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HEADER HYDROLASE 17-OCT-13 4N8E
TITLE DPP4 COMPLEXED WITH COMPOUND 12A
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 4N8E 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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 99769
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 4589
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.36
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.28
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6975
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2267
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6654
REMARK 3 BIN R VALUE (WORKING SET) : 0.2243
REMARK 3 BIN FREE R VALUE : 0.2749
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 321
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 : 11965
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 303
REMARK 3 SOLVENT ATOMS : 1085
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.89000
REMARK 3 B22 (A**2) : -5.17120
REMARK 3 B33 (A**2) : -2.71880
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) : 0.248
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) : 0.213
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 : 0.913
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12641 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17236 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4284 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 306 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1816 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12641 ; 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 : 1652 ; 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 : 14802 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.51
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.60
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): 13.6629 26.0777 56.1876
REMARK 3 T TENSOR
REMARK 3 T11: 0.0723 T22: -0.1267
REMARK 3 T33: -0.1350 T12: 0.0199
REMARK 3 T13: 0.0072 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.4252 L22: 0.8284
REMARK 3 L33: 0.3536 L12: 0.2523
REMARK 3 L13: 0.0493 L23: -0.0064
REMARK 3 S TENSOR
REMARK 3 S11: -0.0189 S12: -0.0306 S13: -0.0202
REMARK 3 S21: -0.0410 S22: 0.0208 S23: 0.0295
REMARK 3 S31: 0.0696 S32: 0.0523 S33: -0.0019
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2467 71.6303 84.0998
REMARK 3 T TENSOR
REMARK 3 T11: 0.1126 T22: -0.1108
REMARK 3 T33: -0.0962 T12: -0.0140
REMARK 3 T13: 0.0061 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 0.5520 L22: 0.4047
REMARK 3 L33: 0.4705 L12: 0.0902
REMARK 3 L13: 0.2755 L23: 0.0494
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: -0.0467 S13: 0.1253
REMARK 3 S21: 0.0230 S22: -0.0542 S23: 0.0050
REMARK 3 S31: -0.0782 S32: 0.0044 S33: 0.0685
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4N8E 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 RCSB082881.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 108620
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.17100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.420
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 (%): 62.75
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 COMPOUND12A, 9% DMSO. RESERVOIR SOLUTION: 30%
REMARK 280 PEG 1000, 200 MM TRIS PH 8.0, 200 MM AMMONIUMSULFATE, 5%
REMARK 280 GLYCEROL. CRYO: DROP + 2.5 UL RESERVOIR PLUS 0.5 UL 1,6-
REMARK 280 HEXANDIOL, VAPOR 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 48.54500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.67400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.02400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.67400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.54500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.02400
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: 59960 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 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 -166.02 -163.89
REMARK 500 ASN A 74 -6.66 71.39
REMARK 500 PHE A 89 -68.03 -90.06
REMARK 500 SER A 106 112.94 -160.42
REMARK 500 GLN A 123 -102.53 -110.19
REMARK 500 TRP A 124 -151.63 -92.30
REMARK 500 HIS A 162 37.11 -148.27
REMARK 500 ASN A 170 19.59 59.60
REMARK 500 ILE A 193 -61.94 -123.35
REMARK 500 VAL A 207 -64.72 -104.56
REMARK 500 ALA A 213 42.64 -141.54
REMARK 500 SER A 242 -162.13 61.70
REMARK 500 GLN A 320 29.90 -73.02
REMARK 500 THR A 411 -169.14 -118.07
REMARK 500 LYS A 423 16.85 53.94
REMARK 500 ASN A 450 73.96 -152.78
REMARK 500 TYR A 547 -65.17 -125.52
REMARK 500 ALA A 548 18.93 55.19
REMARK 500 ASN A 562 -157.92 -144.61
REMARK 500 ARG A 597 54.04 -141.86
REMARK 500 THR A 600 -96.51 -118.63
REMARK 500 SER A 630 -119.41 63.25
REMARK 500 ASP A 678 -102.32 -107.64
REMARK 500 ASN A 710 -70.51 -93.65
