| content |
HEADER HYDROLASE 12-OCT-07 2RIP
TITLE STRUCTURE OF DPPIV IN COMPLEX WITH AN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV; DPP IV; T-CELL
COMPND 5 ACTIVATION ANTIGEN CD26; TP103; ADENOSINE DEAMINASE
COMPND 6 COMPLEXING PROTEIN 2; ADABP;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DPPIV;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS
KEYWDS DPPIV, DIABETES, DRUG DESIGN, AMINOPEPTIDASE, GLYCOPROTEIN,
KEYWDS 2 HYDROLASE, MEMBRANE, PROTEASE, SECRETED, SERINE PROTEASE,
KEYWDS 3 SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.QIU
REVDAT 1 18-MAR-08 2RIP 0
JRNL AUTH J.W.CORBETT,K.DIRICO,W.SONG,B.P.BOSCOE,S.D.DORAN,
JRNL AUTH 2 D.BOYER,X.QIU,M.AMMIRATI,M.A.VANVOLKENBURG,
JRNL AUTH 3 R.K.MCPHERSON,J.C.PARKER,E.D.COX
JRNL TITL DESIGN AND SYNTHESIS OF POTENT AMIDO- AND
JRNL TITL 2 BENZYL-SUBSTITUTED
JRNL TITL 3 CIS-3-AMINO-4-(2-CYANOPYRROLIDIDE)PYRROLIDINYL
JRNL TITL 4 DPP-IV INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 6707 2007
JRNL REFN ASTM BMCLE8 UK ISSN 0960-894X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 20047
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1095
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1170
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.4090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 6158
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.53000
REMARK 3 B22 (A**2) : 1.53000
REMARK 3 B33 (A**2) : -3.06000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.496
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.372
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.972
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.911
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.845
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6319 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8608 ; 1.399 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 728 ; 6.724 ; 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): 926 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4824 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2607 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 192 ; 0.158 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 48 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.203 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3632 ; 0.589 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5892 ; 1.129 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2687 ; 1.396 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2716 ; 2.440 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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: NULL
REMARK 4
REMARK 4 2RIP 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 RCSB044905.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-2004
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
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39722
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : 0.12500
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.00580
REMARK 200 R SYM FOR SHELL (I) : 0.00580
REMARK 200 FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1WCY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%PEG, PH 8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,1/2-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 204.61000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.61000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.61000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 306.91500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.61000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.61000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 102.30500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.61000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.61000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 306.91500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.61000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.61000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 102.30500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 204.61000
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: 9010 ANGSTROM**2
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 61780 ANGSTROM**2
REMARK 350 GAIN IN SOLVENT FREE ENERGY: 49 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 0.000000 -1.000000 0.000000 138.44000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 138.44000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 204.61000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 96 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 171 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 243 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 302 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 51 51.08 76.38
REMARK 500 SER A 64 -153.51 -157.37
REMARK 500 GLU A 73 -93.35 63.01
REMARK 500 ASN A 74 -2.69 -140.48
REMARK 500 ASN A 92 26.12 -79.27
REMARK 500 PHE A 98 -22.54 -151.20
REMARK 500 TYR A 105 147.90 -172.70
REMARK 500 PRO A 109 38.30 -68.41
