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HEADER HYDROLASE/HYDROLASE INHIBITOR 04-DEC-12 3W2T
TITLE CRYSTAL STRUCTURE OF HUMAN DEPIPTIDYL PEPTIDASE IV (DPP-4) IN COMPLEX
TITLE 2 WITH VILDAGLIPTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 33-766;
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;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPRESSF+;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPSC8
KEYWDS ALPHA/BETA, BETA-PROPELLER, HYDROLASE, AMINOPEPTIDASE, SERINE
KEYWDS 2 PROTEASE, SECRETED, SIGNAL-ANCHOR, TRANSMEMBRANE, DIABETES,
KEYWDS 3 GLYCOPROTEIN, CELL MEMBRANE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KISHIDA,M.NABENO,I.MIYAGUCHI,Y.TANAKA,R.KATOU,F.AKAHOSHI
REVDAT 1 15-MAY-13 3W2T 0
JRNL AUTH M.NABENO,F.AKAHOSHI,H.KISHIDA,I.MIYAGUCHI,Y.TANAKA,S.ISHII,
JRNL AUTH 2 T.KADOWAKI
JRNL TITL A COMPARATIVE STUDY OF THE BINDING MODES OF RECENTLY
JRNL TITL 2 LAUNCHED DIPEPTIDYL PEPTIDASE IV INHIBITORS IN THE ACTIVE
JRNL TITL 3 SITE
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 434 191 2013
JRNL REFN ISSN 0006-291X
JRNL PMID 23501107
JRNL DOI 10.1016/J.BBRC.2013.03.010
REMARK 2
REMARK 2 RESOLUTION. 2.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 78227
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4103
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.36
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.42
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5407
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 265
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11942
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 342
REMARK 3 SOLVENT ATOMS : 1027
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.16000
REMARK 3 B22 (A**2) : 1.12000
REMARK 3 B33 (A**2) : 1.04000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.319
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.231
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.142
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12665 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17251 ; 1.319 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1452 ; 6.226 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 618 ;33.777 ;23.981
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1994 ;15.237 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;20.782 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1864 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9682 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7262 ; 0.611 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11770 ; 1.174 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5403 ; 1.772 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5481 ; 2.928 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3W2T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-12.
REMARK 100 THE RCSB ID CODE IS RCSB095814.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82418
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.360
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.23400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.960
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3VJM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.18M SODIUM ACETATE,
REMARK 280 0.18M GLYCINE-SODIUM HYDROXIDE, PH 8.8, VAPOR DIFFUSION, SITTING
REMARK 280 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 59.10800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.54450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.11850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.54450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.10800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.11850
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: 10880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 61.0 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 ASP A 33
REMARK 465 ASP A 34
REMARK 465 ALA A 35
REMARK 465 THR A 36
REMARK 465 ALA A 37
REMARK 465 HIS A 767
REMARK 465 HIS A 768
REMARK 465 HIS A 769
REMARK 465 HIS A 770
REMARK 465 HIS A 771
REMARK 465 HIS A 772
REMARK 465 ASP B 33
REMARK 465 ASP B 34
REMARK 465 ALA B 35
REMARK 465 THR B 36
REMARK 465 ALA B 37
REMARK 465 HIS B 767
REMARK 465 HIS B 768
REMARK 465 HIS B 769
REMARK 465 HIS B 770
REMARK 465 HIS B 771
REMARK 465 HIS B 772
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 -162.43 -160.14
REMARK 500 GLU A 73 56.98 38.94
REMARK 500 ASN A 74 -1.36 59.12
REMARK 500 ASN A 92 -8.82 -59.69
REMARK 500 GLN A 123 -105.93 -109.10
REMARK 500 TRP A 124 -145.36 -92.20
REMARK 500 HIS A 162 30.58 -149.67
REMARK 500 ILE A 193 -61.78 -125.54
REMARK 500 SER A 242 -167.01 71.36
REMARK 500 GLN A 320 36.07 -77.72
REMARK 500 ARG A 358 157.61 179.63
REMARK 500 ASN A 450 83.73 -158.10
REMARK 500 GLU A 495 119.57 -161.55
REMARK 500 TYR A 547 -77.54 -126.81
REMARK 500 ARG A 596 9.34 59.87
REMARK 500 THR A 600 -93.86 -122.93
REMARK 500 SER A 630 -107.72 55.80
REMARK 500 ASP A 678 -91.87 -108.95
REMARK 500 ASN A 710 -73.12 -99.92
REMARK 500 ASP A 739 -159.44 -97.01
REMARK 500 ILE A 742 52.57 32.25
