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HEADER HYDROLASE 30-DEC-02 1J2E
TITLE CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 33-772;
COMPND 5 SYNONYM: DPP IV;
COMPND 6 EC: 3.4.14.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PACGP67-B
KEYWDS SERINE PROTEASE, DIPEPTIDYL PEPTIDASE IV, CD26, PROLYL
KEYWDS 2 OLIGOPEPTIDASE, BETA-PROPELLER STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HIRAMATSU,K.KYONO,Y.HIGASHIYAMA,C.FUKUSHIMA,H.SHIMA,
AUTHOR 2 S.SUGIYAMA,K.INAKA,A.YAMAMOTO,R.SHIMIZU
REVDAT 1 30-DEC-03 1J2E 0
JRNL AUTH H.HIRAMATSU,K.KYONO,Y.HIGASHIYAMA,C.FUKUSHIMA,
JRNL AUTH 2 H.SHIMA,S.SUGIYAMA,K.INAKA,A.YAMAMOTO,R.SHIMIZU
JRNL TITL THE STRUCTURE AND FUNCTION OF HUMAN DIPEPTIDYL
JRNL TITL 2 PEPTIDASE IV, POSSESSING A UNIQUE EIGHT-BLADED
JRNL TITL 3 BETA-PROPELLER FOLD
JRNL REF BIOCHEM.BIOPHYS.RES.COMM. V. 302 849 2003
JRNL REFN ASTM BBRCA9 US ISSN 0006-291X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 58751
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 SET) : 0.249
REMARK 3 FREE R VALUE : 0.302
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5926
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6749
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 746
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11942
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 140
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.78000
REMARK 3 B22 (A**2) : 4.13000
REMARK 3 B33 (A**2) : 0.65000
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) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.71
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J2E COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JAN-2003.
REMARK 100 THE RCSB ID CODE IS RCSB005544.
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 : 9.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58751
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.21300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG4000, 0.18M SODIUM ACETATE,
REMARK 280 0.18M GLY-NAOH, PH 9.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.0K
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 59.02000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.42000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.96000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.42000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.02000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.96000
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 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 33
REMARK 465 ASP A 34
REMARK 465 ALA A 35
REMARK 465 THR A 36
REMARK 465 ALA A 37
REMARK 465 HIS A 767
REMARK 465 HIS A 768
REMARK 465 HIS A 769
REMARK 465 HIS A 770
REMARK 465 HIS A 771
REMARK 465 HIS A 772
REMARK 465 ASP B 33
REMARK 465 ASP B 34
REMARK 465 ALA B 35
REMARK 465 THR B 36
REMARK 465 ALA B 37
REMARK 465 HIS B 767
REMARK 465 HIS B 768
REMARK 465 HIS B 769
REMARK 465 HIS B 770
REMARK 465 HIS B 771
REMARK 465 HIS B 772
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 B 528 SD MET B 528 CE -0.048
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 ASN A 80 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 GLY A 220 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 ILE A 236 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 PHE A 240 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 PRO A 255 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ILE A 287 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 LEU A 300 N - CA - C ANGL. DEV. =-14.0 DEGREES
REMARK 500 ILE A 319 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLN A 320 N - CA - C ANGL. DEV. = 11.3 DEGREES
REMARK 500 THR A 365 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 GLN A 388 N - CA - C ANGL. DEV. =-13.3 DEGREES
REMARK 500 PRO A 451 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 SER A 458 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ILE A 517 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 ILE A 529 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 PRO A 541 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 VAL A 546 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 TYR A 547 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 GLY A 584 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 GLY A 617 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 VAL A 656 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 GLU A 699 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 VAL A 711 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 ASN B 80 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 SER B 131 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 SER B 158 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 ALA B 165 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ASP B 200 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 SER B 217 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ILE B 236 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 PHE B 240 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 LEU B 300 N - CA - C ANGL. DEV. =-14.1 DEGREES
REMARK 500 ILE B 319 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 GLN B 320 N - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 GLN B 388 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 TRP B 402 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 SER B 458 N - CA - C ANGL. DEV. =-14.1 DEGREES
