4A5S-pdb | HEADER HYDROLASE 28-OCT-11 4A5S
TITLE CRYSTAL STRUCTURE OF HUMAN DPP4 IN COMPLEX WITH A NOVAL HETEROCYCLIC
TITLE 2 DPP4 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM, DIPEPTIDYL PEPTIDASE
COMPND 5 4, ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,
COMPND 6 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,
COMPND 7 TP103, CD_ANTIGEN=CD26;
COMPND 8 EC: 3.4.14.5;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS HYDROLASE, TYPE 2 DIABETES, NOVARTIS COMPOUND NVP-BIV988
EXPDTA X-RAY DIFFRACTION
AUTHOR N.OSTERMANN,M.KROEMER,F.ZINK,B.GERHARTZ,J.M.SUTTON,D.E.CLARK,
AUTHOR 2 S.J.DUNSDON,G.FENTON,A.FILLMORE,N.V.HARRIS,C.HIGGS,C.A.HURLEY,
AUTHOR 3 S.L.KRINTEL,R.E.MACKENZIE,A.DUTTAROY,E.GANGL,W.MANIARA,R.SEDRANI,
AUTHOR 4 K.NAMOTO,F.SIROCKIN,J.TRAPPE,U.HASSIEPEN,D.K.BAESCHLIN
REVDAT 1 08-FEB-12 4A5S 0
JRNL AUTH J.M.SUTTON,D.E.CLARK,S.J.DUNSDON,G.FENTON,A.FILLMORE,
JRNL AUTH 2 N.V.HARRIS,C.HIGGS,C.A.HURLEY,S.L.KRINTEL,R.E.MACKENZIE,
JRNL AUTH 3 A.DUTTAROY,E.GANGL,W.MANIARA,R.SEDRANI,K.NAMOTO,N.OSTERMANN,
JRNL AUTH 4 B.GERHARTZ,F.SIROCKIN,J.TRAPPE,U.HASSIEPEN,D.K.BAESCHLIN
JRNL TITL NOVEL HETEROCYCLIC DPP-4 INHIBITORS FOR THE TREATMENT OF
JRNL TITL 2 TYPE 2 DIABETES.
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 1464 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 22177783
JRNL DOI 10.1016/J.BMCL.2011.11.054
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.74
REMARK 3 NUMBER OF REFLECTIONS : 284274
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) : 0.1641
REMARK 3 R VALUE (WORKING SET) : 0.1638
REMARK 3 FREE R VALUE : 0.1789
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.80
REMARK 3 FREE R VALUE TEST SET COUNT : 5116
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) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.74
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 20777
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1925
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 20403
REMARK 3 BIN R VALUE (WORKING SET) : 0.1924
REMARK 3 BIN FREE R VALUE : 0.1959
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 374
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 : 12058
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 333
REMARK 3 SOLVENT ATOMS : 1590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.1534
REMARK 3 B22 (A**2) : 0.2328
REMARK 3 B33 (A**2) : -0.0794
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.155
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.068
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.066
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.066
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.064
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 : 0.9644
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9596
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12792 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 17481 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 4368 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 311 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 1868 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12792 ; 20.00 ; 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 : 1677 ; 5.00 ; 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 : 16099 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.30
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.91
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY.
REMARK 4
REMARK 4 4A5S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-OCT-11.
