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HEADER HYDROLASE 01-AUG-07 2QT9
TITLE HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN COMPLEX WITH A 4-ARYL
TITLE 2 CYCLOHEXYLALANINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL
COMPND 5 ACTIVATION ANTIGEN CD26, TP103, ADENOSINE DEAMINASE
COMPND 6 COMPLEXING PROTEIN 2, ADABP;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DPP4, ADCP2, CD26;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBLUEBAC4.5
KEYWDS ALPHA/BETA, BETA-PROPELLER, DIMER, AMINOPEPTIDASE,
KEYWDS 2 GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE, SECRETED,
KEYWDS 3 SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SCAPIN
REVDAT 1 06-NOV-07 2QT9 0
JRNL AUTH D.E.KAELIN,A.L.SMENTON,G.J.EIERMANN,H.HE,B.LEITING,
JRNL AUTH 2 K.A.LYONS,R.A.PATEL,S.B.PATEL,A.PETROV,G.SCAPIN,
JRNL AUTH 3 J.K.WU,N.A.THORNBERRY,A.E.WEBER,J.L.DUFFY
JRNL TITL 4-ARYLCYCLOHEXYLALANINE ANALOGS AS POTENT,
JRNL TITL 2 SELECTIVE, AND ORALLY ACTIVE INHIBITORS OF
JRNL TITL 3 DIPEPTIDYL PEPTIDASE IV.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 5806 2007
JRNL REFN ASTM BMCLE8 UK ISSN 0960-894X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 118967
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6004
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11123
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 598
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 399
REMARK 3 SOLVENT ATOMS : 1304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.56200
REMARK 3 B22 (A**2) : -3.14800
REMARK 3 B33 (A**2) : -2.41400
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.48
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.86
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) : 0.920 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.410 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.440 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.100 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : MASK
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 40.10
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
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 2QT9 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB044026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17IDB
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
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119087
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.44200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: 1X70
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, SODIUM ACETATE, TRIS, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, PH
REMARK 280 8.000000, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 58.84850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.48500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.03600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.48500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.84850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.03600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300
REMARK 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 10880 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, M, N, O, P, Q, R,
REMARK 350 S, T
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 TRP A 5
REMARK 465 LYS A 6
REMARK 465 VAL A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 LEU A 12
REMARK 465 GLY A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 VAL A 18
REMARK 465 THR A 19
REMARK 465 ILE A 20
REMARK 465 ILE A 21
REMARK 465 THR A 22
REMARK 465 VAL A 23
REMARK 465 PRO A 24
REMARK 465 VAL A 25
REMARK 465 VAL A 26
REMARK 465 LEU A 27
REMARK 465 LEU A 28
REMARK 465 ASN A 29
REMARK 465 LYS A 30
REMARK 465 GLY A 31
REMARK 465 THR A 32
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 ASP A 38
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 THR B 3
REMARK 465 PRO B 4
REMARK 465 TRP B 5
REMARK 465 LYS B 6
REMARK 465 VAL B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 LEU B 12
REMARK 465 GLY B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 VAL B 18
REMARK 465 THR B 19
REMARK 465 ILE B 20
REMARK 465 ILE B 21
REMARK 465 THR B 22
REMARK 465 VAL B 23
REMARK 465 PRO B 24
REMARK 465 VAL B 25
REMARK 465 VAL B 26
REMARK 465 LEU B 27
REMARK 465 LEU B 28
REMARK 465 ASN B 29
REMARK 465 LYS B 30
REMARK 465 GLY B 31
REMARK 465 THR B 32
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 ASP B 38
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 58 80.52 -152.18
REMARK 500 SER A 64 -166.77 -164.17
REMARK 500 GLN A 123 -104.77 -114.90
REMARK 500 TRP A 124 -146.46 -87.97
REMARK 500 HIS A 162 31.84 -148.41
REMARK 500 ILE A 193 -61.98 -128.75
REMARK 500 VAL A 207 -61.79 -99.80
REMARK 500 SER A 242 -166.14 62.97
REMARK 500 GLN A 320 44.26 -63.07
REMARK 500 ASN A 450 77.66 -164.36
REMARK 500 LYS A 536 -8.92 -58.38
REMARK 500 TYR A 547 -70.52 -126.95
REMARK 500 ARG A 597 52.33 -140.74
REMARK 500 THR A 600 -89.85 -120.96
REMARK 500 SER A 630 -122.99 63.19
REMARK 500 ASP A 678 -98.86 -107.91
REMARK 500 ASN A 710 -71.04 -90.69
REMARK 500 ASP A 739 -160.90 -100.61
REMARK 500 ILE A 742 52.78 34.78
REMARK 500 ASN B 74 -7.57 69.16
REMARK 500 SER B 106 118.23 -162.25