REMARK 500 ILE B 517 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ILE B 529 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 PRO B 541 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 VAL B 656 N - CA - C ANGL. DEV. =-13.2 DEGREES
REMARK 500 TRP B 659 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 VAL B 711 N - CA - C ANGL. DEV. = -9.1 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 B 630 -115.81 62.11
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 88 DISTANCE = 5.31 ANGSTROMS
DBREF 1J2E A 33 766 SWS P27487 DPP4_HUMAN 33 766
DBREF 1J2E B 33 766 SWS P27487 DPP4_HUMAN 33 766
SEQADV 1J2E HIS A 767 SWS P27487 HIS TAG
SEQADV 1J2E HIS A 768 SWS P27487 HIS TAG
SEQADV 1J2E HIS A 769 SWS P27487 HIS TAG
SEQADV 1J2E HIS A 770 SWS P27487 HIS TAG
SEQADV 1J2E HIS A 771 SWS P27487 HIS TAG
SEQADV 1J2E HIS A 772 SWS P27487 HIS TAG
SEQADV 1J2E HIS B 767 SWS P27487 HIS TAG
SEQADV 1J2E HIS B 768 SWS P27487 HIS TAG
SEQADV 1J2E HIS B 769 SWS P27487 HIS TAG
SEQADV 1J2E HIS B 770 SWS P27487 HIS TAG
SEQADV 1J2E HIS B 771 SWS P27487 HIS TAG
SEQADV 1J2E HIS B 772 SWS P27487 HIS TAG
SEQRES 1 A 740 ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR THR LEU
SEQRES 2 A 740 THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR
SEQRES 3 A 740 SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS
SEQRES 4 A 740 GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY
SEQRES 5 A 740 ASN SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU
SEQRES 6 A 740 PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP
SEQRES 7 A 740 GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN
SEQRES 8 A 740 TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP
SEQRES 9 A 740 LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO
SEQRES 10 A 740 ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS
SEQRES 11 A 740 LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS
SEQRES 12 A 740 ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR
SEQRES 13 A 740 GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP
SEQRES 14 A 740 VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU
SEQRES 15 A 740 TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN
SEQRES 16 A 740 PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE
SEQRES 17 A 740 TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG
SEQRES 18 A 740 VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL
SEQRES 19 A 740 LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL
SEQRES 20 A 740 THR ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER
SEQRES 21 A 740 MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP
SEQRES 22 A 740 ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG
SEQRES 23 A 740 ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP
SEQRES 24 A 740 GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN
SEQRES 25 A 740 HIS ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE
SEQRES 26 A 740 ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER
SEQRES 27 A 740 PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS
SEQRES 28 A 740 ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE
SEQRES 29 A 740 ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA
SEQRES 30 A 740 LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR
SEQRES 31 A 740 LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN
SEQRES 32 A 740 LEU SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU
SEQRES 33 A 740 LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE
SEQRES 34 A 740 SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY
SEQRES 35 A 740 PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN
SEQRES 36 A 740 ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU
SEQRES 37 A 740 ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS
SEQRES 38 A 740 LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR
SEQRES 39 A 740 GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS
SEQRES 40 A 740 TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER
SEQRES 41 A 740 GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR
SEQRES 42 A 740 TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE
SEQRES 43 A 740 ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET
SEQRES 44 A 740 HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU
SEQRES 45 A 740 ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY
SEQRES 46 A 740 PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER
SEQRES 47 A 740 TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY
SEQRES 48 A 740 SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL
SEQRES 49 A 740 SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG
SEQRES 50 A 740 TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS
SEQRES 51 A 740 TYR ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE
SEQRES 52 A 740 LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP
SEQRES 53 A 740 ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS
SEQRES 54 A 740 ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP
SEQRES 55 A 740 TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA
SEQRES 56 A 740 HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS
SEQRES 57 A 740 GLN CYS PHE SER LEU PRO HIS HIS HIS HIS HIS HIS
SEQRES 1 B 740 ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR THR LEU
SEQRES 2 B 740 THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR
SEQRES 3 B 740 SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS
SEQRES 4 B 740 GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY
SEQRES 5 B 740 ASN SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU
SEQRES 6 B 740 PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP
SEQRES 7 B 740 GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN
SEQRES 8 B 740 TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP
SEQRES 9 B 740 LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO
SEQRES 10 B 740 ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS
SEQRES 11 B 740 LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS
SEQRES 12 B 740 ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR
SEQRES 13 B 740 GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP
SEQRES 14 B 740 VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU
SEQRES 15 B 740 TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN
SEQRES 16 B 740 PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE
SEQRES 17 B 740 TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG
SEQRES 18 B 740 VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL
SEQRES 19 B 740 LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL
SEQRES 20 B 740 THR ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER
SEQRES 21 B 740 MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP
SEQRES 22 B 740 ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG
SEQRES 23 B 740 ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP
SEQRES 24 B 740 GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN
SEQRES 25 B 740 HIS ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE
SEQRES 26 B 740 ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER
SEQRES 27 B 740 PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS
SEQRES 28 B 740 ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE
SEQRES 29 B 740 ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA
SEQRES 30 B 740 LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR
SEQRES 31 B 740 LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN
SEQRES 32 B 740 LEU SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU
SEQRES 33 B 740 LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE
SEQRES 34 B 740 SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY
SEQRES 35 B 740 PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN
SEQRES 36 B 740 ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU
SEQRES 37 B 740 ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS
SEQRES 38 B 740 LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR
SEQRES 39 B 740 GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS
SEQRES 40 B 740 TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER
SEQRES 41 B 740 GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR
SEQRES 42 B 740 TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE
SEQRES 43 B 740 ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET
SEQRES 44 B 740 HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU
SEQRES 45 B 740 ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY
SEQRES 46 B 740 PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER
SEQRES 47 B 740 TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY
SEQRES 48 B 740 SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL
SEQRES 49 B 740 SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG
SEQRES 50 B 740 TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS
SEQRES 51 B 740 TYR ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE
SEQRES 52 B 740 LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP
SEQRES 53 B 740 ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS
SEQRES 54 B 740 ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP
SEQRES 55 B 740 TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA
SEQRES 56 B 740 HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS
SEQRES 57 B 740 GLN CYS PHE SER LEU PRO HIS HIS HIS HIS HIS HIS
MODRES 1J2E ASN A 85 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN A 219 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN A 229 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN A 281 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN A 321 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN B 85 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN B 219 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN B 229 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN B 281 ASN GLYCOSYLATION SITE
MODRES 1J2E ASN B 321 ASN GLYCOSYLATION SITE
HET NAG A 901 14
HET NAG A 902 14
HET NAG A 903 14
HET NAG A 904 14
HET NAG A 905 14
HET NAG B 906 14
HET NAG B 907 14
HET NAG B 908 14
HET NAG B 909 14
HET NAG B 910 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 NAG 10(C8 H15 N1 O6)
FORMUL 13 HOH *273(H2 O1)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 PHE A 95 GLY A 99 5 5
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 ASP A 274 LEU A 276 5 3
HELIX 5 5 PRO A 290 ILE A 295 1 6
HELIX 6 6 VAL A 341 GLN A 344 5 4
HELIX 7 7 GLU A 421 MET A 425 5 5
HELIX 8 8 ASN A 497 ASN A 506 1 10
HELIX 9 9 ASN A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 MET A 616 1 17
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 ARG A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 SER A 686 1 8
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 HIS A 712 VAL A 726 1 15
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 THR B 44 ASN B 51 1 8
HELIX 21 21 ASP B 200 VAL B 207 1 8
HELIX 22 22 ASP B 274 LEU B 276 5 3
HELIX 23 23 PRO B 290 ILE B 295 1 6
HELIX 24 24 LEU B 340 GLN B 344 5 5
HELIX 25 25 GLU B 421 MET B 425 5 5
HELIX 26 26 ASN B 497 GLN B 505 1 9