REMARK 100 THE PDBE ID CODE IS EBI-50100.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 1.00054
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 284276
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.62
REMARK 200 RESOLUTION RANGE LOW (A) : 87.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.89
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.22
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.09
REMARK 200 R MERGE FOR SHELL (I) : 0.40
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.20
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL PROTEIN, 0.4 UL RESERVOIR,
REMARK 280 0.25 UL WATER; PROTEIN SOLUTION: 5.2 MG/ML DPP4, 25 MM
REMARK 280 TRIS PH 8, 25 MM NACL, 2 MM NVP-BIV988-AA-1, 2% DMSO;
REMARK 280 RESERVOIR SOLUTION: 40% PEG 1000, 200 MM TRIS PH 9.0, 200
REMARK 280 MM AMMONIUM SULFATE, 5% GLYCEROL
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 48.59150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.34950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.71200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.34950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.59150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.71200
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: 10090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.7 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 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 PRO B 774
REMARK 465 GLN B 775
REMARK 465 PHE B 776
REMARK 465 GLU B 777
REMARK 465 LYS B 778
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ALA A 767 CA C O CB
REMARK 470 HIS B 773 CA C O CB CG ND1 CD2 CE1 NE2
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 ASN A 74 -5.68 64.71
REMARK 500 GLN A 123 -101.46 -111.60
REMARK 500 TRP A 124 -144.44 -95.83
REMARK 500 HIS A 162 35.67 -151.42
REMARK 500 ILE A 193 -56.78 -128.05
REMARK 500 SER A 242 -165.31 64.32
REMARK 500 GLN A 320 37.64 -74.86
REMARK 500 LYS A 423 16.17 59.41
REMARK 500 ASN A 450 70.55 -151.64
REMARK 500 ASN A 487 26.78 -140.40
REMARK 500 TYR A 547 -75.68 -117.44
REMARK 500 ARG A 597 47.54 -143.09
REMARK 500 THR A 600 -96.58 -119.12
REMARK 500 SER A 630 -124.30 64.27
REMARK 500 ASP A 678 -101.30 -109.35
REMARK 500 ASN A 710 -66.54 -101.77
REMARK 500 ASP A 739 -159.43 -102.43
REMARK 500 ILE A 742 52.99 38.76
REMARK 500 ASN B 74 -0.85 66.78
REMARK 500 GLN B 123 -99.05 -110.60
REMARK 500 TRP B 124 -143.42 -97.47
REMARK 500 HIS B 162 32.97 -152.17
REMARK 500 ILE B 193 -60.23 -130.22
REMARK 500 SER B 242 -163.63 62.43
REMARK 500 GLN B 320 38.28 -77.11
REMARK 500 LYS B 423 16.35 57.11
REMARK 500 ASN B 450 77.22 -159.86
REMARK 500 TYR B 547 -76.25 -118.57
REMARK 500 ARG B 597 50.02 -141.66
REMARK 500 THR B 600 -95.35 -119.74
REMARK 500 SER B 630 -121.54 64.36
REMARK 500 ASP B 678 -95.92 -109.20
REMARK 500 ASN B 710 -69.79 -98.95
REMARK 500 ASP B 739 -156.61 -104.18
REMARK 500 ILE B 742 52.83 38.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE B 389 25.0 L L OUTSIDE RANGE
REMARK 500 LYS B 463 24.0 L L OUTSIDE RANGE
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 N7F A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1767
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1768
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1769
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N7F B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1773
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1774
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1775
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
REMARK 800 ASN A 85 RESIDUES 1085 TO 1089
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 150 RESIDUES 1150 TO 1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 219 RESIDUES 1219 TO 1219
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 229 RESIDUES 1229 TO 1229
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 281 RESIDUES 1281 TO 1281
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 321 RESIDUES 1321 TO 1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 520 RESIDUES 1520 TO 1520
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800 ASN B 85 RESIDUES 2085 TO 2085
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800 ASN B 150 RESIDUES 2150 TO 2150
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800 ASN B 219 RESIDUES 2219 TO 2219
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800 ASN B 229 RESIDUES 2229 TO 2229
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800 ASN B 281 RESIDUES 2281 TO 2281
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B2321 BOUND TO ASN B 321
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1W1I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPPIV OR
REMARK 900 CD26) IN COMPLEX WITH ADENOSINE DEAMINASE
REMARK 900 RELATED ID: 1RWQ RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH 5-
REMARK 900 AMINOMETHYL-6-(2,4-DICHLORO-PHENYL)-2-(3,5-DIMETHOXY
REMARK 900 -PHENYL)-PYRIMIDIN-4-YLAMINE
REMARK 900 RELATED ID: 1TK3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL PEPTIDASE IV/
REMARK 900 CD26
REMARK 900 RELATED ID: 2BGR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 TAT DERIVED NONAPEPTIDES
REMARK 900 TAT(1-9) BOUND TO THE ACTIVE SITE OF DIPEPTIDYL
REMARK 900 PEPTIDASE IV (CD26)
REMARK 900 RELATED ID: 1N1M RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN COMPLEX WITH
REMARK 900 ANINHIBITOR
REMARK 900 RELATED ID: 2G5T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (
REMARK 900 DPPIV)COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO)
REMARK 900 INHIBITOR 21AG
REMARK 900 RELATED ID: 1NU6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP
REMARK 900 -IV)
REMARK 900 RELATED ID: 1PFQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL PEPTIDASE IV
REMARK 900 /CD26
REMARK 900 RELATED ID: 1TKR RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 INHIBITED
REMARK 900 WITHDIISOPROPYL FLUOROPHOSPHATE
REMARK 900 RELATED ID: 2G5P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (
REMARK 900 DPPIV)COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO)
REMARK 900 INHIBITOR 21AC
REMARK 900 RELATED ID: 1X70 RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH A BETA
REMARK 900 AMINOACID INHIBITOR
REMARK 900 RELATED ID: 1WCY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (
REMARK 900 DPPIV)COMPLEX WITH DIPROTIN A
REMARK 900 RELATED ID: 1R9M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV AT
REMARK 900 2.1ANG. RESOLUTION.
