 N ILE C 338
SHEET 6 CG 7 GLN C 344 ILE C 348 -1 O HIS C 345 N ILE C 325
SHEET 7 CG 7 TYR C 322 TYR C 330 -1 O SER C 323 N GLU C 347
SHEET 1 CH 4 HIS C 363 PHE C 364 0
SHEET 2 CH 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 CH 4 LYS C 382 GLN C 388 -1 O HIS C 383 N ILE C 375
SHEET 4 CH 4 CYS C 394 PHE C 396 -1 O THR C 395 N HIS C 386
SHEET 1 CI 4 VAL C 404 LEU C 410 0
SHEET 2 CI 4 TYR C 414 SER C 419 -1 O TYR C 416 N GLU C 408
SHEET 3 CI 4 ASN C 430 GLN C 435 -1 O ASN C 430 N SER C 419
SHEET 4 CI 4 VAL C 442 CYS C 444 -1 O THR C 443 N ARG C 433
SHEET 1 CJ 4 TYR C 457 PHE C 461 0
SHEET 2 CJ 4 TYR C 467 CYS C 472 -1 O GLN C 469 N SER C 460
SHEET 3 CJ 4 LEU C 479 SER C 484 -1 O LEU C 479 N CYS C 472
SHEET 4 CJ 4 GLU C 490 GLU C 495 -1 O ARG C 492 N LEU C 482
SHEET 1 CK 8 SER C 511 LEU C 519 0
SHEET 2 CK 8 THR C 522 LEU C 530 -1 O THR C 522 N LEU C 519
SHEET 3 CK 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 CK 8 TYR C 540 VAL C 546 1 O PRO C 541 N ILE C 574
SHEET 5 CK 8 VAL C 619 TRP C 629 1 N ASP C 620 O TYR C 540
SHEET 6 CK 8 CYS C 649 VAL C 653 1 O CYS C 649 N ILE C 626
SHEET 7 CK 8 GLU C 699 GLY C 705 1 O GLU C 699 N GLY C 650
SHEET 8 CK 8 GLN C 731 TYR C 735 1 O GLN C 731 N LEU C 702
SHEET 1 DA 2 ARG D 41 THR D 42 0
SHEET 2 DA 2 VAL D 507 GLN D 508 1 N GLN D 508 O ARG D 41
SHEET 1 DB 4 LEU D 60 TRP D 62 0
SHEET 2 DB 4 GLU D 67 GLN D 72 -1 O LEU D 69 N GLN D 61
SHEET 3 DB 4 ASN D 75 ASN D 80 -1 O ASN D 75 N GLN D 72
SHEET 4 DB 4 SER D 86 LEU D 90 -1 O SER D 87 N LEU D 78
SHEET 1 DC 4 ASP D 104 VAL D 107 0
SHEET 2 DC 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 DC 4 TYR D 128 ASP D 136 -1 O THR D 129 N VAL D 121
SHEET 4 DC 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 DD 4 TRP D 154 TRP D 157 0
SHEET 2 DD 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
SHEET 3 DD 4 ASP D 171 LYS D 175 -1 O ASP D 171 N TRP D 168
SHEET 4 DD 4 GLN D 183 ARG D 184 -1 O GLN D 183 N VAL D 174
SHEET 1 DE 7 ILE D 194 ASN D 196 0
SHEET 2 DE 7 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 DE 7 LEU D 214 TRP D 216 -1 O TRP D 215 N ALA D 224
SHEET 4 DE 7 PHE D 222 ASN D 229 -1 O ALA D 224 N TRP D 215
SHEET 5 DE 7 SER D 284 ILE D 287
SHEET 6 DE 7 THR D 265 ASP D 272 -1 O PHE D 268 N ILE D 287
