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HEADER HYDROLASE 29-JAN-08 3C43
TITLE HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN COMPLEX WITH A
TITLE 2 FLOUROOLEFIN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL
COMPND 6 ACTIVATION ANTIGEN CD26, TP103, ADENOSINE DEAMINASE
COMPND 7 COMPLEXING PROTEIN 2, ADABP;
COMPND 8 EC: 3.4.14.5;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DPP4, ADCP2, CD26;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBLUEBAC4.5
KEYWDS ALPHA/BETA, BETA-PROPELLER, DIMER, AMINOPEPTIDASE,
KEYWDS 2 GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE, SECRETED,
KEYWDS 3 SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SCAPIN,S.D.EDMONDSON,A.E.WEBER
REVDAT 1 22-APR-08 3C43 0
JRNL AUTH S.D.EDMONDSON,L.WEI,J.XU,J.SHANG,S.XU,J.PANG,
JRNL AUTH 2 A.CHAUDHARY,D.C.DEAN,H.HE,B.LEITING,K.A.LYONS,
JRNL AUTH 3 R.A.PATEL,S.B.PATEL,G.SCAPIN,J.K.WU,M.G.BECONI,
JRNL AUTH 4 N.A.THORNBERRY,A.E.WEBER
JRNL TITL FLUOROOLEFINS AS AMIDE BOND MIMICS IN DIPEPTIDYL
JRNL TITL 2 PEPTIDASE IV INHIBITORS
JRNL REF BIOORG.MED.CHEM.LETT. V. 18 2409 2008
JRNL REFN ASTM BMCLE8 UK ISSN 0960-894X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 88040
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4426
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 92887
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 423
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 : 11930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 398
REMARK 3 SOLVENT ATOMS : 721
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.00200
REMARK 3 B22 (A**2) : -1.60400
REMARK 3 B33 (A**2) : -6.39800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.42
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.89
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3C43 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB046315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88800
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 5.890
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.37
REMARK 200 R MERGE FOR SHELL (I) : 0.43800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: PDB ENTRY 1X70
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, SODIUM ACETATE, TRIS, PH
REMARK 280 8.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 58.93200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.35600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.91750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.35600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.93200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.91750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10640 ANGSTROM**2
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 40 114.26 57.41
REMARK 500 TYR A 58 77.28 -153.76
REMARK 500 GLN A 123 -104.22 -116.60
REMARK 500 TRP A 124 -146.63 -89.39
REMARK 500 ARG A 140 52.95 34.27
REMARK 500 HIS A 162 38.72 -152.30
REMARK 500 ILE A 193 -61.82 -126.73
REMARK 500 SER A 242 -159.91 64.24
REMARK 500 GLN A 320 38.75 -64.85
REMARK 500 ARG A 358 165.18 173.84
REMARK 500 ASN A 450 76.30 -169.10
REMARK 500 ASP A 515 -166.92 -162.38
REMARK 500 GLU A 521 3.43 59.48
REMARK 500 LYS A 536 3.66 -64.66
REMARK 500 TYR A 547 -66.57 -129.16
REMARK 500 ARG A 596 14.44 58.74
REMARK 500 THR A 600 -87.98 -121.74
REMARK 500 ASN A 621 -7.65 -56.80
REMARK 500 SER A 630 -118.73 61.82
REMARK 500 ASP A 678 -92.19 -107.30
REMARK 500 ASN A 710 -69.49 -90.61
REMARK 500 ASP A 739 -161.17 -104.81
REMARK 500 ILE A 742 45.38 37.33
REMARK 500 ARG B 40 115.47 49.80
REMARK 500 SER B 64 -162.74 -161.97
REMARK 500 HIS B 66 19.96 -152.45
REMARK 500 GLU B 73 57.86 71.59
REMARK 500 ASN B 74 -22.80 68.14
REMARK 500 PHE B 95 40.65 -108.38
REMARK 500 GLU B 97 32.18 -90.63
REMARK 500 GLN B 123 -99.98 -116.32
REMARK 500 TRP B 124 -146.61 -95.64
REMARK 500 ASN B 151 35.72 70.85
REMARK 500 HIS B 162 28.72 -146.49
REMARK 500 GLU B 191 124.06 -38.48
REMARK 500 ASP B 192 12.42 57.87
REMARK 500 ILE B 193 -61.74 -127.51
REMARK 500 SER B 242 -161.71 63.69
REMARK 500 GLN B 320 38.24 -65.83
REMARK 500 ARG B 358 161.61 173.99
REMARK 500 ASN B 377 -169.94 -79.94
REMARK 500 LYS B 423 15.09 53.29
REMARK 500 ASP B 438 91.96 -164.00
REMARK 500 ASN B 450 74.65 -168.73
REMARK 500 ARG B 492 171.27 171.14
REMARK 500 TYR B 547 -71.10 -137.06
REMARK 500 THR B 600 -96.48 -123.75
REMARK 500 SER B 630 -121.87 61.77
REMARK 500 ASP B 678 -102.16 -121.12