REMARK 500 TYR B 58 84.97 -151.75
REMARK 500 ASN B 74 -10.28 70.67
REMARK 500 GLN B 123 -99.77 -106.18
REMARK 500 TRP B 124 -145.54 -95.92
REMARK 500 HIS B 162 33.51 -157.61
REMARK 500 GLU B 191 130.22 -38.11
REMARK 500 ASP B 192 9.13 59.42
REMARK 500 ILE B 193 -61.57 -129.90
REMARK 500 SER B 242 -160.69 61.31
REMARK 500 GLN B 320 32.37 -81.07
REMARK 500 ALA B 342 -9.20 -57.50
REMARK 500 ASN B 450 80.86 -163.03
REMARK 500 ASN B 520 50.59 38.63
REMARK 500 TYR B 547 -73.00 -124.86
REMARK 500 ARG B 597 43.52 -141.01
REMARK 500 THR B 600 -95.19 -119.36
REMARK 500 SER B 630 -104.50 52.65
REMARK 500 ASP B 678 -88.95 -118.89
REMARK 500 ASN B 710 -75.07 -97.01
REMARK 500 GLN B 714 -46.02 -28.32
REMARK 500 ASP B 739 -154.67 -87.88
REMARK 500 ILE B 742 57.48 36.27
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 LF7 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LF7 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES A 803 to 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES A 807 to 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES A 810 to 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES A 812 to 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES B 803 to 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES B 806 to 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES B 808 to 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES B 811 to 812
DBREF 3W2T A 33 766 UNP P27487 DPP4_HUMAN 33 766
DBREF 3W2T B 33 766 UNP P27487 DPP4_HUMAN 33 766
SEQADV 3W2T HIS A 767 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS A 768 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS A 769 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS A 770 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS A 771 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS A 772 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS B 767 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS B 768 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS B 769 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS B 770 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS B 771 UNP P27487 EXPRESSION TAG
SEQADV 3W2T HIS B 772 UNP P27487 EXPRESSION TAG
SEQRES 1 A 740 ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR THR LEU
SEQRES 2 A 740 THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR
SEQRES 3 A 740 SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS
SEQRES 4 A 740 GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY
SEQRES 5 A 740 ASN SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU
SEQRES 6 A 740 PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP
SEQRES 7 A 740 GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN
SEQRES 8 A 740 TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP
SEQRES 9 A 740 LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO
SEQRES 10 A 740 ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS
SEQRES 11 A 740 LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS
SEQRES 12 A 740 ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR
SEQRES 13 A 740 GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP
SEQRES 14 A 740 VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU
SEQRES 15 A 740 TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN
SEQRES 16 A 740 PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE
SEQRES 17 A 740 TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG
SEQRES 18 A 740 VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL
SEQRES 19 A 740 LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL
SEQRES 20 A 740 THR ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER
SEQRES 21 A 740 MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP
SEQRES 22 A 740 ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG
SEQRES 23 A 740 ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP
SEQRES 24 A 740 GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN
SEQRES 25 A 740 HIS ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE
SEQRES 26 A 740 ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER
SEQRES 27 A 740 PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS
SEQRES 28 A 740 ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE
SEQRES 29 A 740 ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA
SEQRES 30 A 740 LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR
SEQRES 31 A 740 LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN
SEQRES 32 A 740 LEU SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU
SEQRES 33 A 740 LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE
SEQRES 34 A 740 SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY
SEQRES 35 A 740 PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN
SEQRES 36 A 740 ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU
SEQRES 37 A 740 ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS
SEQRES 38 A 740 LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR
SEQRES 39 A 740 GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS
SEQRES 40 A 740 TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER
SEQRES 41 A 740 GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR
SEQRES 42 A 740 TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE
SEQRES 43 A 740 ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET
SEQRES 44 A 740 HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU
SEQRES 45 A 740 ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY
SEQRES 46 A 740 PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER
SEQRES 47 A 740 TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY
SEQRES 48 A 740 SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL
SEQRES 49 A 740 SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG
SEQRES 50 A 740 TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS
SEQRES 51 A 740 TYR ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE
SEQRES 52 A 740 LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP
SEQRES 53 A 740 ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS
SEQRES 54 A 740 ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP
SEQRES 55 A 740 TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA
SEQRES 56 A 740 HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS
SEQRES 57 A 740 GLN CYS PHE SER LEU PRO HIS HIS HIS HIS HIS HIS
SEQRES 1 B 740 ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR THR LEU
SEQRES 2 B 740 THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR
SEQRES 3 B 740 SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS
SEQRES 4 B 740 GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY
SEQRES 5 B 740 ASN SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU
SEQRES 6 B 740 PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP
SEQRES 7 B 740 GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN
SEQRES 8 B 740 TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP
SEQRES 9 B 740 LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO
SEQRES 10 B 740 ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS
SEQRES 11 B 740 LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS
SEQRES 12 B 740 ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR
SEQRES 13 B 740 GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP
SEQRES 14 B 740 VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU
SEQRES 15 B 740 TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN
SEQRES 16 B 740 PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE
SEQRES 17 B 740 TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG
SEQRES 18 B 740 VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL
SEQRES 19 B 740 LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL
SEQRES 20 B 740 THR ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER
SEQRES 21 B 740 MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP
SEQRES 22 B 740 ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG
SEQRES 23 B 740 ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP
SEQRES 24 B 740 GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN
SEQRES 25 B 740 HIS ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE
SEQRES 26 B 740 ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER
SEQRES 27 B 740 PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS
SEQRES 28 B 740 ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE
SEQRES 29 B 740 ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA
SEQRES 30 B 740 LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR
SEQRES 31 B 740 LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN
SEQRES 32 B 740 LEU SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU
SEQRES 33 B 740 LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE
SEQRES 34 B 740 SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY
SEQRES 35 B 740 PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN
SEQRES 36 B 740 ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU
SEQRES 37 B 740 ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS
SEQRES 38 B 740 LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR
SEQRES 39 B 740 GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS
SEQRES 40 B 740 TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER
SEQRES 41 B 740 GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR
SEQRES 42 B 740 TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE
SEQRES 43 B 740 ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET
SEQRES 44 B 740 HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU
SEQRES 45 B 740 ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY
SEQRES 46 B 740 PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER
SEQRES 47 B 740 TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY
SEQRES 48 B 740 SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL
SEQRES 49 B 740 SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG
SEQRES 50 B 740 TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS
SEQRES 51 B 740 TYR ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE
SEQRES 52 B 740 LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP
SEQRES 53 B 740 ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS
SEQRES 54 B 740 ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP
SEQRES 55 B 740 TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA
SEQRES 56 B 740 HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS
SEQRES 57 B 740 GLN CYS PHE SER LEU PRO HIS HIS HIS HIS HIS HIS
MODRES 3W2T ASN A 321 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN B 219 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN B 321 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN A 281 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN A 92 ASN GLYCOSYLATION SITE
MODRES 3W2T ASN B 281 ASN GLYCOSYLATION SITE
HET LF7 A 801 22
HET GOL A 802 6
HET NAG A 803 14
HET FUL A 804 10
HET NAG A 805 14
HET NAG A 806 14
HET NAG A 807 14
HET NAG A 808 14
HET NAG A 809 14
HET NAG A 810 14
HET NAG A 811 14
HET NAG A 812 14
HET NAG A 813 14
HET LF7 B 801 22
HET GOL B 802 6
HET NAG B 803 14
HET FUL B 804 10
HET NAG B 805 14
HET NAG B 806 14
HET NAG B 807 14
HET NAG B 808 14
HET NAG B 809 14
HET NAG B 810 14
HET NAG B 811 14
HET NAG B 812 14
HETNAM LF7 (2S)-1-{N-[(1R,3S,5R,7S)-3-HYDROXYTRICYCLO[3.3.1.1~3,
HETNAM 2 LF7 7~]DEC-1-YL]GLYCYL}PYRROLIDINE-2-CARBONITRILE
HETNAM GOL GLYCEROL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETSYN LF7 VILDAGLIPTIN
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 3 LF7 2(C17 H25 N3 O2)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 5 NAG 19(C8 H15 N O6)
FORMUL 5 FUL 2(C6 H12 O5)
FORMUL 20 HOH *1027(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 PHE A 95 GLY A 99 5 5
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 ASN A 506 1 10
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 MET A 616 1 17
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 SER A 764 1 21
HELIX 20 20 THR B 44 ASN B 51 1 8
HELIX 21 21 ASP B 200 VAL B 207 1 8
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 VAL B 341 GLN B 344 5 4
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 ASN B 497 GLN B 505 1 9
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 LYS B 615 1 16
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ARG B 658 TYR B 662 5 5
HELIX 32 32 ASP B 663 GLY B 672 1 10
HELIX 33 33 ASN B 679 SER B 686 1 8
HELIX 34 34 VAL B 688 VAL B 698 5 11
HELIX 35 35 HIS B 712 VAL B 726 1 15
HELIX 36 36 SER B 744 SER B 764 1 21
SHEET 1 A 4 ARG A 61 TRP A 62 0
SHEET 2 A 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 A 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 B 4 ILE A 102 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 B 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 TRP A 154 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 C 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 D 3 ILE A 194 ASN A 196 0
SHEET 2 D 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 D 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 E 4 ILE A 194 ASN A 196 0
SHEET 2 E 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 4 THR A 265 ASN A 272 -1 O LYS A 267 N GLN A 227
SHEET 4 E 4 SER A 284 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 G 4 HIS A 298 THR A 307 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 G 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 G 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
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 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 I 4 HIS A 363 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 J 4 VAL A 404 LEU A 410 0
SHEET 2 J 4 TYR A 414 SER A 419 -1 O ILE A 418 N ILE A 405
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 K 4 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 K 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 K 4 LYS A 489 GLU A 495 -1 O LEU A 491 N LEU A 482
SHEET 1 L 8 SER A 511 LEU A 519 0
SHEET 2 L 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 L 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 L 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 L 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 L 8 GLU A 699 GLY A 705 1 O GLU A 699 N GLY A 650
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 M 2 LYS B 41 THR B 42 0
SHEET 2 M 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 N 4 LEU B 60 TRP B 62 0
SHEET 2 N 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 N 4 ASN B 75 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 N 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 O 4 ASP B 104 ILE B 107 0
SHEET 2 O 4 PHE B 113 LYS B 122 -1 O GLU B 117 N ASP B 104
SHEET 3 O 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 O 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 P 4 TRP B 154 TRP B 157 0
SHEET 2 P 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 P 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 P 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 Q 3 ILE B 194 ASN B 196 0
SHEET 2 Q 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 R 4 ILE B 194 ASN B 196 0
SHEET 2 R 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 4 THR B 265 ASN B 272 -1 O THR B 265 N ASN B 229
SHEET 4 R 4 SER B 284 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 S 2 LEU B 235 PHE B 240 0
