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HEADER HYDROLASE 17-OCT-13 4N8D
TITLE DPP4 COMPLEXED WITH SYN-7AA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 39-766;
COMPND 5 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,
COMPND 6 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,
COMPND 7 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV
COMPND 8 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL
COMPND 9 PEPTIDASE IV SOLUBLE FORM;
COMPND 10 EC: 3.4.14.5;
COMPND 11 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 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.OSTERMANN,F.ZINK,M.KROEMER
REVDAT 1 12-FEB-14 4N8D 0
JRNL AUTH K.NAMOTO,F.SIROCKIN,N.OSTERMANN,F.GESSIER,S.FLOHR,R.SEDRANI,
JRNL AUTH 2 B.GERHARTZ,J.TRAPPE,U.HASSIEPEN,A.DUTTAROY,S.FERREIRA,
JRNL AUTH 3 J.M.SUTTON,D.E.CLARK,G.FENTON,M.BESWICK,D.K.BAESCHLIN
JRNL TITL DISCOVERY OF C-(1-ARYL-CYCLOHEXYL)-METHYLAMINES AS
JRNL TITL 2 SELECTIVE, ORALLY AVAILABLE INHIBITORS OF DIPEPTIDYL
JRNL TITL 3 PEPTIDASE IV.
JRNL REF BIOORG.MED.CHEM.LETT. V. 24 731 2014
JRNL REFN ISSN 0960-894X
JRNL PMID 24439847
JRNL DOI 10.1016/J.BMCL.2013.12.118
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 271022
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) : 0.155
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.800
REMARK 3 FREE R VALUE TEST SET COUNT : 4879
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.83
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 19893
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1707
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 19534
REMARK 3 BIN R VALUE (WORKING SET) : 0.1705
REMARK 3 BIN FREE R VALUE : 0.1828
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 359
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 : 11959
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 307
REMARK 3 SOLVENT ATOMS : 1960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03130
REMARK 3 B22 (A**2) : -0.39880
REMARK 3 B33 (A**2) : 0.36740
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) : 0.171
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.066
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12774 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17436 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4350 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 310 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1850 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12774 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1669 ; 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 : 15903 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.37
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.73
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6323 26.0837 56.0168
REMARK 3 T TENSOR
REMARK 3 T11: -0.0254 T22: -0.0438
REMARK 3 T33: -0.0310 T12: 0.0062
REMARK 3 T13: 0.0049 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.3731 L22: 0.6130
REMARK 3 L33: 0.2681 L12: 0.1467
REMARK 3 L13: 0.0468 L23: 0.1622
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: -0.0203 S13: -0.0218
REMARK 3 S21: 0.0283 S22: 0.0020 S23: 0.0571
REMARK 3 S31: 0.0637 S32: 0.0169 S33: 0.0015
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2105 71.5082 83.7952
REMARK 3 T TENSOR
REMARK 3 T11: -0.0134 T22: -0.0132
REMARK 3 T33: -0.0507 T12: -0.0260
REMARK 3 T13: 0.0068 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 0.5645 L22: 0.4340
REMARK 3 L33: 0.3435 L12: 0.0729
REMARK 3 L13: 0.2392 L23: 0.0738
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: -0.0829 S13: 0.1276
REMARK 3 S21: 0.0768 S22: -0.0812 S23: 0.0352
REMARK 3 S31: -0.0604 S32: -0.0030 S33: 0.0781
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4N8D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB082880.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-05
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99187
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 271195
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 76.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.940
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL PROTEIN + 0.4 UL RESERVOIR + 0.25
REMARK 280 UL WATER. PROTEIN SOLUTION: 5.2 MG/ML DPP-IV, 25 MM TRIS PH 8.0,
REMARK 280 25 MM NACL, 0.9 MM SYN-7AA, 9% DMSO. RESERVOIR SOLUTION: 30% PEG
REMARK 280 1000, 200 MM TRIS PH 8.0, 200 MM AMMONIUMSULFATE, 5% GLYCEROL.