REMARK 500 GLN B 123 -99.33 -117.99
REMARK 500 TRP B 124 -141.68 -94.53
REMARK 500 ASN B 138 -76.79 -63.42
REMARK 500 LYS B 139 12.94 -69.89
REMARK 500 ARG B 140 55.84 36.59
REMARK 500 HIS B 162 35.64 -154.36
REMARK 500 ASP B 192 9.27 59.47
REMARK 500 ILE B 193 -60.59 -126.57
REMARK 500 SER B 242 -163.79 63.12
REMARK 500 GLN B 320 48.64 -65.67
REMARK 500 GLU B 332 -8.15 -59.56
REMARK 500 THR B 350 -89.22 -111.34
REMARK 500 ASP B 367 0.42 -69.47
REMARK 500 ASN B 377 -167.49 -79.97
REMARK 500 LYS B 423 26.46 49.36
REMARK 500 ASP B 438 91.71 -162.04
REMARK 500 ASN B 450 76.88 -159.15
REMARK 500 ARG B 492 163.58 176.36
REMARK 500 TYR B 547 -70.27 -131.79
REMARK 500 ARG B 596 8.32 57.16
REMARK 500 THR B 600 -93.83 -120.40
REMARK 500 SER B 630 -121.64 64.74
REMARK 500 ASP B 678 -93.76 -128.55
REMARK 500 ASN B 710 -72.66 -90.20
REMARK 500 ASP B 739 -157.74 -102.57
REMARK 500 ILE B 742 54.28 37.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 700 0.08 SIDE_CHAIN
REMARK 500 TYR B 700 0.07 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1521 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 490 O
REMARK 620 2 LEU A 491 O 82.9
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QTB RELATED DB: PDB
DBREF 2QT9 A 1 766 UNP P27487 DPP4_HUMAN 1 766
DBREF 2QT9 B 1 766 UNP P27487 DPP4_HUMAN 1 766
SEQADV 2QT9 THR A 39 UNP P27487 SER 39 ENGINEERED
SEQADV 2QT9 THR B 39 UNP P27487 SER 39 ENGINEERED
SEQRES 1 A 766 MET LYS THR PRO TRP LYS VAL LEU LEU GLY LEU LEU GLY
SEQRES 2 A 766 ALA ALA ALA LEU VAL THR ILE ILE THR VAL PRO VAL VAL
SEQRES 3 A 766 LEU LEU ASN LYS GLY THR ASP ASP ALA THR ALA ASP THR
SEQRES 4 A 766 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 5 A 766 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 6 A 766 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 7 A 766 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 8 A 766 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 9 A 766 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 10 A 766 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 11 A 766 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 12 A 766 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 13 A 766 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 14 A 766 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 15 A 766 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 16 A 766 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 17 A 766 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 18 A 766 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 19 A 766 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 20 A 766 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 21 A 766 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 22 A 766 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 23 A 766 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 24 A 766 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 25 A 766 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 26 A 766 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 27 A 766 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 28 A 766 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 29 A 766 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 30 A 766 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 31 A 766 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 32 A 766 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 33 A 766 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 34 A 766 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 35 A 766 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 36 A 766 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 37 A 766 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 38 A 766 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 39 A 766 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 40 A 766 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 41 A 766 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 42 A 766 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 43 A 766 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 44 A 766 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 45 A 766 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 46 A 766 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 47 A 766 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 48 A 766 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 49 A 766 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 50 A 766 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 51 A 766 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 52 A 766 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 53 A 766 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 54 A 766 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 55 A 766 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 56 A 766 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 57 A 766 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 58 A 766 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 59 A 766 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 766 MET LYS THR PRO TRP LYS VAL LEU LEU GLY LEU LEU GLY
