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HEADER HYDROLASE/HYDROLASE INHIBITOR 29-AUG-16 5T4E
TITLE HUMAN DPP4 IN COMPLEX WITH LIGAND 19A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADABP,ADENOSINE DEAMINASE COMPLEXING PROTEIN 2,ADCP-2,
COMPND 5 DIPEPTIDYL PEPTIDASE IV,DPP IV,T-CELL ACTIVATION ANTIGEN CD26,TP103;
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 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS STRUCTURE-BASED DRUG DESIGN, DIABETES, DPP4 INHIBITORS, HYDROLASE,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SCAPIN
REVDAT 1 05-OCT-16 5T4E 0
JRNL AUTH D.A.PISSARNITSKI,Z.ZHAO,D.COLE,W.L.WU,M.DOMALSKI,J.W.CLADER,
JRNL AUTH 2 G.SCAPIN,J.VOIGT,A.SORIANO,T.KELLY,M.A.POWLES,Z.YAO,
JRNL AUTH 3 D.A.BURNETT
JRNL TITL SCAFFOLD-HOPPING FROM XANTHINES TO TRICYCLIC GUANINES: A
JRNL TITL 2 CASE STUDY OF DIPEPTIDYL PEPTIDASE 4 (DPP4) INHIBITORS.
JRNL REF BIOORG.MED.CHEM. 2016
JRNL REFN ESSN 1464-3391
JRNL PMID 27670099
JRNL DOI 10.1016/J.BMC.2016.09.007
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 92.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 200807
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 10099
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.26
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 13466
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1872
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12801
REMARK 3 BIN R VALUE (WORKING SET) : 0.1853
REMARK 3 BIN FREE R VALUE : 0.2216
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.94
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 665
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 : 341
REMARK 3 SOLVENT ATOMS : 2109
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.69700
REMARK 3 B22 (A**2) : -3.22220
REMARK 3 B33 (A**2) : -1.47480
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) : 0.156
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.093
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.090
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.087
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.086
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12782 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17453 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4177 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 356 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1879 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12782 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1672 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 15942 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.94
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.49
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5T4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 200915
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 137.216
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05000
REMARK 200 FOR THE DATA SET : 11.1760
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.50400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1X70
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.27-0.30 M SODIUM ACETATE 17-18%
REMARK 280 POLYETHYLENE GLYCOL 3350 0.1 M TRIS HYDROCHLORIDE PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 59.14400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.60800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.94850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.60800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.14400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.94850
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/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O4 NAG A 802 O5 NAG A 803 2.16
REMARK 500 O4 NAG A 808 O5 NAG A 809 2.18
REMARK 500 ND2 ASN A 321 O5 NAG A 808 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 64 -169.31 -163.32
REMARK 500 ASN A 74 -4.46 66.04
REMARK 500 GLN A 123 -100.71 -110.26
REMARK 500 TRP A 124 -144.70 -95.84
REMARK 500 HIS A 162 32.95 -149.94
REMARK 500 ILE A 193 -60.42 -130.60
REMARK 500 ILE A 193 -64.17 -128.28
REMARK 500 SER A 242 -167.45 64.94
REMARK 500 GLN A 320 35.32 -73.01
REMARK 500 ASN A 450 78.98 -156.49
REMARK 500 TYR A 547 -76.48 -124.08
REMARK 500 ARG A 597 48.57 -140.32
REMARK 500 THR A 600 -97.39 -119.42
REMARK 500 SER A 630 -122.44 61.17
REMARK 500 SER A 630 -122.57 61.08
REMARK 500 ASP A 678 -95.41 -110.59
REMARK 500 ASN A 710 -71.54 -97.60
REMARK 500 ASP A 739 -154.85 -100.02
REMARK 500 SER B 64 -168.08 -163.93
REMARK 500 ASN B 74 -0.68 63.91
REMARK 500 GLN B 123 -102.31 -113.75
REMARK 500 TRP B 124 -146.59 -93.77
REMARK 500 HIS B 162 32.69 -149.93
REMARK 500 ILE B 193 -62.52 -128.63