HELIX 27 27 ASN B 562 THR B 570 1 9
HELIX 28 28 GLY B 587 HIS B 592 1 6
HELIX 29 29 ALA B 593 ASN B 595 5 3
HELIX 30 30 THR B 600 SER B 614 1 15
HELIX 31 31 SER B 630 GLY B 641 1 12
HELIX 32 32 ARG B 658 TYR B 662 5 5
HELIX 33 33 ASP B 663 GLY B 672 1 10
HELIX 34 34 ASN B 679 SER B 686 1 8
HELIX 35 35 VAL B 688 LYS B 696 5 9
HELIX 36 36 HIS B 712 VAL B 726 1 15
HELIX 37 37 SER B 744 SER B 764 1 21
SHEET 1 A 4 ARG A 61 TRP A 62 0
SHEET 2 A 4 GLU A 67 LYS A 71 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ILE A 76 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 ASP A 104 ILE A 107 0
SHEET 2 B 4 ILE A 114 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 TRP A 154 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 4 ILE A 285 GLN A 286 0
SHEET 2 D 4 THR A 265 ASN A 272 -1 N VAL A 270 O ILE A 285
SHEET 3 D 4 PHE A 222 ASN A 229 -1 N LEU A 223 O VAL A 271
SHEET 4 D 4 ILE A 194 ASN A 196 -1 N TYR A 195 O PHE A 228
SHEET 1 E 4 ILE A 285 GLN A 286 0
SHEET 2 E 4 THR A 265 ASN A 272 -1 N VAL A 270 O ILE A 285
SHEET 3 E 4 PHE A 222 ASN A 229 -1 N LEU A 223 O VAL A 271
SHEET 4 E 4 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
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 TRP A 305 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 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 G 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 H 4 HIS A 298 TRP A 305 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 ASP A 326 N LEU A 313
SHEET 4 H 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 I 4 HIS A 363 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 ALA A 409
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 THR A 443 N LYS A 433
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 THR A 481 N LEU A 470
SHEET 4 K 4 LYS A 489 GLU A 495 -1 O GLU A 495 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 PHE A 524 N ILE A 517
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
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 ALA A 625 N LEU A 542
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 LEU A 701 N ALA A 652
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 M 4 LEU B 60 TRP B 62 0
SHEET 2 M 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 M 4 ILE B 76 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 M 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 N 4 ILE B 102 ASP B 104 0
SHEET 2 N 4 PHE B 113 LYS B 122 -1 O GLU B 117 N ASP B 104
SHEET 3 N 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 N 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 O 4 THR B 152 TRP B 157 0
SHEET 2 O 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 O 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 O 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 P 4 SER B 284 GLN B 286 0
SHEET 2 P 4 THR B 265 ASN B 272 -1 N VAL B 270 O ILE B 285
SHEET 3 P 4 PHE B 222 ASN B 229 -1 N LEU B 223 O VAL B 271
SHEET 4 P 4 ILE B 194 ASN B 196 -1 N TYR B 195 O PHE B 228
SHEET 1 Q 4 SER B 284 GLN B 286 0
SHEET 2 Q 4 THR B 265 ASN B 272 -1 N VAL B 270 O ILE B 285
SHEET 3 Q 4 PHE B 222 ASN B 229 -1 N LEU B 223 O VAL B 271
SHEET 4 Q 4 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 R 2 LEU B 235 PHE B 240 0
SHEET 2 R 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 S 4 HIS B 298 TRP B 305 0
SHEET 2 S 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 S 4 TYR B 322 TYR B 330 -1 O CYS B 328 N ILE B 311
SHEET 4 S 4 TRP B 337 ASN B 338 -1 O ASN B 338 N ASP B 329
SHEET 1 T 4 HIS B 298 TRP B 305 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 T 4 TYR B 322 TYR B 330 -1 O CYS B 328 N ILE B 311
SHEET 4 T 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 U 4 HIS B 363 PHE B 364 0
SHEET 2 U 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 U 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 U 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 V 4 VAL B 404 LEU B 410 0
SHEET 2 V 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 V 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 V 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 W 4 TYR B 457 PHE B 461 0
SHEET 2 W 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 W 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 W 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 X 8 SER B 511 LEU B 519 0
SHEET 2 X 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 X 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 X 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 X 8 VAL B 619 TRP B 629 1 O TRP B 627 N VAL B 546
SHEET 6 X 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 X 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 X 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
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 C1 NAG A 901 ND2 ASN A 85
LINK C1 NAG A 902 ND2 ASN A 219
LINK C1 NAG A 903 ND2 ASN A 229
LINK C1 NAG A 904 ND2 ASN A 281
LINK C1 NAG A 905 ND2 ASN A 321
LINK C1 NAG B 906 ND2 ASN B 85
LINK C1 NAG B 907 ND2 ASN B 219
LINK C1 NAG B 908 ND2 ASN B 229
LINK C1 NAG B 909 ND2 ASN B 281
LINK C1 NAG B 910 ND2 ASN B 321
CISPEP 1 GLY A 474 PRO A 475 0 0.29
CISPEP 2 GLY B 474 PRO B 475 0 0.35
CRYST1 118.040 125.920 136.840 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 0.008472 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007942 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007308 0.00000
TER 5972 PRO A 766
TER 11944 PRO B 766
MASTER 334 0 10 37 100 0 0 612355 2 170 114
END |