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HEADER HYDROLASE 10-MAR-06 2GBG
TITLE RAT DPP-IV WITH ALKYNYL CYANOPYRROLIDINE #2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM (RESIDUES 38-
COMPND 5 767);
COMPND 6 EC: 3.4.14.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT
KEYWDS SERINE PEPTIDASE BETA PROPELLER
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.LONGENECKER,C.G.JAKOB,E.H.FRY,S.WILK
REVDAT 1 04-JUL-06 2GBG 0
JRNL AUTH K.L.LONGENECKER,K.D.STEWART,D.J.MADAR,C.G.JAKOB,
JRNL AUTH 2 E.H.FRY,S.WILK,C.W.LIN,S.J.BALLARON,M.A.STASHKO,
JRNL AUTH 3 T.H.LUBBEN,H.YONG,D.PIREH,Z.PEI,F.BASHA,
JRNL AUTH 4 P.E.WIEDEMAN,T.W.VON GELDERN,J.M.TREVILLYAN,
JRNL AUTH 5 V.S.STOLL
JRNL TITL CRYSTAL STRUCTURES OF DPP-IV (CD26) FROM RAT
JRNL TITL 2 KIDNEY EXHIBIT FLEXIBLE ACCOMMODATION OF
JRNL TITL 3 PEPTIDASE-SELECTIVE INHIBITORS.
JRNL REF BIOCHEMISTRY V. 45 7474 2006
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 59077
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) : 0.235
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2997
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 : 11840
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : PROTEIN_REPADD.PARAM
REMARK 3 PARAMETER FILE 2 : ADD.PAR
REMARK 3 PARAMETER FILE 3 : MSI_CNX_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : MSI_CNX_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : 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 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GBG COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-2006.
REMARK 100 THE RCSB ID CODE IS RCSB036919.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.20
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59362
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.68800
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8 M AMMONIUM SULFATE AND 100MM
REMARK 280 SODIUM ACETATE, PH 4.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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 5555 Z,X,Y
REMARK 290 6555 1/2+Z,1/2-X,-Y
REMARK 290 7555 1/2-Z,-X,1/2+Y
REMARK 290 8555 -Z,1/2+X,1/2-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,1/2+Z,1/2-X
REMARK 290 11555 1/2+Y,1/2-Z,-X
REMARK 290 12555 1/2-Y,-Z,1/2+X
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 103.75000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 103.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.75000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 103.75000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 103.75000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 103.75000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 103.75000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 103.75000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 103.75000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 103.75000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 103.75000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 103.75000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 103.75000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 103.75000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 103.75000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 103.75000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 103.75000
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 39 CG CD NE CZ NH1 NH2
REMARK 470 THR A 40 OG1 CG2