REMARK 900 RELATED ID: 1NU8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP
REMARK 900 -IV)IN COMPLEX WITH DIPROTIN A (ILI)
REMARK 900 RELATED ID: 1J2E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV
REMARK 900 RELATED ID: 2JID RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH 1-(3,4
REMARK 900 -DIMETHOXY-PHENYL)-3-M-TOLYL-PIPERIDINE-4-YLAMINE
REMARK 900 RELATED ID: 1U8E RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 MUTANT Y547F
REMARK 900 RELATED ID: 2G63 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (
REMARK 900 DPPIV)COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO)
REMARK 900 INHIBITOR 24B
REMARK 900 RELATED ID: 2BUB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPDIDASE IV (CD26
REMARK 900 ) IN COMPLEX WITH A REVERSED AMIDE INHIBITOR
REMARK 900 RELATED ID: 2AJL RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF NOVEL BIARYL-BASED DIPEPTIDYL
REMARK 900 PEPTIDASEIV INHIBITOR
REMARK 900 RELATED ID: 2BGN RELATED DB: PDB
REMARK 900 HIV-1 TAT PROTEIN DERIVED N-TERMINAL NONAPEPTIDE TRP2
REMARK 900 -TAT(1-9) BOUND TO THE ACTIVE SITE OF DIPEPTIDYL
REMARK 900 PEPTIDASE IV (CD26)
REMARK 900 RELATED ID: 1R9N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV
REMARK 900 INCOMPLEX WITH A DECAPEPTIDE (TNPY) AT 2.3 ANG.
REMARK 900 RESOLUTION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 S437I SEQUENCE CONFLICT KNOWN IN UNIPROT.
DBREF 4A5S A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4A5S B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 4A5S ALA A 767 UNP P27487 EXPRESSION TAG
SEQADV 4A5S ALA A 768 UNP P27487 EXPRESSION TAG
SEQADV 4A5S ALA A 769 UNP P27487 EXPRESSION TAG
SEQADV 4A5S SER A 770 UNP P27487 EXPRESSION TAG
SEQADV 4A5S TRP A 771 UNP P27487 EXPRESSION TAG
SEQADV 4A5S SER A 772 UNP P27487 EXPRESSION TAG
SEQADV 4A5S HIS A 773 UNP P27487 EXPRESSION TAG
SEQADV 4A5S PRO A 774 UNP P27487 EXPRESSION TAG
SEQADV 4A5S GLN A 775 UNP P27487 EXPRESSION TAG
SEQADV 4A5S PHE A 776 UNP P27487 EXPRESSION TAG
SEQADV 4A5S GLU A 777 UNP P27487 EXPRESSION TAG
SEQADV 4A5S LYS A 778 UNP P27487 EXPRESSION TAG
SEQADV 4A5S ILE A 437 UNP P27487 SER 437 CONFLICT
SEQADV 4A5S ALA B 767 UNP P27487 EXPRESSION TAG
SEQADV 4A5S ALA B 768 UNP P27487 EXPRESSION TAG
SEQADV 4A5S ALA B 769 UNP P27487 EXPRESSION TAG
SEQADV 4A5S SER B 770 UNP P27487 EXPRESSION TAG
SEQADV 4A5S TRP B 771 UNP P27487 EXPRESSION TAG
SEQADV 4A5S SER B 772 UNP P27487 EXPRESSION TAG
SEQADV 4A5S HIS B 773 UNP P27487 EXPRESSION TAG
SEQADV 4A5S PRO B 774 UNP P27487 EXPRESSION TAG
SEQADV 4A5S GLN B 775 UNP P27487 EXPRESSION TAG
SEQADV 4A5S PHE B 776 UNP P27487 EXPRESSION TAG
SEQADV 4A5S GLU B 777 UNP P27487 EXPRESSION TAG
SEQADV 4A5S LYS B 778 UNP P27487 EXPRESSION TAG
SEQADV 4A5S ILE B 437 UNP P27487 SER 437 CONFLICT
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
HET N7F A 901 37
HET NAG A1085 14
HET NAG A1086 14
