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HEADER HYDROLASE 23-FEB-06 2G5P
TITLE CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPPIV)
TITLE 2 COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO) INHIBITOR 21AC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL
COMPND 6 ACTIVATION ANTIGEN CD26, TP103, ADENOSINE DEAMINASE
COMPND 7 COMPLEXING PROTEIN 2, ADABP, CONTAINS: DIPEPTIDYL
COMPND 8 PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV
COMPND 9 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM,
COMPND 10 DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 11 EC: 3.4.14.5;
COMPND 12 ENGINEERED: 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_COMMON: FALL ARMYWORM
KEYWDS SERINE PEPTIDASE, BETA-PROPELLER
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.LONGENECKER,E.H.FRY,M.R.LAKE,L.R.SOLOMON,Z.PEI,X.LI
REVDAT 1 04-JUL-06 2G5P 0
JRNL AUTH Z.PEI,X.LI,K.LONGENECKER,T.W.VON GELDERN,
JRNL AUTH 2 P.E.WIEDEMAN,T.H.LUBBEN,B.A.ZINKER,K.STEWART,
JRNL AUTH 3 S.J.BALLARON,M.A.STASHKO,A.K.MIKA,D.W.BENO,M.LONG,
JRNL AUTH 4 H.WELLS,A.J.KEMPF-GROTE,D.J.MADAR,T.S.MCDERMOTT,
JRNL AUTH 5 L.BHAGAVATULA,M.G.FICKES,D.PIREH,L.R.SOLOMON,
JRNL AUTH 6 M.R.LAKE,R.EDALJI,E.H.FRY,H.L.SHAM,J.M.TREVILLYAN
JRNL TITL DISCOVERY, STRUCTURE-ACTIVITY RELATIONSHIP, AND
JRNL TITL 2 PHARMACOLOGICAL EVALUATION OF
JRNL TITL 3 (5-SUBSTITUTED-PYRROLIDINYL-2-CARBONYL)-2-
JRNL TITL 4 CYANOPYRROLIDINES AS POTENT DIPEPTIDYL PEPTIDASE
JRNL TITL 5 IV INHIBITORS.
JRNL REF J.MED.CHEM. V. 49 3520 2006
JRNL REFN ASTM JMCMAR US ISSN 0022-2623
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 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 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.6
REMARK 3 NUMBER OF REFLECTIONS : 61107
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 3136
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11898
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 1599
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.51900
REMARK 3 B22 (A**2) : -1.29700
REMARK 3 B33 (A**2) : 2.81600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.53200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : MSI_CNX_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ADD.PAR
REMARK 3 PARAMETER FILE 3 : MSI_CNX_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2G5P COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-2006.
REMARK 100 THE RCSB ID CODE IS RCSB036720.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61222
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.29500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 63.25800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 O ALA A 130 O HOH 952 2.11
REMARK 500 O HOH 27 O HOH 1415 2.14
REMARK 500 O HOH 1 O HOH 296 2.16
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 325 SD MET A 325 CE -0.071
REMARK 500 SER A 630 C SER A 630 O 0.164
REMARK 500 MET B 325 SD MET B 325 CE -0.049
REMARK 500 MET B 689 SD MET B 689 CE -0.069
REMARK 500 MET B 755 SD MET B 755 CE -0.051
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 ARG A 40 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 LEU A 90 CA - CB - CG ANGL. DEV. = 8.1 DEGREES
REMARK 500 GLY A 111 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 SER A 158 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 VAL A 160 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 GLU A 206 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 PHE A 240 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ILE A 287 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 PRO A 290 C - N - CA ANGL. DEV. = 8.4 DEGREES
REMARK 500 LEU A 300 N - CA - C ANGL. DEV. =-13.3 DEGREES
REMARK 500 ILE A 319 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 VAL A 341 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 ALA A 342 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 GLU A 378 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 GLN A 388 N - CA - C ANGL. DEV. =-12.9 DEGREES
REMARK 500 GLU A 448 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 SER A 458 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 ILE A 529 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 TYR A 547 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 ALA A 548 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 VAL A 656 N - CA - C ANGL. DEV. =-12.0 DEGREES
REMARK 500 GLU A 699 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 VAL A 711 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ILE A 742 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 ALA A 743 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG B 40 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 GLY B 111 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 VAL B 160 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 GLU B 206 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 ILE B 236 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 ILE B 287 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 PRO B 290 C - N - CA ANGL. DEV. = 8.1 DEGREES
REMARK 500 LEU B 300 N - CA - C ANGL. DEV. =-13.2 DEGREES
REMARK 500 ILE B 319 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 VAL B 341 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 ALA B 342 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 GLU B 378 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 GLN B 388 N - CA - C ANGL. DEV. =-12.4 DEGREES
REMARK 500 GLU B 448 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 SER B 458 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 ILE B 529 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 TYR B 547 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ALA B 548 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 VAL B 656 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 GLU B 699 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 VAL B 711 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ILE B 742 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ALA B 743 N - CA - C ANGL. DEV. = 8.8 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 278 -9.40 129.84