REMARK 470 THR A 42 OG1 CG2
REMARK 470 LEU A 43 CG CD1 CD2
REMARK 470 PHE A 96 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 442 CG OD1 ND2
REMARK 470 LYS A 503 CG CD CE NZ
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 39 CG CD NE CZ NH1 NH2
REMARK 470 THR B 40 OG1 CG2
REMARK 470 THR B 42 OG1 CG2
REMARK 470 LEU B 43 CG CD1 CD2
REMARK 470 PHE B 96 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B 442 CG OD1 ND2
REMARK 470 LYS B 503 CG CD CE NZ
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 283 SD MET A 283 CE 0.110
REMARK 500 CYS A 299 CB CYS A 299 SG -0.083
REMARK 500 MET A 323 SD MET A 323 CE -0.054
REMARK 500 CYS A 352 CB CYS A 352 SG -0.069
REMARK 500 GLU A 453 CB GLU A 453 CG 0.060
REMARK 500 MET A 504 SD MET A 504 CE 0.053
REMARK 500 SER A 631 C SER A 631 O 0.157
REMARK 500 MET A 639 SD MET A 639 CE -0.072
REMARK 500 MET A 690 SD MET A 690 CE -0.167
REMARK 500 MET A 756 SD MET A 756 CE -0.083
REMARK 500 MET B 283 SD MET B 283 CE 0.122
REMARK 500 CYS B 299 CB CYS B 299 SG -0.069
REMARK 500 CYS B 352 CB CYS B 352 SG -0.058
REMARK 500 GLU B 453 CB GLU B 453 CG 0.052
REMARK 500 MET B 690 SD MET B 690 CE -0.107
REMARK 500 MET B 756 SD MET B 756 CE -0.091
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 ALA A 79 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLU A 89 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASN A 90 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 SER A 156 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 GLU A 204 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLY A 218 N - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 ILE A 234 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 THR A 278 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 LEU A 298 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 SER A 305 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 ILE A 317 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 TRP A 403 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 LEU A 450 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 SER A 459 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 ASP A 497 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 ILE A 518 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 ILE A 530 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 TYR A 548 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 GLY A 585 N - CA - C ANGL. DEV. = 13.3 DEGREES
REMARK 500 GLY A 618 N - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 VAL A 657 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 TRP A 660 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 VAL A 712 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 HIS A 713 N - CA - C ANGL. DEV. = 19.3 DEGREES
REMARK 500 GLU B 89 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASN B 90 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 SER B 156 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 GLU B 204 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 GLY B 218 N - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 ILE B 234 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ILE B 268 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 THR B 278 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 LEU B 298 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 SER B 305 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 ILE B 317 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 TRP B 403 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 LEU B 450 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 SER B 459 N - CA - C ANGL. DEV. =-12.6 DEGREES