SHEET 7 DE 7 PHE D 222 ASN D 229 -1 O LEU D 223 N VAL D 271
SHEET 1 DF 2 LEU D 235 PHE D 240 0
SHEET 2 DF 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 DG 7 HIS D 298 THR D 307 0
SHEET 2 DG 7 ARG D 310 ARG D 317 -1 O ARG D 310 N VAL D 306
SHEET 3 DG 7 TYR D 322 TYR D 330 -1 O TYR D 322 N ARG D 317
SHEET 4 DG 7 TRP D 337 ILE D 338 -1 O ILE D 338 N ASP D 329
SHEET 5 DG 7 TYR D 322 TYR D 330 -1 O ASP D 329 N ILE D 338
SHEET 6 DG 7 GLN D 344 ILE D 348 -1 O HIS D 345 N ILE D 325
SHEET 7 DG 7 TYR D 322 TYR D 330 -1 O SER D 323 N GLU D 347
SHEET 1 DH 4 HIS D 363 PHE D 364 0
SHEET 2 DH 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 DH 4 LYS D 382 GLN D 388 -1 O HIS D 383 N ILE D 375
SHEET 4 DH 4 CYS D 394 PHE D 396 -1 O THR D 395 N HIS D 386
SHEET 1 DI 4 VAL D 404 LEU D 410 0
SHEET 2 DI 4 TYR D 414 SER D 419 -1 O TYR D 416 N GLU D 408
SHEET 3 DI 4 ASN D 430 GLN D 435 -1 O ASN D 430 N SER D 419
SHEET 4 DI 4 VAL D 442 CYS D 444 -1 O THR D 443 N ARG D 433
SHEET 1 DJ 4 TYR D 457 PHE D 461 0
SHEET 2 DJ 4 TYR D 467 CYS D 472 -1 O GLN D 469 N SER D 460
SHEET 3 DJ 4 LEU D 479 SER D 484 -1 O LEU D 479 N CYS D 472
SHEET 4 DJ 4 GLU D 490 GLU D 495 -1 O ARG D 492 N LEU D 482
SHEET 1 DK 8 SER D 511 LEU D 519 0
SHEET 2 DK 8 THR D 522 LEU D 530 -1 O THR D 522 N LEU D 519
SHEET 3 DK 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 DK 8 TYR D 540 VAL D 546 1 O PRO D 541 N ILE D 574
SHEET 5 DK 8 VAL D 619 TRP D 629 1 N ASP D 620 O TYR D 540
SHEET 6 DK 8 CYS D 649 VAL D 653 1 O CYS D 649 N ILE D 626
SHEET 7 DK 8 GLU D 699 GLY D 705 1 O GLU D 699 N GLY D 650
SHEET 8 DK 8 GLN D 731 TYR D 735 1 O GLN D 731 N LEU D 702
SSBOND 1 CYS A 385 CYS A 394 1555 1555
SSBOND 2 CYS A 444 CYS A 447 1555 1555
SSBOND 3 CYS A 454 CYS A 472 1555 1555
SSBOND 4 CYS A 649 CYS A 762 1555 1555
SSBOND 5 CYS B 385 CYS B 394 1555 1555
SSBOND 6 CYS B 444 CYS B 447 1555 1555
SSBOND 7 CYS B 454 CYS B 472 1555 1555
SSBOND 8 CYS B 649 CYS B 762 1555 1555
SSBOND 9 CYS C 385 CYS C 394 1555 1555
SSBOND 10 CYS C 444 CYS C 447 1555 1555
SSBOND 11 CYS C 454 CYS C 472 1555 1555
SSBOND 12 CYS C 649 CYS C 762 1555 1555
SSBOND 13 CYS D 385 CYS D 394 1555 1555
SSBOND 14 CYS D 444 CYS D 447 1555 1555
SSBOND 15 CYS D 454 CYS D 472 1555 1555