REMARK 500 ALA A 342 -27.72 145.27
REMARK 500 GLU A 521 -41.12 72.05
REMARK 500 SER A 630 -114.37 57.66
REMARK 500 SER B 278 -9.40 128.51
REMARK 500 ALA B 342 -27.88 144.93
REMARK 500 GLU B 521 -39.36 72.47
REMARK 500 SER B 630 -110.65 58.62
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 943 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH 1168 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH 1215 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH 1217 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH 1468 DISTANCE = 6.25 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G5T RELATED DB: PDB
DBREF 2G5P A 39 764 UNP P27487 DPP4_HUMAN 39 764
DBREF 2G5P B 39 764 UNP P27487 DPP4_HUMAN 39 764
SEQRES 1 A 726 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 726 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 726 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 726 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 726 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 726 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 726 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 726 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 726 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 726 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 726 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 726 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 726 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 726 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 726 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 726 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 726 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 726 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 726 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 726 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 726 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 726 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 726 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 726 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 726 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 726 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 726 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 726 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 726 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 726 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 726 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 726 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 726 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 726 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 726 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 726 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 726 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 726 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 726 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 726 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 726 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 726 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 726 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 726 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 726 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 726 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 726 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 726 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 726 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 726 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 726 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 726 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 726 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 726 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 726 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 726 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
SEQRES 1 B 726 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 726 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 726 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 726 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 726 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 726 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 726 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 726 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 726 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 726 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 726 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 726 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 726 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 726 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 726 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 726 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 726 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 726 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 726 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 726 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 726 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 726 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 726 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 726 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 726 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 726 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 726 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 726 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 726 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 726 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 726 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 B 726 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 726 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 726 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 726 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 