REMARK 500 ASP A 110 20.48 -159.34
REMARK 500 GLN A 123 -100.35 -111.10
REMARK 500 TRP A 124 -149.89 -88.31
REMARK 500 PRO A 178 -1.04 -50.79
REMARK 500 ASN A 179 20.86 -149.39
REMARK 500 ASP A 192 -3.30 65.05
REMARK 500 VAL A 207 -56.80 -126.98
REMARK 500 SER A 242 -165.29 70.40
REMARK 500 VAL A 279 -47.65 -132.10
REMARK 500 ALA A 306 -62.69 -95.02
REMARK 500 GLN A 320 32.67 -75.27
REMARK 500 GLU A 332 -74.64 -52.86
REMARK 500 LYS A 423 16.20 53.51
REMARK 500 ASN A 450 34.62 -152.07
REMARK 500 PRO A 451 -34.82 -30.99
REMARK 500 ALA A 465 33.10 73.22
REMARK 500 PRO A 478 130.11 -32.60
REMARK 500 LEU A 491 -66.32 -94.44
REMARK 500 ASN A 520 44.99 35.74
REMARK 500 TYR A 547 -69.04 -132.82
REMARK 500 CYS A 551 32.08 73.22
REMARK 500 ARG A 596 10.49 46.46
REMARK 500 THR A 600 -79.63 -130.89
REMARK 500 SER A 630 -131.86 55.78
REMARK 500 GLU A 660 0.59 -66.86
REMARK 500 ARG A 669 -34.80 -37.93
REMARK 500 ASP A 678 -105.25 -92.72
REMARK 500 ASN A 685 0.26 -63.62
REMARK 500 ASN A 710 -71.50 -75.32
REMARK 500 ASP A 737 -6.22 72.25
REMARK 500 ASP A 739 -153.75 -99.60
REMARK 500 ILE A 742 60.46 33.04
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 2085
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR RESIDUE A 3085
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR RESIDUE A 4085
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 4086
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 4087
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1219
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1229
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1281
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR RESIDUE A 1321
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: 34Q BINDING SITE FOR RESIDUE A 800
DBREF 2RIP A 38 766 UNP P27487 DPP4_HUMAN 38 766
SEQRES 1 A 729 ASP SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS
SEQRES 2 A 729 ASN THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE
SEQRES 3 A 729 SER ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE
SEQRES 4 A 729 LEU VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE
SEQRES 5 A 729 LEU GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE
SEQRES 6 A 729 ASN ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU
SEQRES 7 A 729 LEU GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR
SEQRES 8 A 729 THR ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN
SEQRES 9 A 729 LEU ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP
SEQRES 10 A 729 VAL THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL
SEQRES 11 A 729 TRP ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU
SEQRES 12 A 729 PRO SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE
SEQRES 13 A 729 ILE TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU
SEQRES 14 A 729 VAL PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN
SEQRES 15 A 729 GLY THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU
SEQRES 16 A 729 VAL PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER
SEQRES 17 A 729 LEU GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS
SEQRES 18 A 729 ALA GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL
SEQRES 19 A 729 ASN THR ASP SER LEU SER SER VAL THR ASN ALA THR SER
SEQRES 20 A 729 ILE GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP
SEQRES 21 A 729 HIS TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG
SEQRES 22 A 729 ILE SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER
SEQRES 23 A 729 VAL MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG
SEQRES 24 A 729 TRP ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER
SEQRES 25 A 729 THR THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO
SEQRES 26 A 729 HIS PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE
SEQRES 27 A 729 SER ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN
SEQRES 28 A 729 ILE ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR
SEQRES 29 A 729 TRP GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR
SEQRES 30 A 729 LEU TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY
SEQRES 31 A 729 GLY ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR
SEQRES 32 A 729 LYS VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG
SEQRES 33 A 729 CYS GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS
SEQRES 34 A 729 TYR TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU
SEQRES 35 A 729 TYR THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG
SEQRES 36 A 729 VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN
SEQRES 37 A 729 ASN VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE
SEQRES 38 A 729 LEU ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO
SEQRES 39 A 729 PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU
SEQRES 40 A 729 ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR
SEQRES 41 A 729 VAL PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR
SEQRES 42 A 729 GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER
SEQRES 43 A 729 GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG
SEQRES 44 A 729 ARG LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA
SEQRES 45 A 729 ALA ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS
SEQRES 46 A 729 ARG ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL
SEQRES 47 A 729 THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS
SEQRES 48 A 729 CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR
SEQRES 49 A 729 TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO
SEQRES 50 A 729 THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR
SEQRES 51 A 729 VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR
SEQRES 52 A 729 LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE
SEQRES 53 A 729 GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL
SEQRES 54 A 729 GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP
SEQRES 55 A 729 HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR
SEQRES 56 A 729 THR HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU
SEQRES 57 A 729 PRO
MODRES 2RIP ASN A 85 ASN GLYCOSYLATION SITE
MODRES 2RIP ASN A 150 ASN GLYCOSYLATION SITE
MODRES 2RIP ASN A 219 ASN GLYCOSYLATION SITE
MODRES 2RIP ASN A 229 ASN GLYCOSYLATION SITE
MODRES 2RIP ASN A 281 ASN GLYCOSYLATION SITE
MODRES 2RIP ASN A 321 ASN GLYCOSYLATION SITE
HET NAG A1085 14
HET NAG A2085 14
HET MAN A3085 11
HET MAN A4085 11
HET NAG A4086 14
HET NAG A4087 14
HET NAG A1219 14
HET NAG A1229 14
HET NAG A1281 14
HET NAG A1321 14
HET 34Q A 800 25
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM 34Q (3R,4R)-4-(PYRROLIDIN-1-YLCARBONYL)-1-(QUINOXALIN-2-
HETNAM 2 34Q YLCARBONYL)PYRROLIDIN-3-AMINE
HETSYN NAG NAG
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 MAN 2(C6 H12 O6)
FORMUL 8 34Q C18 H21 N5 O2
FORMUL 9 HOH *27(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 VAL A 341 GLN A 344 5 4
HELIX 5 5 GLU A 421 MET A 425 5 5
HELIX 6 6 ASN A 497 ASN A 506 1 10
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 MET A 616 1 17
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 ASP A 725 1 14
HELIX 17 17 SER A 744 SER A 764 1 21
SHEET 1 A 4 LEU A 60 TRP A 62 0
SHEET 2 A 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 A 4 SER A 86 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 B 4 ILE A 102 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 B 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 THR A 152 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 C 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 D 3 ILE A 194 ASN A 196 0
SHEET 2 D 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 D 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 E 4 ILE A 194 ASN A 196 0
SHEET 2 E 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 E 4 ILE A 285 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 G 4 HIS A 298 THR A 307 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 G 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 G 4 ARG A 336 CYS A 339 -1 O ASN A 338 N ASP A 329
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 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 I 4 PRO A 362 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 J 4 VAL A 404 LEU A 410 0
SHEET 2 J 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 ASP A 438 CYS A 444 -1 O ASP A 438 N GLN A 435
SHEET 1 K 4 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 K 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 K 4 LYS A 489 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 L 8 SER A 511 LEU A 519 0
SHEET 2 L 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O SER A 577 N GLN A 527
SHEET 4 L 8 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 5 L 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 L 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 L 8 GLU A 699 GLY A 705 1 O GLU A 699 N GLY A 650
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.07
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.02
LINK ND2 ASN A 85 C1 NAG A1085 1555 1555 1.43
LINK ND2 ASN A 150 C1 NAG A4086 1555 1555 1.45
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 1.45
LINK ND2 ASN A 321 C1 NAG A1321 1555 1555 1.45
LINK O4 NAG A1085 C1 NAG A2085 1555 1555 1.45
LINK O4 NAG A2085 C1 MAN A3085 1555 1555 1.44
LINK O6 MAN A3085 C1 MAN A4085 1555 1555 1.44
LINK O4 NAG A4086 C1 NAG A4087 1555 1555 1.44
CISPEP 1 GLY A 474 PRO A 475 0 -1.99
SITE 1 AC1 7 PHE A 79 ASN A 80 ASN A 85 SER A 86
SITE 2 AC1 7 SER A 87 GLN A 388 THR A 395
SITE 1 AC3 1 HOH A 11
SITE 1 AC4 2 ASP A 38 SER A 39
SITE 1 AC5 3 ARG A 147 ILE A 148 ASN A 150
SITE 1 AC6 1 HOH A 27
SITE 1 AC7 3 ASN A 219 GLN A 308 GLU A 309
SITE 1 AC8 2 ILE A 194 ASN A 229
SITE 1 AC9 2 TRP A 187 ASN A 281
SITE 1 BC1 2 ILE A 319 ASN A 321
SITE 1 BC2 9 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 BC2 9 PHE A 357 SER A 630 TYR A 662 TYR A 666
SITE 3 BC2 9 ASN A 710
CRYST1 69.220 69.220 409.220 90.00 90.00 90.00 P 43 21 2 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 0.014447 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014447 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002444 0.00000
TER 5973 PRO A 766
MASTER 352 0 11 17 49 0 13 6 6158 1 171 57
END |