REMARK 280 CRYO: DROP + 2.5 UL RESERVOIR PLUS 0.5 UL 1,6- HEXANDIOL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 48.65750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.41800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.96200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.41800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.65750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.96200
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: 11370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 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 SER A 39
REMARK 465 ALA A 767
REMARK 465 ALA A 768
REMARK 465 ALA A 769
REMARK 465 SER A 770
REMARK 465 TRP A 771
REMARK 465 SER A 772
REMARK 465 HIS A 773
REMARK 465 PRO A 774
REMARK 465 GLN A 775
REMARK 465 PHE A 776
REMARK 465 GLU A 777
REMARK 465 LYS A 778
REMARK 465 SER B 39
REMARK 465 HIS B 773
REMARK 465 PRO B 774
REMARK 465 GLN B 775
REMARK 465 PHE B 776
REMARK 465 GLU B 777
REMARK 465 LYS B 778
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 -169.09 -162.27
REMARK 500 ASN A 74 -6.96 68.18
REMARK 500 GLN A 123 -101.84 -111.07
REMARK 500 TRP A 124 -144.04 -95.07
REMARK 500 HIS A 162 34.90 -151.77
REMARK 500 ILE A 193 -58.88 -129.18
REMARK 500 ALA A 213 44.82 -140.62
REMARK 500 SER A 242 -164.85 63.28
REMARK 500 GLN A 320 39.68 -78.32
REMARK 500 LYS A 423 16.44 58.33
REMARK 500 ASN A 450 73.66 -153.71
REMARK 500 ASN A 487 27.39 -141.58
REMARK 500 TYR A 547 -74.50 -121.79
REMARK 500 ARG A 597 48.59 -143.71
REMARK 500 THR A 600 -97.12 -120.61
REMARK 500 SER A 630 -123.65 64.96
REMARK 500 ASP A 678 -99.09 -111.96
REMARK 500 ASN A 710 -70.71 -98.52
REMARK 500 ASP A 739 -157.57 -103.19
REMARK 500 ILE A 742 54.02 38.73
REMARK 500 SER B 64 -169.14 -161.60
REMARK 500 ASN B 74 -0.07 66.04
REMARK 500 GLN B 123 -102.41 -110.05
REMARK 500 TRP B 124 -145.50 -94.82
REMARK 500 HIS B 162 34.45 -151.81
REMARK 500 ILE B 193 -60.49 -128.53
REMARK 500 SER B 242 -164.71 62.64
REMARK 500 GLN B 320 40.12 -77.61
REMARK 500 LYS B 423 16.68 57.31
REMARK 500 ASP B 438 104.11 -165.22
REMARK 500 ASN B 450 75.96 -155.87
REMARK 500 TYR B 547 -74.56 -122.02
REMARK 500 ARG B 597 49.24 -142.67
REMARK 500 THR B 600 -96.67 -121.76
REMARK 500 SER B 630 -122.51 64.82
REMARK 500 ASP B 678 -98.75 -110.81
REMARK 500 ASN B 710 -71.82 -99.13
REMARK 500 ASP B 739 -157.48 -103.29
REMARK 500 ILE B 742 54.11 38.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2KS A 815
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2KS B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 85 RESIDUES 801 TO 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 806 BOUND
REMARK 800 TO ASN A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 807 BOUND
REMARK 800 TO ASN A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 808 BOUND
REMARK 800 TO ASN A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 809 BOUND
REMARK 800 TO ASN A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 810 BOUND
REMARK 800 TO ASN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 811 BOUND
REMARK 800 TO ASN A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 801 BOUND
REMARK 800 TO ASN B 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 802 BOUND
REMARK 800 TO ASN B 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 803 BOUND
REMARK 800 TO ASN B 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 804 BOUND
REMARK 800 TO ASN B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 805 BOUND
REMARK 800 TO ASN B 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 806 BOUND
REMARK 800 TO ASN B 321
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4A5S RELATED DB: PDB
REMARK 900 RELATED ID: 4N8E RELATED DB: PDB
DBREF 4N8D A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4N8D B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 4N8D ILE A 437 UNP P27487 SER 437 CONFLICT
SEQADV 4N8D ALA A 767 UNP P27487 EXPRESSION TAG
SEQADV 4N8D ALA A 768 UNP P27487 EXPRESSION TAG
SEQADV 4N8D ALA A 769 UNP P27487 EXPRESSION TAG
SEQADV 4N8D SER A 770 UNP P27487 EXPRESSION TAG
SEQADV 4N8D TRP A 771 UNP P27487 EXPRESSION TAG
SEQADV 4N8D SER A 772 UNP P27487 EXPRESSION TAG
SEQADV 4N8D HIS A 773 UNP P27487 EXPRESSION TAG
SEQADV 4N8D PRO A 774 UNP P27487 EXPRESSION TAG
SEQADV 4N8D GLN A 775 UNP P27487 EXPRESSION TAG
SEQADV 4N8D PHE A 776 UNP P27487 EXPRESSION TAG
SEQADV 4N8D GLU A 777 UNP P27487 EXPRESSION TAG
SEQADV 4N8D LYS A 778 UNP P27487 EXPRESSION TAG
SEQADV 4N8D ILE B 437 UNP P27487 SER 437 CONFLICT
SEQADV 4N8D ALA B 767 UNP P27487 EXPRESSION TAG
SEQADV 4N8D ALA B 768 UNP P27487 EXPRESSION TAG
SEQADV 4N8D ALA B 769 UNP P27487 EXPRESSION TAG
SEQADV 4N8D SER B 770 UNP P27487 EXPRESSION TAG
SEQADV 4N8D TRP B 771 UNP P27487 EXPRESSION TAG
SEQADV 4N8D SER B 772 UNP P27487 EXPRESSION TAG
SEQADV 4N8D HIS B 773 UNP P27487 EXPRESSION TAG
SEQADV 4N8D PRO B 774 UNP P27487 EXPRESSION TAG