SSBOND 16 CYS D 649 CYS D 762 1555 1555
LINK ND2 ASN A 85 C1 NAG A1085 1555 1555
LINK ND2 ASN A 92 C1 NDG A1092 1555 1555
LINK ND2 ASN A 229 C1 NAG A1229 1555 1555
LINK ND2 ASN A 279 C1 NAG A1279 1555 1555
LINK ND2 ASN A 321 C1 NAG A1321 1555 1555
LINK ND2 ASN A 685 C1 NDG A1685 1555 1555
LINK O4 NAG A1229 C1 NAG A1230 1555 1555
LINK O4 NDG A1685 C1 NDG A1686 1555 1555
LINK ND2 ASN B 85 C1 NAG B1085 1555 1555
LINK ND2 ASN B 92 C1 NDG B1092 1555 1555
LINK ND2 ASN B 229 C1 NAG B1229 1555 1555
LINK ND2 ASN B 279 C1 NAG B1279 1555 1555
LINK ND2 ASN B 321 C1 NAG B1321 1555 1555
LINK ND2 ASN B 685 C1 NAG B1685 1555 1555
LINK O4 NDG B1092 C1 NAG B1093 1555 1555
LINK O4 NAG B1685 C1 NAG B1686 1555 1555
LINK ND2 ASN C 85 C1 NAG C1085 1555 1555
LINK ND2 ASN C 92 C1 NDG C1092 1555 1555
LINK ND2 ASN C 229 C1 NAG C1229 1555 1555
LINK ND2 ASN C 279 C1 NAG C1279 1555 1555
LINK ND2 ASN C 321 C1 NAG C1321 1555 1555
LINK ND2 ASN C 685 C1 NAG C1685 1555 1555
LINK O4 NAG C1685 C1 NDG C1686 1555 1555
LINK ND2 ASN D 85 C1 NDG D1085 1555 1555
LINK ND2 ASN D 92 C1 NDG D1092 1555 1555
LINK ND2 ASN D 229 C1 NDG D1229 1555 1555
LINK ND2 ASN D 279 C1 NAG D1279 1555 1555
LINK ND2 ASN D 321 C1 NDG D1321 1555 1555
LINK ND2 ASN D 685 C1 NAG D1685 1555 1555
LINK O4 NDG D1092 C1 NAG D1093 1555 1555
LINK O4 NDG D1229 C1 NAG D1230 1555 1555
LINK O4 NDG D1321 C1 NDG D1322 1555 1555
LINK O4 NAG D1685 C1 NAG D1686 1555 1555
CISPEP 1 GLY A 474 PRO A 475 0 -0.19
CISPEP 2 GLY B 474 PRO B 475 0 -0.14
CISPEP 3 GLY C 474 PRO C 475 0 -0.55
CISPEP 4 GLY D 474 PRO D 475 0 -0.05
SITE 1 AC1 4 ASN A 80 ASN A 85 SER A 86 SER A 87
SITE 1 AC2 4 GLU A 73 ASN A 75 ASN A 92 GLY A 521
SITE 1 AC3 4 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 1 AC5 3 ASN A 279 TYR C 285 HOH X 72
SITE 1 AC6 4 THR A 144 ASN A 321 SER A 349 ASP A 678
SITE 1 AC7 6 GLY A 599 THR A 600 ASN A 685 SER A 686
SITE 2 AC7 6 ARG A 691 HOH Z 185
SITE 1 AC8 4 GLY A 99 TYR A 100 ARG A 597 TYR A 682
SITE 1 AC9 4 TYR B 83 ASN B 85 SER B 86 SER B 87
SITE 1 BC1 4 GLU B 73 ASN B 75 ASN B 92 ILE B 348
SITE 1 BC2 2 GLU B 73 THR B 350
SITE 1 BC3 4 ASN B 229 THR B 231 HOH Y 247 HOH Y 248
SITE 1 BC4 2 ASN B 279 TYR D 285
SITE 1 BC5 7 ASN B 321 ILE B 348 SER B 349 THR B 350
SITE 2 BC5 7 HOH Y 249 HOH Y 250 HOH Y 251