REMARK 500 ASP B 497 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 ILE B 518 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 ILE B 530 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 TYR B 548 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 GLY B 585 N - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 GLY B 618 N - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 VAL B 657 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 VAL B 712 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 HIS B 713 N - CA - C ANGL. DEV. = 19.7 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 GLU A 80 -88.13 123.44
REMARK 500 THR A 92 -80.36 36.64
REMARK 500 SER A 631 -115.26 47.52
REMARK 500 PHE A 714 -45.39 71.67
REMARK 500 GLU B 80 -87.62 123.61
REMARK 500 THR B 92 -80.36 35.96
REMARK 500 SER B 631 -115.87 43.18
REMARK 500 PHE B 714 -44.22 72.32
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GBC RELATED DB: PDB
REMARK 900 NATIVE DPP-IV FROM RAT
REMARK 900 RELATED ID: 2GBF RELATED DB: PDB
REMARK 900 RAT DPP-IV WITH ALKYNYL CYANOPYRROLIDINE #1
DBREF 2GBG A 38 767 UNP P14740 DPP4_RAT 38 767
DBREF 2GBG B 38 767 UNP P14740 DPP4_RAT 38 767
SEQRES 1 A 730 ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN THR
SEQRES 2 A 730 PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER ASP
SEQRES 3 A 730 SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 4 A 730 PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU GLU
SEQRES 5 A 730 ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER ASP
SEQRES 6 A 730 TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU GLU
SEQRES 7 A 730 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 A 730 SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 A 730 THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 10 A 730 TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP LYS
SEQRES 11 A 730 ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO SER
SEQRES 12 A 730 HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE PHE
SEQRES 13 A 730 ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE PHE
SEQRES 14 A 730 GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 A 730 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL PRO
SEQRES 16 A 730 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 A 730 TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA GLY
SEQRES 18 A 730 ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN THR
SEQRES 19 A 730 ASP SER LEU SER SER THR THR THR THR ILE PRO MET GLN
SEQRES 20 A 730 ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS TYR
SEQRES 21 A 730 LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE SER
SEQRES 22 A 730 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 A 730 ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP ASN
SEQRES 24 A 730 CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA THR
SEQRES 25 A 730 GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE
SEQRES 26 A 730 THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER ASP
SEQRES 27 A 730 LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS ASP
SEQRES 28 A 730 ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS GLY