SEQADV 4N8D GLN B 775 UNP P27487 EXPRESSION TAG
SEQADV 4N8D PHE B 776 UNP P27487 EXPRESSION TAG
SEQADV 4N8D GLU B 777 UNP P27487 EXPRESSION TAG
SEQADV 4N8D LYS B 778 UNP P27487 EXPRESSION TAG
SEQRES 1 A 740 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 740 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 740 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 740 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 740 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 740 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 740 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 740 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 740 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 740 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 740 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 740 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 740 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 740 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 740 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 740 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 740 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 740 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 740 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 740 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 740 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 740 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 740 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 740 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 740 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 740 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 740 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 740 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 740 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 740 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 740 ARG ASN LEU TYR LYS ILE GLN LEU ILE ASP TYR THR LYS
SEQRES 32 A 740 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 740 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 740 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 740 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 740 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 740 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 740 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 740 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 740 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 740 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 740 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 740 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 740 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 740 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 740 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 740 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 740 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 740 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 740 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 740 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 740 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 740 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 740 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 740 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 740 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 57 A 740 ALA ALA ALA SER TRP SER HIS PRO GLN PHE GLU LYS
SEQRES 1 B 740 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 740 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 740 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 740 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 740 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 740 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 740 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 740 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 740 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 740 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 740 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 740 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 740 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 740 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 740 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 740 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 740 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 740 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 740 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 740 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 740 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 740 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 740 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 740 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 740 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 740 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 740 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 740 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 740 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 740 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 740 ARG ASN LEU TYR LYS ILE GLN LEU ILE ASP TYR THR LYS