HET MAN A1087 11
HET MAN A1088 11
HET MAN A1089 11
HET NAG A1150 14
HET NAG A1219 14
HET NAG A1229 14
HET NAG A1281 14
HET NAG A1321 14
HET NAG A1520 14
HET SO4 A1767 5
HET SO4 A1768 5
HET SO4 A1769 5
HET N7F B 901 37
HET SO4 B1773 5
HET SO4 B1774 5
HET SO4 B1775 5
HET NAG B2085 14
HET NAG B2150 14
HET NAG B2219 14
HET NAG B2229 14
HET NAG B2281 14
HET NAG B2321 14
HETNAM N7F 6-[(3S)-3-AMINOPIPERIDIN-1-YL]-5-BENZYL-4-
HETNAM 2 N7F OXO-3-(QUINOLIN-4-YLMETHYL)-4,5-DIHYDRO-3H-
HETNAM 3 N7F PYRROLO[3,2-D]PYRIMIDINE-7-CARBONITRILE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM SO4 SULFATE ION
FORMUL 3 N7F 2(C29 H27 N7 O)
FORMUL 4 NAG 14(C8 H15 N O6)
FORMUL 5 MAN 3(C6 H12 O6)
FORMUL 6 SO4 6(O4 S 2-)
FORMUL 7 HOH *1590(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 PRO A 290 ILE A 295 1 6
HELIX 4 4 VAL A 341 GLN A 344 5 4
HELIX 5 5 GLU A 421 MET A 425 5 5
HELIX 6 6 ASN A 497 GLN A 505 1 9
HELIX 7 7 ASN A 562 THR A 570 1 9
HELIX 8 8 GLY A 587 HIS A 592 1 6
HELIX 9 9 ALA A 593 ASN A 595 5 3
HELIX 10 10 THR A 600 LYS A 615 1 16
HELIX 11 11 SER A 630 GLY A 641 1 12
HELIX 12 12 ARG A 658 TYR A 662 5 5
HELIX 13 13 ASP A 663 GLY A 672 1 10
HELIX 14 14 ASN A 679 SER A 686 1 8
HELIX 15 15 VAL A 688 VAL A 698 5 11
HELIX 16 16 PHE A 713 VAL A 726 1 14
HELIX 17 17 SER A 744 PHE A 763 1 20
HELIX 18 18 THR B 44 ASN B 51 1 8
HELIX 19 19 GLU B 91 GLU B 97 5 7
HELIX 20 20 ASP B 200 VAL B 207 1 8
HELIX 21 21 PRO B 290 ILE B 295 1 6
HELIX 22 22 VAL B 341 GLN B 344 5 4
HELIX 23 23 GLU B 421 MET B 425 5 5
HELIX 24 24 ASN B 497 GLN B 505 1 9
HELIX 25 25 ASN B 562 THR B 570 1 9
HELIX 26 26 GLY B 587 HIS B 592 1 6
HELIX 27 27 ALA B 593 ASN B 595 5 3
HELIX 28 28 THR B 600 MET B 616 1 17
HELIX 29 29 SER B 630 GLY B 641 1 12
HELIX 30 30 ARG B 658 TYR B 662 5 5
HELIX 31 31 ASP B 663 GLY B 672 1 10
HELIX 32 32 ASN B 679 SER B 686 1 8
HELIX 33 33 VAL B 688 VAL B 698 5 11
HELIX 34 34 HIS B 712 VAL B 726 1 15
HELIX 35 35 SER B 744 PHE B 763 1 20
SHEET 1 AA 2 LYS A 41 THR A 42 0
SHEET 2 AA 2 VAL A 507 GLN A 508 1 N GLN A 508 O LYS A 41
SHEET 1 AB 4 LEU A 60 TRP A 62 0
SHEET 2 AB 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AB 4 ASN A 75 ASN A 80 -1 O ASN A 75 N GLN A 72
SHEET 4 AB 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AC 4 ASP A 104 ILE A 107 0
SHEET 2 AC 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AC 4 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 4 AC 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AD 4 THR A 152 TRP A 157 0
SHEET 2 AD 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 AD 4 ASP A 171 LYS A 175 -1 O ASP A 171 N TRP A 168
SHEET 4 AD 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AE 2 ILE A 194 ASN A 196 0
SHEET 2 AE 2 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 1 AF 2 LEU A 214 TRP A 216 0
SHEET 2 AF 2 PHE A 222 ASN A 229 -1 O ALA A 224 N TRP A 215