REMARK 500 ASN B 710 -75.49 -87.57
REMARK 500 ASP B 739 -160.17 -101.38
REMARK 500 SER B 764 58.31 39.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 700 0.08 SIDE_CHAIN
REMARK 500 TYR B 735 0.06 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1085
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1092
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR RESIDUE A 1150
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1219
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1220
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1229
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1321
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1322
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1520
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2085
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2086
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2092
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2150
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2219
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2220
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2229
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2230
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2281
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2282
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE B 2321
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: 315 BINDING SITE FOR RESIDUE A 1
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: 315 BINDING SITE FOR RESIDUE B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X70 RELATED DB: PDB
REMARK 900 RELATED ID: 2FJP RELATED DB: PDB
REMARK 900 RELATED ID: 2HHA RELATED DB: PDB
REMARK 900 RELATED ID: 2IIT RELATED DB: PDB
REMARK 900 RELATED ID: 2IIV RELATED DB: PDB
REMARK 900 RELATED ID: 2OPH RELATED DB: PDB
REMARK 900 RELATED ID: 3C45 RELATED DB: PDB
DBREF 3C43 A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3C43 B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 3C43 THR A 39 UNP P27487 SER 39 ENGINEERED
SEQADV 3C43 THR B 39 UNP P27487 SER 39 ENGINEERED
SEQRES 1 A 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
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 VAL
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 ILE GLU PRO ASN LEU PRO
SEQRES 12 A 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 728 TYR ASN GLY ILE 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 VAL PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR 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 TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR LYS ILE GLN LEU SER 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 VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 728 ASN GLU 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 LEU ASP
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU ASN 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 ALA
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN 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 SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER ARG 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 HIS 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 ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
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 VAL
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 ILE GLU PRO ASN LEU PRO
SEQRES 12 B 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 728 TYR ASN GLY ILE 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 VAL PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR 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 TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR LYS ILE GLN LEU SER 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 VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 728 ASN GLU 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 LEU ASP
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU ASN 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 ALA
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN 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 SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER ARG 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 HIS 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 ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