SITE 1 BC6 7 ARG B 597 GLY B 599 THR B 600 ASN B 685
SITE 2 BC6 7 SER B 686 ARG B 691 HOH Y 252
SITE 1 BC7 2 ARG B 597 TYR B 682
SITE 1 BC8 4 MET B 616 LEU C 78 ASN C 85 SER C 87
SITE 1 BC9 4 GLU C 73 ASN C 74 ASN C 75 ASN C 92
SITE 1 CC1 6 ILE C 194 ASN C 229 THR C 231 GLU C 232
SITE 2 CC1 6 LYS C 267 HOH X 66
SITE 1 CC2 1 ASN C 279
SITE 1 CC3 4 ASN C 321 SER C 349 ASP C 678 HOH X 206
SITE 1 CC4 6 THR C 600 ASN C 685 SER C 686 ARG C 691
SITE 2 CC4 6 HOH X 174 HOH X 207
SITE 1 CC5 3 ARG C 597 TYR C 682 HOH X 207
SITE 1 CC6 2 ASN D 85 SER D 87
SITE 1 CC7 4 GLU D 73 ASN D 75 ASN D 92 ILE D 348
SITE 1 CC8 1 GLU D 73
SITE 1 CC9 5 GLN D 227 ASN D 229 THR D 231 GLU D 232
SITE 2 CC9 5 LYS D 267
SITE 1 DC1 1 GLU D 232
SITE 1 DC3 4 ALA D 319 ASN D 321 SER D 349 THR D 350
SITE 1 DC4 2 ARG D 596 ASP D 678
SITE 1 DC5 7 ARG D 597 THR D 600 MET D 638 ASN D 685
SITE 2 DC5 7 SER D 686 ARG D 691 HOH W 144
SITE 1 DC6 3 ARG D 597 GLU D 604 TYR D 682
SITE 1 DC7 7 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 DC7 7 SER A 630 TYR A 662 TYR A 666
SITE 1 DC8 7 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 DC8 7 SER B 630 TYR B 662 TYR B 666
SITE 1 DC9 7 ARG C 125 GLU C 205 GLU C 206 TYR C 547
SITE 2 DC9 7 SER C 630 TYR C 662 TYR C 666
SITE 1 FC1 6 GLU D 205 GLU D 206 TYR D 547 SER D 630
SITE 2 FC1 6 TYR D 662 TYR D 666
SITE 1 FC2 6 ALA A 360 GLU A 361 HIS A 363 GLY A 406
SITE 2 FC2 6 ILE A 407 HOH Z 186
SITE 1 FC3 7 ALA B 360 GLU B 361 HIS B 363 GLY B 406
SITE 2 FC3 7 ILE B 407 HOH Y 253 HOH Y 254
SITE 1 FC4 5 ALA C 360 GLU C 361 HIS C 363 ILE C 407
SITE 2 FC4 5 HOH X 208
SITE 1 FC5 7 GLU D 361 HIS D 363 ILE D 374 GLY D 406
SITE 2 FC5 7 ILE D 407 HOH W 176 HOH W 177
SITE 1 FC6 3 ARG A 125 SER A 630 HIS A 740
SITE 1 FC7 4 ARG B 125 TRP B 629 SER B 630 HIS B 740
SITE 1 FC8 4 ARG C 125 TRP C 629 SER C 630 HIS C 740
SITE 1 FC9 4 ARG D 125 TRP D 629 SER D 630 HIS D 740
CRYST1 62.425 118.131 133.317 112.40 94.98 90.99 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016019 0.000277 0.001627 0.00000
SCALE2 0.000000 0.008466 0.003522 0.00000
SCALE3 0.000000 0.000000 0.008155 0.00000
TER 5967 PRO A 766
TER 11934 PRO B 766
TER 17901 PRO C 766
TER 23868 PRO D 766
MASTER 477 0 45 76 201 0 58 625244 4 610 224
END |