SEQRES 29 A 730 ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER ASP
SEQRES 30 A 730 TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET PRO
SEQRES 31 A 730 GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP HIS
SEQRES 32 A 730 THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO GLU
SEQRES 33 A 730 ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU ALA
SEQRES 34 A 730 LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU PRO
SEQRES 35 A 730 LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU LEU
SEQRES 36 A 730 ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU
SEQRES 37 A 730 GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE
SEQRES 38 A 730 VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE LEU
SEQRES 39 A 730 PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU
SEQRES 40 A 730 ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP
SEQRES 41 A 730 ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER
SEQRES 42 A 730 THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY
SEQRES 43 A 730 SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN
SEQRES 44 A 730 LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE GLU
SEQRES 45 A 730 ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP SER
SEQRES 46 A 730 LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY TYR
SEQRES 47 A 730 VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE
SEQRES 48 A 730 LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU
SEQRES 49 A 730 TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU
SEQRES 50 A 730 PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER
SEQRES 51 A 730 THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU
SEQRES 52 A 730 TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS
SEQRES 53 A 730 PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP
SEQRES 54 A 730 ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU
SEQRES 55 A 730 ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE
SEQRES 56 A 730 TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE SER
SEQRES 57 A 730 LEU ARG
SEQRES 1 B 730 ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS ASN THR
SEQRES 2 B 730 PHE ARG VAL LYS SER TYR SER LEU ARG TRP VAL SER ASP
SEQRES 3 B 730 SER GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 4 B 730 PHE ASN ALA GLU HIS GLY ASN SER SER ILE PHE LEU GLU
SEQRES 5 B 730 ASN SER THR PHE GLU ILE PHE GLY ASP SER ILE SER ASP
SEQRES 6 B 730 TYR SER VAL SER PRO ASP ARG LEU PHE VAL LEU LEU GLU
SEQRES 7 B 730 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 B 730 SER TYR SER ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 B 730 THR GLU GLU LYS ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 10 B 730 TRP SER GLN GLU GLY HIS LYS LEU ALA TYR VAL TRP LYS
SEQRES 11 B 730 ASN ASP ILE TYR VAL LYS ILE GLU PRO HIS LEU PRO SER
SEQRES 12 B 730 HIS ARG ILE THR SER THR GLY LYS GLU ASN VAL ILE PHE
SEQRES 13 B 730 ASN GLY ILE ASN ASP TRP VAL TYR GLU GLU GLU ILE PHE
SEQRES 14 B 730 GLY ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 B 730 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLY VAL PRO
SEQRES 16 B 730 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 B 730 TYR PRO LYS THR VAL TRP ILE PRO TYR PRO LYS ALA GLY
SEQRES 18 B 730 ALA VAL ASN PRO THR VAL LYS PHE PHE ILE VAL ASN THR
SEQRES 19 B 730 ASP SER LEU SER SER THR THR THR THR ILE PRO MET GLN