SEQRES 32 B 740 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 740 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 740 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 740 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 740 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 740 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 740 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 740 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 740 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 740 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 740 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 740 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 740 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 740 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 740 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 740 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 740 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 740 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 740 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 740 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 740 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 740 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 740 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 740 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 740 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 57 B 740 ALA ALA ALA SER TRP SER HIS PRO GLN PHE GLU LYS
MODRES 4N8D ASN A 219 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN B 321 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN A 85 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN A 321 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN B 229 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN A 520 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN B 219 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN A 229 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN A 281 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN A 150 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN B 150 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN B 281 ASN GLYCOSYLATION SITE
MODRES 4N8D ASN B 85 ASN GLYCOSYLATION SITE
HET NAG A 801 14
HET NAG A 802 14
HET MAN A 803 11
HET MAN A 804 11
HET MAN A 805 11
HET NAG A 806 14
HET NAG A 807 14
HET NAG A 808 14
HET NAG A 809 14
HET NAG A 810 14
HET NAG A 811 14
HET SO4 A 812 5
HET SO4 A 813 5
HET SO4 A 814 5
HET 2KS A 815 24
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 SO4 B 807 5
HET SO4 B 808 5
HET SO4 B 809 5
HET 2KS B 810 24
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM SO4 SULFATE ION
HETNAM 2KS 1-(CIS-1-PHENYL-4-{[(2E)-3-PHENYLPROP-2-EN-1-
HETNAM 2 2KS YL]OXY}CYCLOHEXYL)METHANAMINE
FORMUL 3 NAG 14(C8 H15 N O6)
FORMUL 3 MAN 3(C6 H12 O6)
FORMUL 10 SO4 6(O4 S 2-)
FORMUL 13 2KS 2(C22 H27 N O)
FORMUL 24 HOH *1960(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
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 MET A 616 1 17
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 PHE A 763 1 20
HELIX 19 19 THR B 44 ASN B 51 1 8
HELIX 20 20 GLU B 91 GLU B 97 5 7
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 VAL B 341 GLN B 344 5 4
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 MET B 616 1 17
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 VAL B 698 5 11
HELIX 36 36 HIS B 712 VAL B 726 1 15
HELIX 37 37 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 PHE A 79 N TYR A 68
SHEET 4 B 4 SER A 86 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 C 4 ASP A 104 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O GLU A 117 N ASP A 104
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 ILE A 285 ILE A 287 -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 VAL A 252 N TYR A 238
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 THR A 307 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 I 4 TYR A 322 TYR A 330 -1 O 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 ASP A 438 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 GLN A 469 N SER A 460
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 LEU A 491 N LEU A 482
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
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 ASP A 545 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