MODRES 3C43 ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN A 92 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN A 281 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN A 321 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN A 520 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN B 92 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN B 219 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN B 281 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN B 321 ASN GLYCOSYLATION SITE
MODRES 3C43 ASN A 150 ASN GLYCOSYLATION SITE
HET NAG A1085 14
HET NDG A1086 14
HET NAG A1092 14
HET NDG A1150 14
HET NAG A1151 14
HET NAG A1219 14
HET NAG A1220 14
HET NAG A1229 14
HET NDG A1230 14
HET NAG A1281 14
HET NAG A1321 14
HET NAG A1322 14
HET NAG A1520 14
HET NAG B2085 14
HET NAG B2086 14
HET NAG B2092 14
HET NAG B2150 14
HET NAG B2219 14
HET NAG B2220 14
HET NAG B2229 14
HET NAG B2230 14
HET NAG B2281 14
HET NAG B2282 14
HET NAG B2321 14
HET 315 A 1 31
HET 315 B 2 31
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM 315 (2S,3S)-4-CYCLOPROPYL-3-{(3R,5R)-3-[2-FLUORO-4-
HETNAM 2 315 (METHYLSULFONYL)PHENYL]-1,2,4-OXADIAZOLIDIN-5-YL}-1-
HETNAM 3 315 [(3S)-3-FLUOROPYRROLIDIN-1-YL]-1-OXOBUTAN-2-AMINE
HETSYN NAG NAG
FORMUL 3 NAG 21(C8 H15 N O6)
FORMUL 3 NDG 3(C8 H15 N O6)
FORMUL 18 315 2(C20 H28 F2 N4 O4 S)
FORMUL 20 HOH *721(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 PRO A 290 ILE A 295 1 6
HELIX 4 4 LEU A 340 GLN A 344 5 5
HELIX 5 5 GLU A 421 MET A 425 5 5
HELIX 6 6 ASN A 497 GLN A 505 1 9
HELIX 7 7 ASN A 562 THR A 570 1 9
HELIX 8 8 GLY A 587 HIS A 592 1 6
HELIX 9 9 ALA A 593 ASN A 595 5 3
HELIX 10 10 THR A 600 LYS A 615 1 16
HELIX 11 11 SER A 630 GLY A 641 1 12
HELIX 12 12 ARG A 658 TYR A 662 5 5
HELIX 13 13 ASP A 663 GLY A 672 1 10
HELIX 14 14 ASN A 679 SER A 686 1 8
HELIX 15 15 VAL A 688 VAL A 698 5 11
HELIX 16 16 HIS A 712 VAL A 726 1 15
HELIX 17 17 SER A 744 PHE A 763 1 20
HELIX 18 18 THR B 44 LYS B 50 1 7
HELIX 19 19 GLU B 91 GLY B 99 5 9
HELIX 20 20 ASP B 200 VAL B 207 1 8
HELIX 21 21 ASP B 274 LEU B 276 5 3
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 VAL B 341 GLN B 344 5 4
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 ASN B 497 GLN B 505 1 9
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 LYS B 615 1 16
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ARG B 658 TYR B 662 5 5
HELIX 32 32 ASP B 663 GLY B 672 1 10
HELIX 33 33 ASN B 679 SER B 686 1 8
HELIX 34 34 VAL B 688 VAL B 698 5 11
HELIX 35 35 PHE B 713 VAL B 726 1 14
HELIX 36 36 SER B 744 PHE B 763 1 20
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 ARG A 61 TRP A 62 0
SHEET 2 B 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ASN A 75 ASN A 80 -1 O ASN A 75 N GLN A 72
SHEET 4 B 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 C 4 ILE A 102 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O GLU A 117 N ASN A 103
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 TRP A 154 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 F 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 THR A 307 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 I 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 I 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 L 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 L 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 4 LEU B 60 TRP B 62 0
SHEET 2 N 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 N 4 ASN B 75 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 N 4 SER B 86 LEU B 90 -1 O LEU B 90 N ILE B 76
SHEET 1 O 4 ILE B 102 ILE B 107 0
SHEET 2 O 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 O 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 O 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 P 4 TRP B 154 TRP B 157 0
SHEET 2 P 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 P 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 P 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 Q 3 ILE B 194 ASN B 196 0
SHEET 2 Q 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 R 4 ILE B 194 ASN B 196 0
SHEET 2 R 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 4 THR B 265 ASN B 272 -1 O VAL B 271 N LEU B 223
SHEET 4 R 4 ILE B 285 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 S 2 LEU B 235 PHE B 240 0