SEQRES 20 B 730 ILE THR ALA PRO ALA SER VAL THR THR GLY ASP HIS TYR
SEQRES 21 B 730 LEU CYS ASP VAL ALA TRP VAL SER GLU ASP ARG ILE SER
SEQRES 22 B 730 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 B 730 ALA ILE CYS ASP TYR ASP LYS THR THR LEU VAL TRP ASN
SEQRES 24 B 730 CYS PRO THR THR GLN GLU HIS ILE GLU THR SER ALA THR
SEQRES 25 B 730 GLY TRP CYS GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE
SEQRES 26 B 730 THR SER ASP GLY SER SER PHE TYR LYS ILE VAL SER ASP
SEQRES 27 B 730 LYS ASP GLY TYR LYS HIS ILE CYS GLN PHE GLN LYS ASP
SEQRES 28 B 730 ARG LYS PRO GLU GLN VAL CYS THR PHE ILE THR LYS GLY
SEQRES 29 B 730 ALA TRP GLU VAL ILE SER ILE GLU ALA LEU THR SER ASP
SEQRES 30 B 730 TYR LEU TYR TYR ILE SER ASN GLU TYR LYS GLU MET PRO
SEQRES 31 B 730 GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU THR ASP HIS
SEQRES 32 B 730 THR ASN LYS LYS CYS LEU SER CYS ASP LEU ASN PRO GLU
SEQRES 33 B 730 ARG CYS GLN TYR TYR SER VAL SER LEU SER LYS GLU ALA
SEQRES 34 B 730 LYS TYR TYR GLN LEU GLY CYS ARG GLY PRO GLY LEU PRO
SEQRES 35 B 730 LEU TYR THR LEU HIS ARG SER THR ASP GLN LYS GLU LEU
SEQRES 36 B 730 ARG VAL LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU
SEQRES 37 B 730 GLN ASP VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE
SEQRES 38 B 730 VAL LEU ASN GLU THR ARG PHE TRP TYR GLN MET ILE LEU
SEQRES 39 B 730 PRO PRO HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU
SEQRES 40 B 730 ILE ASP VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP
SEQRES 41 B 730 ALA ALA PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER
SEQRES 42 B 730 THR GLU ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY
SEQRES 43 B 730 SER GLY TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN
SEQRES 44 B 730 LYS ARG LEU GLY THR LEU GLU VAL GLU ASP GLN ILE GLU
SEQRES 45 B 730 ALA ALA ARG GLN PHE LEU LYS MET GLY PHE VAL ASP SER
SEQRES 46 B 730 LYS ARG VAL ALA ILE TRP GLY TRP SER TYR GLY GLY TYR
SEQRES 47 B 730 VAL THR SER MET VAL LEU GLY SER GLY SER GLY VAL PHE
SEQRES 48 B 730 LYS CYS GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU
SEQRES 49 B 730 TYR TYR ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU
SEQRES 50 B 730 PRO THR PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER
SEQRES 51 B 730 THR VAL MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU
SEQRES 52 B 730 TYR LEU LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS
SEQRES 53 B 730 PHE GLN GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP
SEQRES 54 B 730 ALA GLY VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU
SEQRES 55 B 730 ASP HIS GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE
SEQRES 56 B 730 TYR SER HIS MET SER HIS PHE LEU GLN GLN CYS PHE SER
SEQRES 57 B 730 LEU ARG
HET SO4 900 5
HET 1AD A 768 19
HETNAM SO4 SULFATE ION
HETNAM 1AD (1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-PROP-1-YN-1-
HETNAM 2 1AD YLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINE
FORMUL 3 SO4 O4 S1 2-
FORMUL 4 1AD C15 H25 N3 O1
HELIX 1 1 THR A 42 LYS A 48 1 7
HELIX 2 2 SER A 91 ILE A 95 5 5
HELIX 3 3 ASP A 198 ILE A 205 1 8
HELIX 4 4 PRO A 216 GLY A 218 5 3
HELIX 5 5 ASP A 272 THR A 277 5 6
HELIX 6 6 PRO A 288 THR A 293 1 6
HELIX 7 7 PRO A 338 GLU A 342 5 5
HELIX 8 8 GLU A 422 MET A 426 5 5
HELIX 9 9 ASN A 498 LEU A 505 1 8
HELIX 10 10 GLN A 506 VAL A 508 5 3
HELIX 11 11 ASN A 563 ASN A 573 1 11