REMARK 500 SER B 242 -164.85 64.52
REMARK 500 GLN B 320 34.46 -73.64
REMARK 500 LYS B 423 19.65 57.17
REMARK 500 ASP B 438 95.99 -162.47
REMARK 500 ASN B 450 82.11 -156.88
REMARK 500 TYR B 547 -75.21 -121.90
REMARK 500 ARG B 597 47.83 -140.54
REMARK 500 THR B 600 -101.05 -120.26
REMARK 500 SER B 630 -120.80 65.71
REMARK 500 ASP B 678 -97.02 -107.90
REMARK 500 ASN B 710 -71.26 -96.14
REMARK 500 ASP B 739 -159.17 -102.05
REMARK 500 ILE B 742 51.41 37.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1983 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A1984 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A1985 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A1986 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A1987 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A1988 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A1989 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A1990 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A1991 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A1992 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A1993 DISTANCE = 8.08 ANGSTROMS
REMARK 525 HOH A1994 DISTANCE = 9.60 ANGSTROMS
REMARK 525 HOH B1911 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B1912 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH B1913 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH B1914 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH B1915 DISTANCE = 6.64 ANGSTROMS
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 A 811 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 490 O
REMARK 620 2 LEU A 491 O 83.1
REMARK 620 3 LEU B 276 O 64.2 59.6
REMARK 620 4 VAL B 279 O 64.0 57.9 1.7
REMARK 620 5 HOH B1169 O 123.6 92.5 65.5 66.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 75L A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 75L B 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 801 bound
REMARK 800 to ASN A 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 802 through NAG A 803 bound to ASN A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 804 through NAG A 805 bound to ASN A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 806 bound
REMARK 800 to ASN A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 807 bound
REMARK 800 to ASN A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 808 through NAG A 809 bound to ASN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 801 through NAG B 802 bound to ASN B 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 803 bound
REMARK 800 to ASN B 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 804 through NAG B 805 bound to ASN B 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 806 through NAG B 807 bound to ASN B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 808 through NAG B 809 bound to ASN B 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 810 bound
REMARK 800 to ASN B 321
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5T4H RELATED DB: PDB
REMARK 900 RELATED ID: 5T4B RELATED DB: PDB
REMARK 900 RELATED ID: 5T4F RELATED DB: PDB
DBREF 5T4E A 40 766 UNP P27487 DPP4_HUMAN 40 766
DBREF 5T4E B 40 766 UNP P27487 DPP4_HUMAN 40 766
SEQADV 5T4E THR A 39 UNP P27487 EXPRESSION TAG
SEQADV 5T4E THR B 39 UNP P27487 EXPRESSION TAG
SEQRES 1 A 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 B 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET NAG A 807 14
HET NAG A 808 14
HET NAG A 809 14
HET 75L A 810 37
HET NA A 811 1
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 805 14
HET NAG B 806 14
HET NAG B 807 14
HET NAG B 808 14
HET NAG B 809 14
HET NAG B 810 14
HET 75L B 811 37
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 75L 2-[(3R)-3-AMINOPIPERIDIN-1-YL]-3-(BUT-2-YN-1-YL)-6-[(4-
HETNAM 2 75L METHYLQUINAZOLIN-2-YL)METHYL]-6,7,8,9-
HETNAM 3 75L TETRAHYDROPYRIMIDO[2,1-B]PURIN-4(3H)-ONE
HETNAM NA SODIUM ION
FORMUL 3 NAG 19(C8 H15 N O6)
FORMUL 9 75L 2(C27 H31 N9 O)
FORMUL 10 NA NA 1+
FORMUL 18 HOH *2109(H2 O)
HELIX 1 AA1 THR A 44 ASN A 51 1 8
HELIX 2 AA2 GLU A 91 ASP A 96 5 6
HELIX 3 AA3 ASP A 200 VAL A 207 1 8
HELIX 4 AA4 PRO A 290 ILE A 295 1 6
HELIX 5 AA5 VAL A 341 GLN A 344 5 4
HELIX 6 AA6 GLU A 421 MET A 425 5 5
HELIX 7 AA7 ASN A 497 GLN A 505 1 9
HELIX 8 AA8 ASN A 562 THR A 570 1 9
HELIX 9 AA9 GLY A 587 HIS A 592 1 6
HELIX 10 AB1 ALA A 593 ASN A 595 5 3
HELIX 11 AB2 THR A 600 LYS A 615 1 16
HELIX 12 AB3 SER A 630 GLY A 641 1 12
HELIX 13 AB4 ARG A 658 TYR A 662 5 5
HELIX 14 AB5 ASP A 663 GLY A 672 1 10
HELIX 15 AB6 ASN A 679 SER A 686 1 8
HELIX 16 AB7 VAL A 688 VAL A 698 5 11
HELIX 17 AB8 HIS A 712 VAL A 726 1 15
HELIX 18 AB9 SER A 744 PHE A 763 1 20
HELIX 19 AC1 THR B 44 ASN B 51 1 8
HELIX 20 AC2 ASP B 200 VAL B 207 1 8
