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HEADER COMPLEX (HYDROLASE/INHIBITOR) 09-JUN-05 2BUC
TITLE CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPDIDASE IV (CD26)
TITLE 2 IN COMPLEX WITH A TETRAHYDROISOQUINOLINE 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
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 2BUC 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. 2.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.00
REMARK 3 NUMBER OF REFLECTIONS : 113230
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.22208
REMARK 3 R VALUE (WORKING SET) : 0.22094
REMARK 3 FREE R VALUE : 0.27872
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2311
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.564
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8268
REMARK 3 BIN R VALUE (WORKING SET) : 0.300
REMARK 3 BIN FREE R VALUE SET COUNT : 168
REMARK 3 BIN FREE R VALUE : 0.324
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 : 606
REMARK 3 SOLVENT ATOMS : 951
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.498
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.68
REMARK 3 B22 (A**2) : -0.39
REMARK 3 B33 (A**2) : 0.08
REMARK 3 B12 (A**2) : 0.45
REMARK 3 B13 (A**2) : -0.98
REMARK 3 B23 (A**2) : 0.67
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.825
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.332
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.268
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.168
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 25219 ; 0.005 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 34354 ; 0.908 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2908 ; 4.985 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3657 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 19360 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 12049 ; 0.162 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 1455 ; 0.105 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 127 ; 0.147 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 7 ; 0.117 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 14512 ; 0.269 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 23548 ; 0.500 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 10707 ; 0.483 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 10806 ; 0.864 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 39 A 540 5
REMARK 3 1 B 39 B 540 5
REMARK 3 1 C 39 C 540 5
REMARK 3 1 D 39 D 540 5
REMARK 3 2 A 555 A 620 5
REMARK 3 2 B 555 B 620 5
REMARK 3 2 C 555 C 620 5
REMARK 3 2 D 555 D 620 5
REMARK 3 3 A 640 A 766 5
REMARK 3 3 B 640 B 766 5
REMARK 3 3 C 640 C 766 5
REMARK 3 3 D 640 D 766 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3290 ; 0.18 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 3290 ; 0.15 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 3290 ; 0.18 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 3290 ; 0.16 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 2417 ; 0.45 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 2417 ; 0.41 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 2417 ; 0.47 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 2417 ; 0.41 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3290 ; 0.14 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 3290 ; 0.15 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 3290 ; 0.15 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 3290 ; 0.15 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 2417 ; 0.45 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 2417 ; 0.46 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 2417 ; 0.51 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 2417 ; 0.48 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS :1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2BUC COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 10-JUN-2005.
REMARK 100 THE EBI ID CODE IS EBI-24440.
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) : 0.97954
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 : 115542
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 19.28
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 1.98
REMARK 200 R MERGE (I) : 0.20
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 LEU A 415 CA - CB - CG ANGL. DEV. = 9.4 DEGREES
REMARK 500 LEU A 542 CA - CB - CG ANGL. DEV. = 6.7 DEGREES
REMARK 500 VAL A 711 N - CA - C ANGL. DEV. = -6.6 DEGREES
REMARK 500 LEU B 415 CA - CB - CG ANGL. DEV. = 12.3 DEGREES
REMARK 500 LEU B 542 CA - CB - CG ANGL. DEV. = 6.5 DEGREES
REMARK 500 LEU C 542 CA - CB - CG ANGL. DEV. = 6.5 DEGREES
REMARK 500 VAL C 711 N - CA - C ANGL. DEV. = -6.9 DEGREES
REMARK 500 LEU D 415 CA - CB - CG ANGL. DEV. = 11.1 DEGREES
REMARK 500 VAL D 711 N - CA - C ANGL. DEV. = -6.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 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 ARG A 40 131.22 68.00
REMARK 500 SER A 630 -113.91 57.88
REMARK 500 ARG B 40 125.12 72.43
REMARK 500 SER B 630 -104.36 52.04
REMARK 500 ARG C 40 130.52 75.83
REMARK 500 SER C 630 -114.02 55.26
REMARK 500 ARG D 40 122.30 69.03
REMARK 500 SER D 630 -111.56 56.69
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: 008 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: 008 BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: 008 BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: 008 BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
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: 2BUA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL
REMARK 900 PEPTIDASE IV (CD26) IN COMPLEX WITH A LOW
REMARK 900 MOLECULAR WEIGHT INHIBITOR.