REMARK 500 SER B 64 -166.30 -163.88
REMARK 500 HIS B 66 -1.27 -146.31
REMARK 500 ASN B 74 -4.48 71.54
REMARK 500 GLU B 97 33.78 -83.01
REMARK 500 SER B 106 112.03 -160.92
REMARK 500 GLN B 123 -96.74 -117.37
REMARK 500 TRP B 124 -151.48 -95.34
REMARK 500 HIS B 162 36.63 -148.41
REMARK 500 ILE B 193 -62.40 -124.60
REMARK 500 VAL B 207 -66.29 -105.03
REMARK 500 ALA B 213 42.98 -140.56
REMARK 500 SER B 242 -159.73 61.45
REMARK 500 GLN B 320 28.93 -72.10
REMARK 500 THR B 411 -169.72 -118.42
REMARK 500 ASP B 438 95.85 -164.05
REMARK 500 ASN B 450 76.74 -152.55
REMARK 500 TYR B 547 -65.47 -126.10
REMARK 500 ALA B 548 19.21 55.12
REMARK 500 ASN B 562 -158.58 -141.71
REMARK 500 ARG B 597 53.79 -142.85
REMARK 500 THR B 600 -96.07 -118.30
REMARK 500 SER B 630 -120.44 65.58
REMARK 500 ASP B 678 -101.51 -105.87
REMARK 500 ASN B 710 -70.03 -93.23
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 2KV 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 2KV 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: 4N8D RELATED DB: PDB
DBREF 4N8E A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4N8E B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 4N8E ILE A 437 UNP P27487 SER 437 CONFLICT
SEQADV 4N8E ALA A 767 UNP P27487 EXPRESSION TAG
SEQADV 4N8E ALA A 768 UNP P27487 EXPRESSION TAG
SEQADV 4N8E ALA A 769 UNP P27487 EXPRESSION TAG
SEQADV 4N8E SER A 770 UNP P27487 EXPRESSION TAG
SEQADV 4N8E TRP A 771 UNP P27487 EXPRESSION TAG
SEQADV 4N8E SER A 772 UNP P27487 EXPRESSION TAG
SEQADV 4N8E HIS A 773 UNP P27487 EXPRESSION TAG
SEQADV 4N8E PRO A 774 UNP P27487 EXPRESSION TAG
SEQADV 4N8E GLN A 775 UNP P27487 EXPRESSION TAG
SEQADV 4N8E PHE A 776 UNP P27487 EXPRESSION TAG
SEQADV 4N8E GLU A 777 UNP P27487 EXPRESSION TAG
SEQADV 4N8E LYS A 778 UNP P27487 EXPRESSION TAG
SEQADV 4N8E ILE B 437 UNP P27487 SER 437 CONFLICT
SEQADV 4N8E ALA B 767 UNP P27487 EXPRESSION TAG
SEQADV 4N8E ALA B 768 UNP P27487 EXPRESSION TAG
SEQADV 4N8E ALA B 769 UNP P27487 EXPRESSION TAG
SEQADV 4N8E SER B 770 UNP P27487 EXPRESSION TAG
SEQADV 4N8E TRP B 771 UNP P27487 EXPRESSION TAG
SEQADV 4N8E SER B 772 UNP P27487 EXPRESSION TAG
SEQADV 4N8E HIS B 773 UNP P27487 EXPRESSION TAG
SEQADV 4N8E PRO B 774 UNP P27487 EXPRESSION TAG
SEQADV 4N8E GLN B 775 UNP P27487 EXPRESSION TAG
SEQADV 4N8E PHE B 776 UNP P27487 EXPRESSION TAG
SEQADV 4N8E GLU B 777 UNP P27487 EXPRESSION TAG
SEQADV 4N8E 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 4N8E ASN A 520 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN A 85 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN B 321 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN B 219 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN A 321 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN B 150 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN B 229 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN A 229 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN B 281 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN A 219 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN A 150 ASN GLYCOSYLATION SITE
MODRES 4N8E ASN A 281 ASN GLYCOSYLATION SITE
MODRES 4N8E 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 2KV A 815 22
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 2KV B 810 22
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM SO4 SULFATE ION
HETNAM 2KV 1-[CIS-4-(AMINOMETHYL)-4-(3-CHLOROPHENYL)
HETNAM 2 2KV CYCLOHEXYL]PIPERIDIN-2-ONE
FORMUL 3 NAG 14(C8 H15 N O6)
FORMUL 3 MAN 3(C6 H12 O6)
FORMUL 10 SO4 6(O4 S 2-)
FORMUL 13 2KV 2(C18 H25 CL N2 O)
FORMUL 24 HOH *1085(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 GLU A 91 ASP A 96 5 6
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 ASP A 274 LEU A 276 5 3
HELIX 5 5 PRO A 290 ILE A 295 1 6
HELIX 6 6 VAL A 341 GLN A 344 5 4
HELIX 7 7 GLU A 421 MET A 425 5 5
HELIX 8 8 ASN A 497 GLN A 505 1 9
HELIX 9 9 ASN A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 LYS A 615 1 16
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 ARG A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 SER A 686 1 8
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 PHE A 713 VAL A 726 1 14
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 THR B 44 ASN B 51 1 8
HELIX 21 21 GLU B 91 GLU B 97 5 7
HELIX 22 22 ASP B 200 VAL B 207 1 8
HELIX 23 23 ASP B 274 LEU B 276 5 3
HELIX 24 24 PRO B 290 ILE B 295 1 6
HELIX 25 25 VAL B 341 GLN B 344 5 4
HELIX 26 26 GLU B 421 MET B 425 5 5
HELIX 27 27 ASN B 497 GLN B 505 1 9
HELIX 28 28 ASN B 562 THR B 570 1 9
HELIX 29 29 GLY B 587 HIS B 592 1 6
HELIX 30 30 ALA B 593 ASN B 595 5 3
HELIX 31 31 THR B 600 LYS B 615 1 16
HELIX 32 32 SER B 630 GLY B 641 1 12
HELIX 33 33 ARG B 658 TYR B 662 5 5
HELIX 34 34 ASP B 663 GLY B 672 1 10
HELIX 35 35 ASN B 679 SER B 686 1 8
HELIX 36 36 VAL B 688 VAL B 698 5 11