SHEET 2 S 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 T 4 HIS B 298 TRP B 305 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 T 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 T 4 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 1 U 4 HIS B 298 TRP B 305 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 U 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 U 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 V 4 HIS B 363 PHE B 364 0
SHEET 2 V 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 V 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 V 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 W 4 VAL B 404 LEU B 410 0
SHEET 2 W 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 W 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 W 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 X 4 CYS B 454 PHE B 461 0
SHEET 2 X 4 TYR B 467 PRO B 475 -1 O GLY B 474 N GLN B 455
SHEET 3 X 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 X 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Y 8 SER B 511 LEU B 519 0
SHEET 2 Y 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Y 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Y 8 TYR B 540 ASP B 545 1 N ASP B 545 O ALA B 576
SHEET 5 Y 8 VAL B 619 TRP B 629 1 O ASP B 620 N TYR B 540
SHEET 6 Y 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Y 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Y 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 2.06
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.06
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.05
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.08
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.07
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.06
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.08
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.02
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.08
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.07
LINK ND2 ASN A 321 C1 NAG A 812 1555 1555 1.43
LINK ND2 ASN A 219 C1 NAG A 807 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG A 809 1555 1555 1.44
LINK ND2 ASN B 219 C1 NAG B 806 1555 1555 1.44
LINK ND2 ASN B 321 C1 NAG B 811 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG B 808 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG A 810 1555 1555 1.44
LINK O4 NAG A 810 C1 NAG A 811 1555 1555 1.44
LINK O4 NAG B 808 C1 NAG B 809 1555 1555 1.44
LINK O4 NAG A 812 C1 NAG A 813 1555 1555 1.44
LINK ND2 ASN A 85 C1 NAG A 803 1555 1555 1.44
LINK O4 NAG A 807 C1 NAG A 808 1555 1555 1.44
LINK ND2 ASN B 85 C1 NAG B 803 1555 1555 1.44
LINK O4 NAG B 811 C1 NAG B 812 1555 1555 1.45
LINK O6 NAG A 803 C1 FUL A 804 1555 1555 1.45
LINK O4 NAG B 806 C1 NAG B 807 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A 806 1555 1555 1.45
LINK O6 NAG B 803 C1 FUL B 804 1555 1555 1.46
LINK ND2 ASN B 150 C1 NAG B 805 1555 1555 1.46
LINK ND2 ASN A 92 C1 NAG A 805 1555 1555 1.46
LINK ND2 ASN B 281 C1 NAG B 810 1555 1555 1.46
LINK OG SER A 630 C20 LF7 A 801 1555 1555 1.45
LINK OG SER B 630 C20 LF7 B 801 1555 1555 1.44
CISPEP 1 GLY A 474 PRO A 475 0 7.43
CISPEP 2 GLY B 474 PRO B 475 0 7.78
SITE 1 AC1 13 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC1 13 SER A 630 TYR A 631 VAL A 656 TYR A 662
SITE 3 AC1 13 TYR A 666 ASN A 710 HOH A2006 HOH A2075
SITE 4 AC1 13 HOH A2211
SITE 1 AC2 8 GLY A 352 TRP A 353 ASN A 595 ARG A 596
SITE 2 AC2 8 ARG A 669 GLY A 672 NAG A 812 HOH A2327
SITE 1 AC3 4 GLU A 73 ASN A 74 ASN A 75 ASN A 92
SITE 1 AC4 3 ARG A 147 ILE A 148 ASN A 150
SITE 1 AC5 5 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC5 5 HOH A2067
SITE 1 AC6 13 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 AC6 13 SER B 630 TYR B 631 VAL B 656 TYR B 662
SITE 3 AC6 13 TYR B 666 ASN B 710 HOH B 954 HOH B 973
SITE 4 AC6 13 HOH B1029
SITE 1 AC7 7 GLN B 320 GLY B 352 ASN B 595 ARG B 596
SITE 2 AC7 7 ARG B 669 GLY B 672 HOH B1002
SITE 1 AC8 3 ARG B 147 ILE B 148 ASN B 150
SITE 1 AC9 2 VAL B 279 ASN B 281
SITE 1 BC1 6 VAL A 78 TYR A 83 ASN A 85 SER A 86
SITE 2 BC1 6 SER A 87 HOH A2131
SITE 1 BC2 9 ASN A 219 THR A 221 ASN A 272 GLN A 308
SITE 2 BC2 9 GLU A 309 TYR A 330 GLU A 332 HOH A2148
SITE 3 BC2 9 HOH A2399
SITE 1 BC3 7 TRP A 187 THR A 188 ASN A 281 HOH A2072
SITE 2 BC3 7 HOH A2169 HOH A2340 HOH A2348
SITE 1 BC4 5 ASN A 321 MET A 348 SER A 349 THR A 350
SITE 2 BC4 5 GOL A 802
SITE 1 BC5 7 ASN A 179 GLU B 67 ASN B 80 ASN B 85
SITE 2 BC5 7 SER B 86 SER B 87 HOH B1056
SITE 1 BC6 8 ASN B 219 THR B 221 ASN B 272 GLN B 308
SITE 2 BC6 8 GLU B 309 TYR B 330 GLU B 332 HOH B1200
SITE 1 BC7 6 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 BC7 6 HOH B1235 HOH B1258
SITE 1 BC8 4 ASN B 321 SER B 349 ARG B 596 ASP B 678
CRYST1 118.216 126.237 137.089 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 0.008459 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007922 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007295 0.00000
TER 5972 PRO A 766
TER 11944 PRO B 766
MASTER 391 0 25 36 100 0 34 613311 2 377 114
END |