HELIX 12 12 GLY A 588 HIS A 593 1 6
HELIX 13 13 ALA A 594 ASN A 596 5 3
HELIX 14 14 THR A 601 MET A 617 1 17
HELIX 15 15 SER A 631 GLY A 642 1 12
HELIX 16 16 ASP A 664 GLY A 673 1 10
HELIX 17 17 ASN A 680 SER A 687 1 8
HELIX 18 18 VAL A 689 VAL A 699 5 11
HELIX 19 19 PHE A 714 ALA A 727 1 14
HELIX 20 20 SER A 745 PHE A 764 1 20
HELIX 21 21 THR B 42 LYS B 48 1 7
HELIX 22 22 SER B 91 ILE B 95 5 5
HELIX 23 23 ASP B 198 ILE B 205 1 8
HELIX 24 24 PRO B 216 GLY B 218 5 3
HELIX 25 25 ASP B 272 THR B 277 5 6
HELIX 26 26 PRO B 288 THR B 293 1 6
HELIX 27 27 PRO B 338 GLU B 342 5 5
HELIX 28 28 GLU B 422 MET B 426 5 5
HELIX 29 29 ASN B 498 LEU B 505 1 8
HELIX 30 30 GLN B 506 VAL B 508 5 3
HELIX 31 31 ASN B 563 ASN B 573 1 11
HELIX 32 32 GLY B 588 HIS B 593 1 6
HELIX 33 33 ALA B 594 ASN B 596 5 3
HELIX 34 34 THR B 601 MET B 617 1 17
HELIX 35 35 SER B 631 GLY B 642 1 12
HELIX 36 36 ARG B 659 TYR B 663 5 5
HELIX 37 37 ASP B 664 GLY B 673 1 10
HELIX 38 38 ASN B 680 SER B 687 1 8
HELIX 39 39 VAL B 689 VAL B 699 5 11
HELIX 40 40 PHE B 714 ALA B 727 1 14
HELIX 41 41 SER B 745 PHE B 764 1 20
SHEET 1 A 4 ARG A 59 TRP A 60 0
SHEET 2 A 4 GLU A 65 LYS A 69 -1 O LEU A 67 N ARG A 59
SHEET 3 A 4 ILE A 74 ASN A 78 -1 O LEU A 75 N TYR A 68
SHEET 4 A 4 ILE A 86 LEU A 88 -1 O PHE A 87 N ILE A 74
SHEET 1 B 4 ILE A 100 VAL A 105 0
SHEET 2 B 4 PHE A 111 LYS A 120 -1 O LEU A 113 N SER A 104
SHEET 3 B 4 TYR A 126 ASP A 134 -1 O SER A 129 N TYR A 116
SHEET 4 B 4 GLN A 139 LEU A 140 -1 O GLN A 139 N ASP A 134
SHEET 1 C 4 TRP A 152 TRP A 155 0
SHEET 2 C 4 LEU A 162 TRP A 166 -1 O VAL A 165 N TRP A 152
SHEET 3 C 4 ASP A 169 LYS A 173 -1 O TYR A 171 N TYR A 164
SHEET 4 C 4 HIS A 181 ARG A 182 -1 O HIS A 181 N VAL A 172
SHEET 1 D 3 ILE A 192 ASN A 194 0
SHEET 2 D 3 PHE A 220 ASN A 227 -1 O PHE A 226 N PHE A 193
SHEET 3 D 3 LEU A 212 TRP A 214 -1 N TRP A 213 O ALA A 222
SHEET 1 E 4 ILE A 192 ASN A 194 0
SHEET 2 E 4 PHE A 220 ASN A 227 -1 O PHE A 226 N PHE A 193
SHEET 3 E 4 THR A 263 ASN A 270 -1 O PHE A 267 N TYR A 223
SHEET 4 E 4 MET A 283 ILE A 285 -1 O ILE A 285 N PHE A 266
SHEET 1 F 2 LEU A 233 PHE A 238 0
SHEET 2 F 2 LYS A 248 PRO A 253 -1 O VAL A 250 N TYR A 236
SHEET 1 G 4 HIS A 296 SER A 305 0
SHEET 2 G 4 ARG A 308 ARG A 315 -1 O LEU A 314 N TYR A 297
SHEET 3 G 4 TYR A 320 ASP A 329 -1 O VAL A 322 N TRP A 313
SHEET 4 G 4 VAL A 334 ASN A 336 -1 O VAL A 334 N ASP A 329
SHEET 1 H 4 HIS A 296 SER A 305 0
SHEET 2 H 4 ARG A 308 ARG A 315 -1 O LEU A 314 N TYR A 297
SHEET 3 H 4 TYR A 320 ASP A 329 -1 O VAL A 322 N TRP A 313
SHEET 4 H 4 ILE A 344 THR A 346 -1 O GLU A 345 N SER A 321
SHEET 1 I 4 HIS A 361 PHE A 362 0
SHEET 2 I 4 SER A 368 SER A 374 -1 O TYR A 370 N HIS A 361
SHEET 3 I 4 LYS A 380 GLN A 386 -1 O HIS A 381 N VAL A 373
SHEET 4 I 4 THR A 396 PHE A 397 -1 O THR A 396 N GLN A 384
SHEET 1 J 4 VAL A 405 LEU A 411 0
SHEET 2 J 4 TYR A 415 SER A 420 -1 O ILE A 419 N ILE A 406
SHEET 3 J 4 ASN A 431 GLN A 436 -1 O TYR A 433 N TYR A 418
SHEET 4 J 4 ASP A 439 LYS A 443 -1 O ASN A 442 N GLN A 436
SHEET 1 K 4 TYR A 458 LEU A 462 0
SHEET 2 K 4 TYR A 468 CYS A 473 -1 O GLY A 472 N SER A 459
SHEET 3 K 4 LEU A 480 ARG A 485 -1 O THR A 482 N LEU A 471
SHEET 4 K 4 GLU A 491 ASP A 497 -1 O GLU A 496 N TYR A 481
SHEET 1 L 8 SER A 512 LEU A 520 0
SHEET 2 L 8 THR A 523 LEU A 531 -1 O TYR A 527 N ASP A 516
SHEET 3 L 8 ILE A 575 PHE A 579 -1 O VAL A 576 N ILE A 530
SHEET 4 L 8 TYR A 541 VAL A 547 1 N LEU A 544 O ILE A 575