726 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 726 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 726 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 726 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 726 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 726 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 726 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 726 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 726 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 726 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 726 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 726 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 726 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 726 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 726 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 726 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 726 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 726 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 726 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 726 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 726 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
HET ADF A 800 29
HETNAM ADF 4-{[(2R,5S)-5-{[(2S)-2-(AMINOMETHYL)PYRROLIDIN-1-
HETNAM 2 ADF YL]CARBONYL}PYRROLIDIN-2-YL]METHOXY}-3-TERT-
HETNAM 3 ADF BUTYLBENZOIC ACID
FORMUL 3 ADF C22 H33 N3 O4
FORMUL 4 HOH *1599(H2 O1)
HELIX 1 1 THR A 44 LYS A 50 1 7
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 GLU A 421 MET A 425 5 5
HELIX 5 5 ASN A 497 GLN A 505 1 9
HELIX 6 6 ASN A 562 ASN A 572 1 11
HELIX 7 7 GLY A 587 HIS A 592 1 6
HELIX 8 8 ALA A 593 ASN A 595 5 3
HELIX 9 9 THR A 600 SER A 614 1 15
HELIX 10 10 SER A 630 GLY A 641 1 12
HELIX 11 11 ARG A 658 TYR A 662 5 5
HELIX 12 12 ASP A 663 GLY A 672 1 10
HELIX 13 13 ASN A 679 SER A 686 1 8
HELIX 14 14 VAL A 688 VAL A 698 5 11
HELIX 15 15 PHE A 713 ASP A 725 1 13
HELIX 16 16 SER A 744 SER A 764 1 21
HELIX 17 17 THR B 44 LYS B 50 1 7
HELIX 18 18 ASP B 200 VAL B 207 1 8
HELIX 19 19 PRO B 290 ILE B 295 1 6
HELIX 20 20 GLU B 421 MET B 425 5 5
HELIX 21 21 ASN B 497 GLN B 505 1 9
HELIX 22 22 ASN B 562 GLU B 571 1 10
HELIX 23 23 GLY B 587 HIS B 592 1 6
HELIX 24 24 ALA B 593 ASN B 595 5 3
HELIX 25 25 THR B 600 SER B 614 1 15
HELIX 26 26 SER B 630 GLY B 641 1 12
HELIX 27 27 ARG B 658 TYR B 662 5 5
HELIX 28 28 ASP B 663 GLY B 672 1 10
HELIX 29 29 ASN B 679 SER B 686 1 8
HELIX 30 30 VAL B 688 VAL B 698 5 11
HELIX 31 31 PHE B 713 ASP B 725 1 13
HELIX 32 32 SER B 744 SER B 764 1 21
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 LEU A 60 TRP A 62 0
SHEET 2 B 4 GLU A 67 TYR A 70 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ILE A 76 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 B 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 C 4 ASP A 104 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
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 LYS A 175 N LEU A 164
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 ILE A 285 ILE A 287 -1 O ILE A 287 N PHE A 268
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 ARG A 310 N ALA A 306
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 TRP A 337 CYS A 339 -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 ARG A 310 N ALA A 306
SHEET 3 I 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 I 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
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 LEU A 701 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 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 LEU B 60 TRP B 62 0
SHEET 2 O 4 GLU B 67 TYR B 70 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 O 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 P 4 ILE B 102 ILE B 107 0
SHEET 2 P 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 P 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 P 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 Q 4 TRP B 154 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 Q 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 S 4 ILE B 285 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
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 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 U 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 V 4 HIS B 298 THR B 307 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 V 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 V 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 W 4 HIS B 363 PHE B 364 0
SHEET 2 W 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 W 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 W 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 X 4 VAL B 404 LEU B 410 0
SHEET 2 X 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 X 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 X 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 Y 4 TYR B 457 PHE B 461 0
SHEET 2 Y 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 Y 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 Z 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Z 8 TYR B 540 VAL B 546 1 N ASP B 545 O ALA B 576
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Z 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 328 CYS A 339
SSBOND 2 CYS A 385 CYS A 394
SSBOND 3 CYS A 444 CYS A 447
SSBOND 4 CYS A 454 CYS A 472
SSBOND 5 CYS A 649 CYS A 762
SSBOND 6 CYS B 328 CYS B 339
SSBOND 7 CYS B 385 CYS B 394
SSBOND 8 CYS B 444 CYS B 447
SSBOND 9 CYS B 454 CYS B 472
SSBOND 10 CYS B 649 CYS B 762
LINK OG SER A 630 C21 ADF A 800
CISPEP 1 ALA A 289 PRO A 290 0 -2.05
CISPEP 2 GLY A 474 PRO A 475 0 -0.54
CISPEP 3 ALA B 289 PRO B 290 0 0.48
CISPEP 4 GLY B 474 PRO B 475 0 0.31
CRYST1 65.515 126.516 112.215 90.00 99.10 90.00 P 1 21 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 0.015264 0.000000 0.002445 0.00000
SCALE2 0.000000 0.007904 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009025 0.00000
TER 5950 SER A 764
TER 11900 SER B 764
MASTER 334 0 1 32 102 0 0 613526 2 50 112
END |