HELIX 21 AC3 ASP B 274 LEU B 276 5 3
HELIX 22 AC4 PRO B 290 ILE B 295 1 6
HELIX 23 AC5 VAL B 341 GLN B 344 5 4
HELIX 24 AC6 GLU B 421 MET B 425 5 5
HELIX 25 AC7 ASN B 497 GLN B 505 1 9
HELIX 26 AC8 ASN B 562 THR B 570 1 9
HELIX 27 AC9 GLY B 587 HIS B 592 1 6
HELIX 28 AD1 ALA B 593 ASN B 595 5 3
HELIX 29 AD2 THR B 600 MET B 616 1 17
HELIX 30 AD3 SER B 630 GLY B 641 1 12
HELIX 31 AD4 ARG B 658 TYR B 662 5 5
HELIX 32 AD5 ASP B 663 GLY B 672 1 10
HELIX 33 AD6 ASN B 679 SER B 686 1 8
HELIX 34 AD7 VAL B 688 VAL B 698 5 11
HELIX 35 AD8 HIS B 712 VAL B 726 1 15
HELIX 36 AD9 SER B 744 PHE B 763 1 20
SHEET 1 AA1 2 LYS A 41 THR A 42 0
SHEET 2 AA1 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 AA2 4 LEU A 60 TRP A 62 0
SHEET 2 AA2 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AA2 4 ASN A 75 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 AA2 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 AA3 4 ASP A 104 ILE A 107 0
SHEET 2 AA3 4 PHE A 113 LYS A 122 -1 O GLU A 117 N ASP A 104
SHEET 3 AA3 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
SHEET 4 AA3 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AA4 4 THR A 152 TRP A 157 0
SHEET 2 AA4 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 AA4 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 AA4 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA5 3 ILE A 194 ASN A 196 0
SHEET 2 AA5 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA6 4 ILE A 194 ASN A 196 0
SHEET 2 AA6 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA6 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 AA6 4 ILE A 285 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 AA7 2 LEU A 235 PHE A 240 0
SHEET 2 AA7 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 AA8 4 HIS A 298 THR A 307 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AA8 4 TYR A 322 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 AA8 4 ARG A 336 CYS A 339 -1 O ARG A 336 N ASP A 331
SHEET 1 AA9 4 HIS A 298 THR A 307 0
SHEET 2 AA9 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AA9 4 TYR A 322 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 AA9 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 AB1 4 HIS A 363 PHE A 364 0
SHEET 2 AB1 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AB1 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 AB1 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB2 4 VAL A 404 LEU A 410 0
SHEET 2 AB2 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 AB2 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB2 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB3 4 TYR A 457 PHE A 461 0
SHEET 2 AB3 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 AB3 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AB3 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB4 8 SER A 511 LEU A 519 0
SHEET 2 AB4 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 AB4 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AB4 8 TYR A 540 ASP A 545 1 N ASP A 545 O ALA A 576
SHEET 5 AB4 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB4 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 AB4 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB5 2 LYS B 41 THR B 42 0
SHEET 2 AB5 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 AB6 4 ARG B 61 TRP B 62 0
SHEET 2 AB6 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 AB6 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 AB6 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 AB7 4 ASP B 104 ILE B 107 0
SHEET 2 AB7 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 AB7 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 AB7 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 AB8 4 THR B 152 TRP B 157 0
SHEET 2 AB8 4 LEU B 164 TRP B 168 -1 O VAL B 167 N GLN B 153
SHEET 3 AB8 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 AB8 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 AB9 3 ILE B 194 ASN B 196 0
SHEET 2 AB9 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB9 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AC1 4 ILE B 194 ASN B 196 0
SHEET 2 AC1 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AC1 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 AC1 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 AC2 2 LEU B 235 PHE B 240 0
SHEET 2 AC2 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 AC3 4 HIS B 298 THR B 307 0
SHEET 2 AC3 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 AC3 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 AC3 4 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 1 AC4 4 HIS B 298 THR B 307 0
SHEET 2 AC4 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 AC4 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 AC4 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 AC5 4 HIS B 363 PHE B 364 0