SHEET 1 AG 4 SER A 284 ILE A 287 0
SHEET 2 AG 4 THR A 265 ASN A 272 -1 O PHE A 268 N ILE A 287
SHEET 3 AG 4 PHE A 222 ASN A 229 -1 O LEU A 223 N VAL A 271
SHEET 4 AG 4 LEU A 214 TRP A 216 -1 O TRP A 215 N ALA A 224
SHEET 1 AH 4 SER A 284 ILE A 287 0
SHEET 2 AH 4 THR A 265 ASN A 272 -1 O PHE A 268 N ILE A 287
SHEET 3 AH 4 PHE A 222 ASN A 229 -1 O LEU A 223 N VAL A 271
SHEET 4 AH 4 ILE A 194 ASN A 196 -1 O TYR A 195 N PHE A 228
SHEET 1 AI 2 LEU A 235 PHE A 240 0
SHEET 2 AI 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AJ 4 HIS A 298 THR A 307 0
SHEET 2 AJ 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AJ 4 TYR A 322 TYR A 330 -1 O TYR A 322 N ARG A 317
SHEET 4 AJ 4 TRP A 337 CYS A 339 1 O ASN A 338 N ASP A 329
SHEET 1 AK 4 HIS A 298 THR A 307 0
SHEET 2 AK 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AK 4 TYR A 322 TYR A 330 -1 O TYR A 322 N ARG A 317
SHEET 4 AK 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 AL 2 TRP A 337 CYS A 339 0
SHEET 2 AL 2 TYR A 322 TYR A 330 1 O ASP A 329 N ASN A 338
SHEET 1 AM 4 HIS A 363 PHE A 364 0
SHEET 2 AM 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AM 4 ARG A 382 GLN A 388 -1 O HIS A 383 N ILE A 375
SHEET 4 AM 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AN 4 VAL A 404 LEU A 410 0
SHEET 2 AN 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 AN 4 ASN A 430 GLN A 435 -1 O ASN A 430 N SER A 419
SHEET 4 AN 4 ASP A 438 CYS A 444 -1 N ASP A 438 O GLN A 435
SHEET 1 AO 4 TYR A 457 PHE A 461 0
SHEET 2 AO 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 AO 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AO 4 LYS A 489 GLU A 495 -1 O LYS A 489 N SER A 484
SHEET 1 AP 8 SER A 511 LEU A 519 0
SHEET 2 AP 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 AP 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AP 8 TYR A 540 ASP A 545 1 O PRO A 541 N ILE A 574
SHEET 5 AP 8 VAL A 619 TRP A 629 1 N ASP A 620 O TYR A 540
SHEET 6 AP 8 CYS A 649 VAL A 653 1 O CYS A 649 N ILE A 626
SHEET 7 AP 8 GLU A 699 GLY A 705 1 O GLU A 699 N GLY A 650
SHEET 8 AP 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 BA 2 LYS B 41 THR B 42 0
SHEET 2 BA 2 VAL B 507 GLN B 508 1 N GLN B 508 O LYS B 41
SHEET 1 BB 4 LEU B 60 TRP B 62 0
SHEET 2 BB 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 BB 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 BB 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 BC 4 ASP B 104 ILE B 107 0
SHEET 2 BC 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 BC 4 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 4 BC 4 GLN B 141 ILE B 143 -1 O GLN B 141 N ASP B 136
SHEET 1 BD 4 TRP B 154 TRP B 157 0
SHEET 2 BD 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 BD 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 BD 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 BE 2 ILE B 194 ASN B 196 0