SHEET 2 S 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 T 4 HIS B 298 THR B 307 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 T 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 T 4 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 U 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 U 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 V 4 HIS B 363 PHE B 364 0
SHEET 2 V 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 V 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 V 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 W 4 VAL B 404 LEU B 410 0
SHEET 2 W 4 TYR B 414 SER B 419 -1 O ILE B 418 N ILE B 405
SHEET 3 W 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 W 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 X 4 TYR B 457 PHE B 461 0
SHEET 2 X 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 X 4 LEU B 479 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 X 4 LYS B 489 GLU B 495 -1 O LEU B 494 N TYR B 480
SHEET 1 Y 8 SER B 511 ILE B 518 0
SHEET 2 Y 8 LYS B 523 LEU B 530 -1 O PHE B 524 N ILE B 517
SHEET 3 Y 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Y 8 TYR B 540 VAL B 546 1 N ASP B 545 O ALA B 576
SHEET 5 Y 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 Y 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Y 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 Y 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.04
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.04
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.05
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
LINK O4 NAG A1229 C1 NDG A1230 1555 1555 1.13
LINK ND2 ASN A 85 C1 NAG A1085 1555 1555 1.45
LINK ND2 ASN A 92 C1 NAG A1092 1555 1555 1.46
LINK ND2 ASN A 219 C1 NAG A1219 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG A1229 1555 1555 1.45
LINK ND2 ASN A 281 C1 NAG A1281 1555 1555 1.46
LINK ND2 ASN A 321 C1 NAG A1321 1555 1555 1.44
LINK ND2 ASN A 520 C1 NAG A1520 1555 1555 1.45
LINK ND2 ASN B 85 C1 NAG B2085 1555 1555 1.45
LINK ND2 ASN B 92 C1 NAG B2092 1555 1555 1.46
LINK ND2 ASN B 150 C1 NAG B2150 1555 1555 1.46
LINK ND2 ASN B 219 C1 NAG B2219 1555 1555 1.45
LINK ND2 ASN B 229 C1 NAG B2229 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG B2281 1555 1555 1.45
LINK ND2 ASN B 321 C1 NAG B2321 1555 1555 1.45
LINK O4 NAG A1085 C1 NDG A1086 1555 1555 1.39
LINK O4 NDG A1150 C1 NAG A1151 1555 1555 1.40
LINK O4 NAG A1219 C1 NAG A1220 1555 1555 1.39
LINK O4 NAG A1321 C1 NAG A1322 1555 1555 1.39
LINK O4 NAG B2085 C1 NAG B2086 1555 1555 1.53
LINK O4 NAG B2219 C1 NAG B2220 1555 1555 1.50
LINK O4 NAG B2229 C1 NAG B2230 1555 1555 1.45
LINK O4 NAG B2281 C1 NAG B2282 1555 1555 1.42
LINK ND2 ASN A 150 C1 NDG A1150 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 0.57
CISPEP 2 GLY B 474 PRO B 475 0 0.11
CISPEP 3 LEU B 765 PRO B 766 0 -0.30
SITE 1 AC1 6 GLU A 67 ASN A 85 SER A 86 SER A 87
SITE 2 AC1 6 HOH A1818 HOH A1846
SITE 1 AC2 4 GLU A 73 ASN A 74 ASN A 75 ASN A 92
SITE 1 AC3 2 PRO A 149 ASN A 150
SITE 1 AC4 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC5 3 TYR A 330 GLU A 332 HOH A1585
SITE 1 AC6 5 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC6 5 HOH A1547
SITE 1 AC7 4 ASN A 321 MET A 348 SER A 349 THR A 350
SITE 1 AC8 1 ASP A 678
SITE 1 AC9 2 ASN A 520 ARG A 581
SITE 1 BC1 4 GLU B 67 ASN B 85 SER B 86 SER B 87
SITE 1 BC2 1 HOH B2536
SITE 1 BC3 6 GLU B 73 ASN B 74 ASN B 75 GLU B 91
SITE 2 BC3 6 ASN B 92 HOH B2451
SITE 1 BC4 3 ARG B 147 ASN B 150 HOH B2641
SITE 1 BC5 4 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 1 BC6 3 PHE B 222 ASN B 272 GLU B 332
SITE 1 BC7 6 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 BC7 6 HOH B2384 HOH B2568
SITE 1 BC8 1 THR B 231
SITE 1 BC9 3 TRP B 187 ASN B 281 HOH B2462
SITE 1 CC1 2 THR B 188 HOH B2462
SITE 1 CC2 2 ASN B 321 SER B 349
SITE 1 CC3 15 ARG A 125 GLU A 205 GLU A 206 PHE A 357
SITE 2 CC3 15 TYR A 547 SER A 552 GLN A 553 LYS A 554
SITE 3 CC3 15 SER A 630 TYR A 631 TYR A 662 TYR A 666
SITE 4 CC3 15 ASN A 710 HOH A1679 HOH A1806
SITE 1 CC4 15 ARG B 125 GLU B 205 GLU B 206 PHE B 357
SITE 2 CC4 15 TYR B 547 SER B 552 GLN B 553 LYS B 554
SITE 3 CC4 15 SER B 630 TYR B 631 TYR B 662 TYR B 666
SITE 4 CC4 15 ASN B 710 HOH B2584 HOH B2591
CRYST1 117.864 125.835 136.712 90.00 90.00 90.00 P 21 21 21 8
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 0.008484 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007315 0.00000
TER 5966 PRO A 766
TER 11932 PRO B 766
MASTER 355 0 26 36 100 0 32 613049 2 433 112
END |