DBREF 2BUC A 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2BUC B 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2BUC C 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2BUC 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 NAG 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 NAG 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 NAG D1092 14
HET NAG D1093 14
HET NDG D1229 14
HET NDG D1230 14
HET NDG D1279 14
HET NAG D1321 14
HET NDG D1322 14
HET NAG D1685 14
HET NAG D1686 14
HET 008 A1767 26
HET 008 B1767 26
HET 008 C1767 26
HET 008 D1767 26
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 008 (S)-2-[(R)-3-AMINO-4-(2-FLUORO-PHENYL)-
HETNAM 2 008 BUTYRYL]-1,2,3,4-TETRAHYDRO-ISOQUINOLINE-3-
HETNAM 3 008 CARBOXYLIC ACID AMIDE
FORMUL 5 008 4(C20 H22 N3 O2 F1)
FORMUL 6 SO4 8(O4 S1 2-)
FORMUL 7 NAG 24(C8 H15 N1 O6)
FORMUL 8 NDG 9(C8 H15 N1 O6)
FORMUL 10 HOH *951(H2 O1)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 ASN A 92 GLU A 97 1 6
HELIX 3 3 ASP A 200 GLU A 206 1 7
HELIX 4 4 ARG A 274 LEU A 276 5 3
HELIX 5 5 PRO A 290 ILE A 295 1 6
HELIX 6 6 SER A 340 ALA A 342 5 3
HELIX 7 7 GLU A 421 MET A 425 5 5
HELIX 8 8 ASN A 497 ASP A 506 1 10
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 THR A 687 VAL A 698 5 12
HELIX 18 18 HIS A 712 GLY A 727 1 16
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 ASN B 92 GLU B 97 1 6
HELIX 22 22 ASP B 200 VAL B 207 1 8
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 497 GLN B 505 1 9
HELIX 27 27 SER B 562 THR B 570 1 9
HELIX 28 28 GLY B 587 HIS B 592 1 6
HELIX 29 29 ALA B 593 ASN B 595 5 3
HELIX 30 30 THR B 600 MET B 616 1 17
HELIX 31 31 SER B 630 GLY B 641 1 12
HELIX 32 32 LYS B 658 TYR B 662 5 5
HELIX 33 33 ASP B 663 GLY B 672 1 10
HELIX 34 34 ASN B 679 ASN B 685 1 7
HELIX 35 35 VAL B 688 GLN B 697 5 10
HELIX 36 36 HIS B 712 GLY B 727 1 16
HELIX 37 37 SER B 744 PHE B 763 1 20
HELIX 38 38 THR C 44 LYS C 50 1 7
HELIX 39 39 ASN C 92 GLU C 97 1 6
HELIX 40 40 ASP C 200 VAL C 207 1 8
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 497 GLN C 505 1 9
HELIX 46 46 SER C 562 THR C 570 1 9
HELIX 47 47 GLY C 587 HIS C 592 1 6
HELIX 48 48 ALA C 593 ASN C 595 5 3
HELIX 49 49 THR C 600 MET C 616 1 17
HELIX 50 50 SER C 630 GLY C 641 1 12
HELIX 51 51 ASP C 663 GLY C 672 1 10
HELIX 52 52 ASN C 679 ASN C 685 1 7
HELIX 53 53 VAL C 688 VAL C 698 5 11
HELIX 54 54 HIS C 712 GLY C 727 1 16
HELIX 55 55 SER C 744 PHE C 763 1 20
HELIX 56 56 THR D 44 LYS D 50 1 7
HELIX 57 57 ASN D 92 GLU D 97 1 6
HELIX 58 58 ASP D 200 VAL D 207 1 8
HELIX 59 59 ARG D 274 LEU D 276 5 3
HELIX 60 60 PRO D 290 ILE D 295 1 6
HELIX 61 61 SER D 340 ALA D 342 5 3
HELIX 62 62 GLU D 421 MET D 425 5 5
HELIX 63 63 ASN D 497 GLN D 505 1 9
HELIX 64 64 SER D 562 THR D 570 1 9
HELIX 65 65 GLY D 587 HIS D 592 1 6
HELIX 66 66 ALA D 593 ASN D 595 5 3
HELIX 67 67 THR D 600 LYS D 615 1 16
HELIX 68 68 SER D 630 GLY D 641 1 12
HELIX 69 69 ASP D 663 GLY D 672 1 10
HELIX 70 70 ASN D 679 ASN D 685 1 7
HELIX 71 71 VAL D 688 GLN D 697 5 10
HELIX 72 72 PHE D 713 ALA D 726 1 14
HELIX 73 73 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 ILE A 148 THR A 152 -1 O ILE A 148 N TYR A 132
SHEET 1 AD 4 TRP A 154 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 THR A 395 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 CYS A 454 PHE A 461 0
SHEET 2 AL 4 TYR A 467 PRO A 475 -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 N LEU A 491 O 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 ILE B 148 THR B 152 -1 O ILE B 148 N TYR B 132
SHEET 1 BD 4 ASP B 104 VAL B 107 0