SHEET 2 BE 2 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 1 BF 2 LEU B 214 TRP B 216 0
SHEET 2 BF 2 PHE B 222 ASN B 229 -1 O ALA B 224 N TRP B 215
SHEET 1 BG 4 ILE B 285 ILE B 287 0
SHEET 2 BG 4 THR B 265 ASN B 272 -1 O PHE B 268 N ILE B 287
SHEET 3 BG 4 PHE B 222 ASN B 229 -1 O LEU B 223 N VAL B 271
SHEET 4 BG 4 LEU B 214 TRP B 216 -1 O TRP B 215 N ALA B 224
SHEET 1 BH 4 ILE B 285 ILE B 287 0
SHEET 2 BH 4 THR B 265 ASN B 272 -1 O PHE B 268 N ILE B 287
SHEET 3 BH 4 PHE B 222 ASN B 229 -1 O LEU B 223 N VAL B 271
SHEET 4 BH 4 ILE B 194 ASN B 196 -1 O TYR B 195 N PHE B 228
SHEET 1 BI 2 LEU B 235 PHE B 240 0
SHEET 2 BI 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 BJ 4 HIS B 298 THR B 307 0
SHEET 2 BJ 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 BJ 4 TYR B 322 TYR B 330 -1 O TYR B 322 N ARG B 317
SHEET 4 BJ 4 TRP B 337 CYS B 339 1 O ASN B 338 N ASP B 329
SHEET 1 BK 4 HIS B 298 THR B 307 0
SHEET 2 BK 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 BK 4 TYR B 322 TYR B 330 -1 O TYR B 322 N ARG B 317
SHEET 4 BK 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 BL 2 TRP B 337 CYS B 339 0
SHEET 2 BL 2 TYR B 322 TYR B 330 1 O ASP B 329 N ASN B 338
SHEET 1 BM 4 HIS B 363 PHE B 364 0
SHEET 2 BM 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 BM 4 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 BM 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 BN 4 VAL B 404 LEU B 410 0
SHEET 2 BN 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 BN 4 ASN B 430 GLN B 435 -1 O ASN B 430 N SER B 419
SHEET 4 BN 4 ASP B 438 CYS B 444 -1 N ASP B 438 O GLN B 435
SHEET 1 BO 4 TYR B 457 PHE B 461 0
SHEET 2 BO 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 BO 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 BO 4 LYS B 489 GLU B 495 -1 O LYS B 489 N SER B 484
SHEET 1 BP 8 SER B 511 LEU B 519 0
SHEET 2 BP 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 BP 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 BP 8 TYR B 540 ASP B 545 1 O PRO B 541 N ILE B 574
SHEET 5 BP 8 VAL B 619 TRP B 629 1 N ASP B 620 O TYR B 540
SHEET 6 BP 8 CYS B 649 VAL B 653 1 O CYS B 649 N ILE B 626
SHEET 7 BP 8 GLU B 699 GLY B 705 1 O GLU B 699 N GLY B 650
SHEET 8 BP 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
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 2.01
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 2.06
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 2.08
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.06
LINK ND2 ASN A 85 C1 NAG A1085 1555 1555 1.43
LINK ND2 ASN A 150 C1 NAG A1150 1555 1555 1.43
LINK ND2 ASN A 219 C1 NAG A1219 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG A1229 1555 1555 1.43
LINK ND2 ASN A 281 C1 NAG A1281 1555 1555 1.43
LINK ND2 ASN A 321 C1 NAG A1321 1555 1555 1.44
LINK ND2 ASN A 520 C1 NAG A1520 1555 1555 1.43
LINK O4 NAG A1085 C1 NAG A1086 1555 1555 1.41