SHEET 2 AC5 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC5 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 AC5 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 AC6 4 VAL B 404 LEU B 410 0
SHEET 2 AC6 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 AC6 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC6 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AC7 4 TYR B 457 PHE B 461 0
SHEET 2 AC7 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 AC7 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 AC7 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AC8 8 SER B 511 LEU B 519 0
SHEET 2 AC8 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 AC8 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 AC8 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 AC8 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 AC8 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 AC8 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 AC8 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 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.02
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.08
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.06
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.07
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.06
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.46
LINK ND2 ASN A 150 C1 NAG A 802 1555 1555 1.45
LINK ND2 ASN A 219 C1 NAG A 804 1555 1555 1.41
LINK ND2 ASN A 229 C1 NAG A 806 1555 1555 1.46
LINK ND2 ASN A 281 C1 NAG A 807 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG A 808 1555 1555 1.38
LINK O GLY A 490 NA NA A 811 1555 1555 2.38
LINK O LEU A 491 NA NA A 811 1555 1555 2.43
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.46
LINK ND2 ASN B 150 C1 NAG B 803 1555 1555 1.48
LINK ND2 ASN B 219 C1 NAG B 804 1555 1555 1.38
LINK ND2 ASN B 229 C1 NAG B 806 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG B 808 1555 1555 1.48
LINK ND2 ASN B 321 C1 NAG B 810 1555 1555 1.45
LINK O4 NAG A 802 C1 NAG A 803 1555 1555 1.46
LINK O4 NAG A 804 C1 NAG A 805 1555 1555 1.45
LINK O4 NAG A 808 C1 NAG A 809 1555 1555 1.41
LINK O4 NAG B 801 C1 NAG B 802 1555 1555 1.45
LINK O4 NAG B 804 C1 NAG B 805 1555 1555 1.43
LINK O4 NAG B 806 C1 NAG B 807 1555 1555 1.44
LINK O4 NAG B 808 C1 NAG B 809 1555 1555 1.43
LINK O LEU B 276 NA NA A 811 1555 2564 2.26
LINK O VAL B 279 NA NA A 811 1555 2564 2.24
LINK NA NA A 811 O HOH B1169 1555 2565 2.46
CISPEP 1 GLY A 474 PRO A 475 0 5.80
CISPEP 2 GLY B 474 PRO B 475 0 1.55
SITE 1 AC1 14 GLU A 205 GLU A 206 TYR A 547 TRP A 629
SITE 2 AC1 14 SER A 630 TYR A 631 VAL A 656 TYR A 662
SITE 3 AC1 14 TYR A 666 TYR A 752 HOH A1022 HOH A1374
SITE 4 AC1 14 HOH A1419 HOH A1594
SITE 1 AC2 5 GLY A 490 LEU A 491 LEU B 276 VAL B 279
SITE 2 AC2 5 HOH B1169
SITE 1 AC3 11 GLU B 205 GLU B 206 TYR B 547 TRP B 629
SITE 2 AC3 11 SER B 630 TYR B 631 VAL B 656 TYR B 662
SITE 3 AC3 11 TYR B 666 HOH B1101 HOH B1518
SITE 1 AC4 8 GLU A 67 VAL A 78 ASN A 85 SER A 86
SITE 2 AC4 8 SER A 87 HOH A 902 HOH A1113 HOH A1148
SITE 1 AC5 4 ILE A 148 ASN A 150 HOH A1236 HOH A1606
SITE 1 AC6 10 ASN A 219 THR A 221 PHE A 222 GLN A 308
SITE 2 AC6 10 GLU A 309 TYR A 330 GLU A 332 HOH A 929
SITE 3 AC6 10 HOH A1086 HOH A1221
SITE 1 AC7 8 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC7 8 HOH A 912 HOH A1168 HOH A1339 HOH A1397
SITE 1 AC8 6 TRP A 187 VAL A 279 ASN A 281 HOH A1088
SITE 2 AC8 6 HOH A1328 HOH A1537
SITE 1 AC9 6 ASN A 321 SER A 349 THR A 350 HOH A1287
SITE 2 AC9 6 HOH A1447 HOH A1457
SITE 1 AD1 6 GLU B 67 VAL B 78 ASN B 85 SER B 86
SITE 2 AD1 6 SER B 87 HOH B1023
SITE 1 AD2 4 ARG B 147 ILE B 148 ASN B 150 HOH B1011
SITE 1 AD3 14 ASN B 219 THR B 221 PHE B 222 ASN B 272
SITE 2 AD3 14 GLN B 308 GLU B 309 TYR B 330 GLU B 332
SITE 3 AD3 14 HOH B 927 HOH B1009 HOH B1034 HOH B1104
SITE 4 AD3 14 HOH B1155 HOH B1161
SITE 1 AD4 6 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 AD4 6 HOH B 917 HOH B1405
SITE 1 AD5 14 ASN A 450 TRP B 187 THR B 188 ASN B 281
SITE 2 AD5 14 HOH B 901 HOH B 903 HOH B 915 HOH B1048
SITE 3 AD5 14 HOH B1106 HOH B1123 HOH B1128 HOH B1164
SITE 4 AD5 14 HOH B1362 HOH B1508
SITE 1 AD6 9 ILE B 319 ASN B 321 MET B 348 SER B 349
SITE 2 AD6 9 THR B 350 HOH B1235 HOH B1343 HOH B1408
SITE 3 AD6 9 HOH B1506
CRYST1 118.288 125.897 137.216 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 0.008454 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007943 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007288 0.00000
TER 6013 PRO A 766
TER 12006 PRO B 766
MASTER 404 0 22 36 102 0 37 614380 2 375 112
END |