SHEET 5 L 8 VAL A 620 TRP A 630 1 O ASP A 621 N TYR A 541
SHEET 6 L 8 CYS A 650 VAL A 654 1 O VAL A 654 N GLY A 629
SHEET 7 L 8 GLU A 700 GLY A 706 1 O ILE A 704 N ALA A 653
SHEET 8 L 8 GLN A 732 TYR A 736 1 O GLN A 732 N TYR A 701
SHEET 1 M 4 ARG B 59 TRP B 60 0
SHEET 2 M 4 GLU B 65 LYS B 69 -1 O LEU B 67 N ARG B 59
SHEET 3 M 4 ILE B 74 ASN B 78 -1 O LEU B 75 N TYR B 68
SHEET 4 M 4 ILE B 86 LEU B 88 -1 O PHE B 87 N ILE B 74
SHEET 1 N 4 ILE B 100 VAL B 105 0
SHEET 2 N 4 PHE B 111 LYS B 120 -1 O LEU B 113 N SER B 104
SHEET 3 N 4 TYR B 126 ASP B 134 -1 O SER B 129 N TYR B 116
SHEET 4 N 4 GLN B 139 LEU B 140 -1 O GLN B 139 N ASP B 134
SHEET 1 O 4 TRP B 152 TRP B 155 0
SHEET 2 O 4 LEU B 162 TRP B 166 -1 O VAL B 165 N TRP B 152
SHEET 3 O 4 ASP B 169 LYS B 173 -1 O TYR B 171 N TYR B 164
SHEET 4 O 4 HIS B 181 ARG B 182 -1 O HIS B 181 N VAL B 172
SHEET 1 P 3 ILE B 192 ASN B 194 0
SHEET 2 P 3 PHE B 220 ASN B 227 -1 O PHE B 226 N PHE B 193
SHEET 3 P 3 LEU B 212 TRP B 214 -1 N TRP B 213 O ALA B 222
SHEET 1 Q 4 ILE B 192 ASN B 194 0
SHEET 2 Q 4 PHE B 220 ASN B 227 -1 O PHE B 226 N PHE B 193
SHEET 3 Q 4 THR B 263 ASN B 270 -1 O PHE B 267 N TYR B 223
SHEET 4 Q 4 MET B 283 ILE B 285 -1 O ILE B 285 N PHE B 266
SHEET 1 R 2 LEU B 233 PHE B 238 0
SHEET 2 R 2 LYS B 248 PRO B 253 -1 O VAL B 250 N TYR B 236
SHEET 1 S 4 HIS B 296 SER B 305 0
SHEET 2 S 4 ARG B 308 ARG B 315 -1 O LEU B 314 N TYR B 297
SHEET 3 S 4 TYR B 320 ASP B 329 -1 O VAL B 322 N TRP B 313
SHEET 4 S 4 VAL B 334 ASN B 336 -1 O VAL B 334 N ASP B 329
SHEET 1 T 4 HIS B 296 SER B 305 0
SHEET 2 T 4 ARG B 308 ARG B 315 -1 O LEU B 314 N TYR B 297
SHEET 3 T 4 TYR B 320 ASP B 329 -1 O VAL B 322 N TRP B 313
SHEET 4 T 4 ILE B 344 THR B 346 -1 O GLU B 345 N SER B 321
SHEET 1 U 4 HIS B 361 PHE B 362 0
SHEET 2 U 4 SER B 368 SER B 374 -1 O TYR B 370 N HIS B 361
SHEET 3 U 4 LYS B 380 GLN B 386 -1 O HIS B 381 N VAL B 373
SHEET 4 U 4 THR B 396 PHE B 397 -1 O THR B 396 N GLN B 384
SHEET 1 V 3 VAL B 405 LEU B 411 0
SHEET 2 V 3 TYR B 415 SER B 420 -1 O ILE B 419 N ILE B 406
SHEET 3 V 3 ASN B 431 GLN B 436 -1 O TYR B 433 N TYR B 418
SHEET 1 W 4 TYR B 458 LEU B 462 0
SHEET 2 W 4 TYR B 468 CYS B 473 -1 O GLY B 472 N SER B 459
SHEET 3 W 4 LEU B 480 ARG B 485 -1 O THR B 482 N LEU B 471
SHEET 4 W 4 GLU B 491 ASP B 497 -1 O GLU B 496 N TYR B 481
SHEET 1 X 8 SER B 512 LEU B 520 0
SHEET 2 X 8 THR B 523 LEU B 531 -1 O TYR B 527 N ASP B 516
SHEET 3 X 8 ILE B 575 PHE B 579 -1 O VAL B 576 N ILE B 530
SHEET 4 X 8 TYR B 541 VAL B 547 1 N LEU B 544 O ILE B 575
SHEET 5 X 8 VAL B 620 TRP B 630 1 O ASP B 621 N TYR B 541
SHEET 6 X 8 CYS B 650 VAL B 654 1 O VAL B 654 N GLY B 629
SHEET 7 X 8 GLU B 700 GLY B 706 1 O ILE B 704 N ALA B 653
SHEET 8 X 8 GLN B 732 TYR B 736 1 O GLN B 732 N TYR B 701
SSBOND 1 CYS A 326 CYS A 337
SSBOND 2 CYS A 383 CYS A 395
SSBOND 3 CYS A 445 CYS A 448
SSBOND 4 CYS A 455 CYS A 473
SSBOND 5 CYS A 650 CYS A 763
SSBOND 6 CYS B 326 CYS B 337
SSBOND 7 CYS B 383 CYS B 395
SSBOND 8 CYS B 445 CYS B 448
SSBOND 9 CYS B 455 CYS B 473
SSBOND 10 CYS B 650 CYS B 763
LINK OG SER A 631 C8 1AD A 768
CRYST1 207.500 207.500 207.500 90.00 90.00 90.00 P 21 3 24
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 0.004819 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004819 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004819 0.00000
TER 5921 ARG A 767
TER 11842 ARG B 767
MASTER 389 0 2 41 97 0 0 611864 2 45 114
END |