SEQRES 2 B 766 ALA ALA ALA LEU VAL THR ILE ILE THR VAL PRO VAL VAL
SEQRES 3 B 766 LEU LEU ASN LYS GLY THR ASP ASP ALA THR ALA ASP THR
SEQRES 4 B 766 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 5 B 766 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 6 B 766 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 7 B 766 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 8 B 766 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 9 B 766 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 10 B 766 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 11 B 766 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 12 B 766 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 13 B 766 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 14 B 766 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 15 B 766 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 16 B 766 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 17 B 766 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 18 B 766 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 19 B 766 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 20 B 766 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 21 B 766 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 22 B 766 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 23 B 766 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 24 B 766 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 25 B 766 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 26 B 766 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 27 B 766 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 28 B 766 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 29 B 766 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 30 B 766 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 31 B 766 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 32 B 766 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 33 B 766 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 34 B 766 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 35 B 766 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 36 B 766 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 37 B 766 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 38 B 766 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 39 B 766 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 40 B 766 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 41 B 766 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 42 B 766 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 43 B 766 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 44 B 766 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 45 B 766 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 46 B 766 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 47 B 766 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 48 B 766 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 49 B 766 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 50 B 766 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 51 B 766 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 52 B 766 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 53 B 766 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 54 B 766 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 55 B 766 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 56 B 766 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 57 B 766 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 58 B 766 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 59 B 766 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
MODRES 2QT9 ASN A 85 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN A 92 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN A 150 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN A 219 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN A 229 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN A 281 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN A 321 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN A 520 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN B 85 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN B 92 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN B 150 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN B 219 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN B 229 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN B 281 ASN GLYCOSYLATION SITE
MODRES 2QT9 ASN B 321 ASN GLYCOSYLATION SITE
HET NAG L1085 14
HET NDG L1086 14
HET NAG A1092 14
HET NDG M1150 14
HET NAG M1151 14
HET NAG N1219 14
HET NAG N1220 14
HET NAG O1229 14
HET NDG O1230 14
HET NAG A1281 14
HET NDG P1321 14
HET NAG P1322 14
HET NAG A1520 14
HET NAG Q2085 14
HET NAG Q2086 14
HET NAG B2092 14
HET NAG B2150 14
HET NAG R2219 14
HET NAG R2220 14
HET NAG S2229 14
HET NAG S2230 14
HET NAG T2281 14
HET NAG T2282 14
HET NAG B2321 14
HET NA A1521 1
HET 524 A1522 31
HET 524 B2322 31
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM NA SODIUM ION
HETNAM 524 (2S,3S)-3-AMINO-4-[(3S)-3-FLUOROPYRROLIDIN-1-YL]-N,N-
HETNAM 2 524 DIMETHYL-4-OXO-2-(TRANS-4-[1,2,4]TRIAZOLO[1,5-
HETNAM 3 524 A]PYRIDIN-5-YLCYCLOHEXYL)BUTANAMIDE