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 LEU B 60 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 PHE B 79 N TYR B 68
SHEET 4 O 4 SER B 86 LEU B 90 -1 O LEU B 90 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 ASP B 133 N LEU B 116
SHEET 4 P 4 GLN B 141 ILE B 143 -1 O ILE B 143 N ILE B 134
SHEET 1 Q 4 TRP B 154 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 Q 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 S 4 ILE B 285 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 U 4 TYR B 322 TYR B 330 -1 O 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 TYR B 416 N ALA B 409
SHEET 3 X 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 X 4 ASP B 438 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 GLN B 469 N SER B 460
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 Y 4 LYS B 489 GLU B 495 -1 O LEU B 491 N LEU B 482
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O TYR B 526 N ASP B 515
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 ASP B 545 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 544
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 ILE B 703 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 2.07
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 2.10
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.08
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.07
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.04
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.09
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.06
LINK O6 MAN A 803 C1 MAN A 805 1555 1555 1.39
LINK O4 NAG A 801 C1 NAG A 802 1555 1555 1.41
LINK O3 MAN A 803 C1 MAN A 804 1555 1555 1.43
LINK ND2 ASN A 219 C1 NAG A 807 1555 1555 1.43
LINK ND2 ASN B 321 C1 NAG B 806 1555 1555 1.43
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.43
LINK ND2 ASN A 321 C1 NAG A 810 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG B 804 1555 1555 1.43
LINK ND2 ASN A 520 C1 NAG A 811 1555 1555 1.43
LINK ND2 ASN B 219 C1 NAG B 803 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG A 808 1555 1555 1.43
LINK ND2 ASN A 281 C1 NAG A 809 1555 1555 1.43
LINK ND2 ASN A 150 C1 NAG A 806 1555 1555 1.43
LINK ND2 ASN B 150 C1 NAG B 802 1555 1555 1.43
LINK ND2 ASN B 281 C1 NAG B 805 1555 1555 1.43
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.44
LINK O4 NAG A 802 C1 MAN A 803 1555 1555 1.46
CISPEP 1 GLY A 474 PRO A 475 0 11.09
CISPEP 2 GLY B 474 PRO B 475 0 8.73
SITE 1 AC1 5 ARG A 596 ARG A 597 ASN A 679 HOH A1803
SITE 2 AC1 5 HOH A1814
SITE 1 AC2 3 GLU A 146 ARG A 147 HOH A1412
SITE 1 AC3 5 ARG A 658 ARG A 684 HOH A1075 GLU B 244
SITE 2 AC3 5 SER B 245
SITE 1 AC4 11 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 AC4 11 ARG A 358 SER A 630 TYR A 662 TYR A 666
SITE 3 AC4 11 VAL A 711 HIS A 740 HOH A1462
SITE 1 AC5 5 THR B 144 GLU B 145 GLU B 146 ARG B 147
SITE 2 AC5 5 HOH B1657
SITE 1 AC6 4 ARG B 596 ARG B 597 ASP B 678 ASN B 679
SITE 1 AC7 5 GLU A 244 ARG B 658 ARG B 684 HOH B1335
SITE 2 AC7 5 HOH B1654
SITE 1 AC8 12 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 AC8 12 ARG B 358 TYR B 547 SER B 630 TYR B 662
SITE 3 AC8 12 TYR B 666 VAL B 711 HIS B 740 HOH B1346
SITE 1 AC9 26 GLU A 67 VAL A 78 ASN A 85 SER A 86
SITE 2 AC9 26 SER A 87 LEU A 519 ASN A 520 GLU A 608
SITE 3 AC9 26 ARG A 611 NAG A 811 HOH A1071 HOH A1167
SITE 4 AC9 26 HOH A1184 HOH A1249 HOH A1279 HOH A1280
SITE 5 AC9 26 HOH A1443 HOH A1473 HOH A1664 HOH A1676
SITE 6 AC9 26 HOH A1710 HOH A1784 HOH A1812 HOH A1828
SITE 7 AC9 26 HOH A1830 ASP B 393
SITE 1 BC1 5 ARG A 147 ILE A 148 ASN A 150 HOH A1345
SITE 2 BC1 5 HOH A1692
SITE 1 BC2 6 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 2 BC2 6 HOH A1519 HOH A1593
SITE 1 BC3 7 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 BC3 7 HOH A1147 HOH A1336 HOH A1790
SITE 1 BC4 5 TRP A 187 VAL A 279 ASN A 281 HOH A1202
SITE 2 BC4 5 HOH A1470
SITE 1 BC5 7 ASN A 321 MET A 348 SER A 349 THR A 350
SITE 2 BC5 7 HOH A1364 HOH A1910 HOH B1605
SITE 1 BC6 4 ASN A 520 ARG A 581 ASP A 605 MAN A 805
SITE 1 BC7 5 VAL B 78 ASN B 85 SER B 86 SER B 87
SITE 2 BC7 5 HOH B1357
SITE 1 BC8 6 ARG B 147 ILE B 148 ASN B 150 HOH B1275
SITE 2 BC8 6 HOH B1315 HOH B1451
SITE 1 BC9 6 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC9 6 HOH B1220 HOH B1480
SITE 1 CC1 8 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 CC1 8 HOH B1096 HOH B1197 HOH B1236 HOH B1761
SITE 1 CC2 5 TRP B 187 VAL B 279 ASN B 281 HOH B1337
SITE 2 CC2 5 HOH B1498
SITE 1 CC3 6 ASN B 321 MET B 348 SER B 349 THR B 350
SITE 2 CC3 6 HOH B1620 HOH B1698
CRYST1 97.315 121.924 190.836 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 0.010276 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008202 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005240 0.00000
TER 6016 PRO A 766
TER 12079 SER B 772
MASTER 437 0 25 37 102 0 46 614226 2 340 114
END |