LINK O4 NAG A1086 C1 MAN A1087 1555 1555 1.44
LINK O6 MAN A1087 C1 MAN A1089 1555 1555 1.38
LINK O3 MAN A1087 C1 MAN A1088 1555 1555 1.42
LINK ND2 ASN B 85 C1 NAG B2085 1555 1555 1.43
LINK ND2 ASN B 150 C1 NAG B2150 1555 1555 1.43
LINK ND2 ASN B 219 C1 NAG B2219 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG B2229 1555 1555 1.43
LINK ND2 ASN B 281 C1 NAG B2281 1555 1555 1.43
LINK ND2 ASN B 321 C1 NAG B2321 1555 1555 1.43
CISPEP 1 GLY A 474 PRO A 475 0 10.28
CISPEP 2 GLY B 474 PRO B 475 0 5.35
SITE 1 AC1 15 GLU A 205 GLU A 206 ASP A 545 VAL A 546
SITE 2 AC1 15 TYR A 547 TRP A 627 GLY A 628 TRP A 629
SITE 3 AC1 15 SER A 630 TYR A 631 TYR A 662 TYR A 666
SITE 4 AC1 15 VAL A 711 HOH A3859 HOH A3862
SITE 1 AC2 3 ARG A 596 ARG A 597 HOH A3761
SITE 1 AC3 3 GLU A 146 ARG A 147 HOH A3186
SITE 1 AC4 5 ARG A 658 ARG A 684 HOH A3752 HOH A3771
SITE 2 AC4 5 GLU B 244
SITE 1 AC5 16 GLU B 205 GLU B 206 ASP B 545 VAL B 546
SITE 2 AC5 16 TYR B 547 TRP B 627 GLY B 628 TRP B 629
SITE 3 AC5 16 SER B 630 TYR B 631 TYR B 662 TYR B 666
SITE 4 AC5 16 VAL B 711 HOH B3712 HOH B3714 HOH B3715
SITE 1 AC6 4 THR B 144 GLU B 145 GLU B 146 ARG B 147
SITE 1 AC7 2 ARG B 596 ARG B 597
SITE 1 AC8 4 GLU A 244 ARG B 658 ARG B 684 HOH B3643
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 A1520 HOH A3056 HOH A3081
SITE 4 AC9 26 HOH A3082 HOH A3650 HOH A3651 HOH A3863
SITE 5 AC9 26 HOH A3864 HOH A3865 HOH A3866 HOH A3867
SITE 6 AC9 26 HOH A3868 HOH A3870 HOH A3871 HOH A3872
SITE 7 AC9 26 HOH A3873 LYS B 391
SITE 1 BC1 3 ARG A 147 ASN A 150 HOH A3187
SITE 1 BC2 5 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 2 BC2 5 HOH A3288
SITE 1 BC3 7 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 BC3 7 HOH A3296 HOH A3299 HOH A3300
SITE 1 BC4 5 TRP A 187 VAL A 279 ASN A 281 HOH A3380
SITE 2 BC4 5 HOH A3877
SITE 1 BC5 9 ILE A 319 ASN A 321 MET A 348 SER A 349
SITE 2 BC5 9 THR A 350 ARG A 596 HOH A3448 ARG B 140
SITE 3 BC5 9 HOH B3150
SITE 1 BC6 6 ASN A 520 ARG A 581 ASP A 605 MAN A1089
SITE 2 BC6 6 HOH A3309 HOH A3878
SITE 1 BC7 5 VAL B 78 ASN B 85 SER B 86 SER B 87
SITE 2 BC7 5 HOH B3043
SITE 1 BC8 7 ARG B 147 ILE B 148 ASN B 150 HOH B3093
SITE 2 BC8 7 HOH B3161 HOH B3162 HOH B3716
SITE 1 BC9 6 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC9 6 HOH B3252 HOH B3717
SITE 1 CC1 7 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 CC1 7 HOH B3259 HOH B3262 HOH B3718
SITE 1 CC2 4 TRP B 187 VAL B 279 ASN B 281 HOH B3320
SITE 1 CC3 5 ASN B 321 MET B 348 SER B 349 THR B 350
SITE 2 CC3 5 HOH B3606
CRYST1 97.183 121.424 190.699 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 0.010290 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008236 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005244 0.00000
TER 6009 ALA A 767
TER 12060 HIS B 773
MASTER 498 0 25 35 116 0 45 613990 2 366 114
END
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