SHEET 2 BD 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 BD 4 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 4 BD 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 BE 4 TRP B 154 TRP B 157 0
SHEET 2 BE 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 BE 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 BE 4 GLN B 183 ARG B 184 -1 O GLN B 183 N VAL B 174
SHEET 1 BF 7 ILE B 194 ASN B 196 0
SHEET 2 BF 7 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BF 7 LEU B 214 TRP B 216 -1 O TRP B 215 N ALA B 224
SHEET 4 BF 7 PHE B 222 ASN B 229 -1 O ALA B 224 N TRP B 215
SHEET 5 BF 7 SER B 284 ILE B 287
SHEET 6 BF 7 THR B 265 ASP B 272 -1 O PHE B 268 N ILE B 287
SHEET 7 BF 7 PHE B 222 ASN B 229 -1 O LEU B 223 N VAL B 271
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 N LEU B 491 O 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 TRP C 154 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 THR C 283 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 N LEU C 491 O 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 THR D 152 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 THR D 283 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 N LEU D 491 O 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 NAG 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 NAG 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 NAG 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 NAG D1092 1555 1555
LINK ND2 ASN D 229 C1 NDG D1229 1555 1555
LINK ND2 ASN D 279 C1 NDG D1279 1555 1555
LINK ND2 ASN D 321 C1 NAG D1321 1555 1555
LINK ND2 ASN D 685 C1 NAG D1685 1555 1555
LINK O4 NAG D1092 C1 NAG D1093 1555 1555
LINK O4 NDG D1229 C1 NDG D1230 1555 1555
LINK O4 NAG D1321 C1 NDG D1322 1555 1555
LINK O4 NAG D1685 C1 NAG D1686 1555 1555
CISPEP 1 GLY A 474 PRO A 475 0 4.63
CISPEP 2 GLY B 474 PRO B 475 0 4.90
CISPEP 3 GLY C 474 PRO C 475 0 2.10
CISPEP 4 GLY D 474 PRO D 475 0 4.39
SITE 1 AC1 13 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 AC1 13 PHE A 357 TYR A 547 SER A 630 TYR A 662
SITE 3 AC1 13 TYR A 666 ASN A 710 HIS A 740 HOH Z 163
SITE 4 AC1 13 HOH Z 243
SITE 1 AC2 12 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 AC2 12 PHE B 357 ARG B 358 TYR B 547 TYR B 662
SITE 3 AC2 12 TYR B 666 ASN B 710 HIS B 740 HOH Y 187
SITE 1 AC3 11 ARG C 125 GLU C 205 GLU C 206 SER C 209
SITE 2 AC3 11 PHE C 357 TYR C 662 TYR C 666 ASN C 710
SITE 3 AC3 11 HIS C 740 HOH X 160 HOH X 227
SITE 1 AC4 10 ARG D 125 GLU D 205 GLU D 206 SER D 209
SITE 2 AC4 10 PHE D 357 TYR D 547 TYR D 662 TYR D 666
SITE 3 AC4 10 ASN D 710 HIS D 740
SITE 1 AC5 7 ALA A 360 GLU A 361 HIS A 363 ILE A 374
SITE 2 AC5 7 GLY A 406 ILE A 407 HOH Z 123
SITE 1 AC6 8 ALA B 360 GLU B 361 HIS B 363 ILE B 374
SITE 2 AC6 8 GLY B 406 ILE B 407 HOH Y 138 HOH Y 246
SITE 1 AC7 7 ALA C 360 GLU C 361 HIS C 363 ILE C 374
SITE 2 AC7 7 GLY C 406 ILE C 407 HOH X 116
SITE 1 AC8 8 ALA D 360 GLU D 361 HIS D 363 ILE D 374
SITE 2 AC8 8 GLY D 406 ILE D 407 HOH W 132 HOH W 233
SITE 1 AC9 5 ARG A 125 TYR A 547 SER A 630 HIS A 740
SITE 2 AC9 5 HOH Z 244
SITE 1 BC1 4 ARG B 125 TYR B 547 SER B 630 HIS B 740
SITE 1 BC2 5 ARG C 125 TYR C 547 SER C 630 HIS C 740
SITE 2 BC2 5 HOH X 228
SITE 1 BC3 4 ARG D 125 TYR D 547 SER D 630 HIS D 740
CRYST1 61.644 117.491 133.057 112.44 94.72 91.30 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 0.016222 0.000368 0.001605 0.00000
SCALE2 0.000000 0.008513 0.003551 0.00000
SCALE3 0.000000 0.000000 0.008171 0.00000
TER 5967 PRO A 766
TER 11934 PRO B 766
TER 17901 PRO C 766
TER 23868 PRO D 766
MASTER 353 0 45 73 205 0 27 625421 4 662 224
END |