HELIX 37 37 PHE B 713 VAL B 726 1 14
HELIX 38 38 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 ARG A 61 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 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 ILE A 287 -1 O ILE A 287 N PHE A 268
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 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O GLN A 314 N CYS A 301
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 TRP A 305 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O GLN A 314 N CYS A 301
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 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 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 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 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 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 PHE B 79 N TYR B 68
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 ASP B 133 N LEU B 116
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 VAL B 167 N TRP B 154
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 SER B 284 ILE B 287 -1 O ILE B 287 N PHE B 268
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 GLU B 347 N SER B 323
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 ARG B 471 N SER B 458
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 ARG B 492 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 THR B 522 N LEU B 519
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 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 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 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.03
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 2.04
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.03
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.02
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.05
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.03
LINK O4 NAG A 801 C1 NAG A 802 1555 1555 1.39
LINK O6 MAN A 803 C1 MAN A 805 1555 1555 1.40
LINK ND2 ASN A 520 C1 NAG A 811 1555 1555 1.42
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.43
LINK ND2 ASN B 321 C1 NAG B 806 1555 1555 1.43
LINK ND2 ASN B 219 C1 NAG B 803 1555 1555 1.43
LINK ND2 ASN A 321 C1 NAG A 810 1555 1555 1.43
LINK ND2 ASN B 150 C1 NAG B 802 1555 1555 1.43
LINK O3 MAN A 803 C1 MAN A 804 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG B 804 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG A 808 1555 1555 1.44
LINK ND2 ASN B 281 C1 NAG B 805 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG A 807 1555 1555 1.44
LINK ND2 ASN A 150 C1 NAG A 806 1555 1555 1.44
LINK O4 NAG A 802 C1 MAN A 803 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG A 809 1555 1555 1.44
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.44
CISPEP 1 GLY A 474 PRO A 475 0 1.27
CISPEP 2 GLY B 474 PRO B 475 0 0.90
SITE 1 AC1 4 ARG A 596 ARG A 597 ASP A 678 ASN A 679
SITE 1 AC2 3 GLU A 146 ARG A 147 HOH A1481
SITE 1 AC3 3 ARG A 658 ARG A 684 SER B 245
SITE 1 AC4 12 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 AC4 12 PHE A 357 TYR A 547 SER A 630 TYR A 662
SITE 3 AC4 12 TYR A 666 HIS A 740 HOH A1041 HOH A1073
SITE 1 AC5 4 THR B 144 GLU B 145 GLU B 146 ARG B 147
SITE 1 AC6 5 ARG B 596 ARG B 597 ASP B 678 ASN B 679
SITE 2 AC6 5 HOH B1115
SITE 1 AC7 4 GLU A 244 ARG B 658 ARG B 684 HOH B1391
SITE 1 AC8 10 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 AC8 10 SER B 630 TYR B 631 TYR B 662 TYR B 666
SITE 3 AC8 10 HIS B 740 HOH B1046
SITE 1 AC9 13 ASN A 85 SER A 87 ASN A 520 GLU A 608
SITE 2 AC9 13 ARG A 611 NAG A 811 HOH A1075 HOH A1134
SITE 3 AC9 13 HOH A1192 HOH A1237 HOH A1242 HOH A1326
SITE 4 AC9 13 LYS B 391
SITE 1 BC1 3 ARG A 147 ILE A 148 ASN A 150
SITE 1 BC2 6 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 2 BC2 6 HOH A1150 HOH A1449
SITE 1 BC3 5 ASN A 229 THR A 231 GLU A 232 LYS A 267
SITE 2 BC3 5 HOH A1045
SITE 1 BC4 3 TRP A 187 ASN A 281 HOH A1099
SITE 1 BC5 5 ILE A 319 ASN A 321 SER A 349 THR A 350
SITE 2 BC5 5 ARG A 596
SITE 1 BC6 4 ASN A 520 ARG A 581 MAN A 805 HOH A1040
SITE 1 BC7 4 ASN B 85 SER B 86 SER B 87 HOH B1093
SITE 1 BC8 3 ARG B 147 ASN B 150 HOH B1102
SITE 1 BC9 5 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC9 5 HOH B1013
SITE 1 CC1 5 ILE B 194 ASN B 229 THR B 231 LYS B 267
SITE 2 CC1 5 HOH B1084
SITE 1 CC2 6 TRP B 187 VAL B 279 ASN B 281 HOH B1199
SITE 2 CC2 6 HOH B1305 HOH B1342
SITE 1 CC3 4 ILE B 319 ASN B 321 SER B 349 ARG B 596
CRYST1 97.090 122.048 191.348 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 0.010300 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005226 0.00000
TER 5960 PRO A 766
TER 11967 SER B 772
MASTER 445 0 25 38 102 0 35 613353 2 336 114
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