HETSYN NAG NAG
HETSYN 524 5-(4-{(1S,2S)-2-AMMONIO-1-[(DIMETHYLAMINO)CARBONYL]-3-
HETSYN 2 524 [(3S)-3-FLUOROPYRROLIDIN-1-YL]-3-
HETSYN 3 524 OXOPROPYL}CYCLOHEXYL)[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-1-
HETSYN 4 524 IUM
FORMUL 3 NAG 20(C8 H15 N O6)
FORMUL 3 NDG 4(C8 H15 N O6)
FORMUL 18 NA NA 1+
FORMUL 19 524 2(C22 H31 F N6 O2)
FORMUL 21 HOH *1304(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 GLU A 206 1 7
HELIX 3 3 ASP A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 VAL A 341 GLN A 344 5 4
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 GLN A 505 1 9
HELIX 8 8 ASN A 562 THR A 570 1 9
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
HELIX 11 11 THR A 600 SER A 614 1 15
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 ARG A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 GLY A 672 1 10
HELIX 15 15 ASN A 679 SER A 686 1 8
HELIX 16 16 VAL A 688 VAL A 698 5 11
HELIX 17 17 HIS A 712 VAL A 726 1 15
HELIX 18 18 SER A 744 SER A 764 1 21
HELIX 19 19 THR B 44 ASN B 51 1 8
HELIX 20 20 ASP B 200 GLU B 206 1 7
HELIX 21 21 ASP B 274 LEU B 276 5 3
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 VAL B 341 GLN B 344 5 4
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 ASN B 497 GLN B 505 1 9
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 LYS B 615 1 16
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ARG B 658 TYR B 662 5 5
HELIX 32 32 ASP B 663 GLY B 672 1 10
HELIX 33 33 ASN B 679 SER B 686 1 8
HELIX 34 34 VAL B 688 VAL B 698 5 11
HELIX 35 35 HIS B 712 VAL B 726 1 15
HELIX 36 36 SER B 744 PHE B 763 1 20
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 LEU A 60 TRP A 62 0
SHEET 2 B 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ASN A 75 ASN A 80 -1 O ASN A 75 N GLN A 72
SHEET 4 B 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 C 4 ILE A 102 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
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 SER A 284 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
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 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 ARG A 336 CYS A 339 -1 O ARG A 336 N ASP A 331
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 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 I 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 L 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 L 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 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 ARG B 61 TRP B 62 0
SHEET 2 O 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 O 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 P 4 ASP B 104 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 ALA B 165 N THR B 156
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 GLN B 286 -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 CYS B 328 N ILE B 311
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 CYS B 328 N ILE B 311
SHEET 4 V 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
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 ILE B 418 N ILE B 405
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 THR B 481 N LEU B 470
SHEET 4 Y 4 LYS B 489 GLU B 495 -1 O LEU B 494 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 LEU B 530 N SER B 511
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 1555 1555 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.04
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.04
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.06
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
LINK ND2 ASN A 85 C1 NAG L1085 1555 1555 1.46
LINK ND2 ASN A 92 C1 NAG A1092 1555 1555 1.46
LINK ND2 ASN A 150 C1 NDG M1150 1555 1555 1.45
LINK ND2 ASN A 219 C1 NAG N1219 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG O1229 1555 1555 1.45
LINK ND2 ASN A 281 C1 NAG A1281 1555 1555 1.46
LINK ND2 ASN A 321 C1 NDG P1321 1555 1555 1.46
LINK O GLY A 490 NA NA A1521 1555 1555 2.43
LINK O LEU A 491 NA NA A1521 1555 1555 2.44
LINK ND2 ASN A 520 C1 NAG A1520 1555 1555 1.46
LINK ND2 ASN B 85 C1 NAG Q2085 1555 1555 1.45
LINK ND2 ASN B 92 C1 NAG B2092 1555 1555 1.45
LINK ND2 ASN B 150 C1 NAG B2150 1555 1555 1.46
LINK ND2 ASN B 219 C1 NAG R2219 1555 1555 1.45
LINK ND2 ASN B 229 C1 NAG S2229 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG T2281 1555 1555 1.45
LINK ND2 ASN B 321 C1 NAG B2321 1555 1555 1.44
LINK O4 NAG L1085 C1 NDG L1086 1555 1555 1.39
LINK O4 NDG M1150 C1 NAG M1151 1555 1555 1.39
LINK O4 NAG N1219 C1 NAG N1220 1555 1555 1.39
LINK O4 NAG O1229 C1 NDG O1230 1555 1555 1.38
LINK O4 NDG P1321 C1 NAG P1322 1555 1555 1.40
LINK O4 NAG Q2085 C1 NAG Q2086 1555 1555 1.39
LINK O4 NAG R2219 C1 NAG R2220 1555 1555 1.39
LINK O4 NAG S2229 C1 NAG S2230 1555 1555 1.39
LINK O4 NAG T2281 C1 NAG T2282 1555 1555 1.38
CISPEP 1 GLY A 474 PRO A 475 0 1.75
CISPEP 2 GLY B 474 PRO B 475 0 0.29
CRYST1 117.697 126.072 136.970 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 0.008496 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007932 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007301 0.00000
TER 5966 PRO A 766
TER 11932 PRO B 766
MASTER 404 0 27 36 102 0 0 613633 2 436 118
END |