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HEADER HYDROLASE/HYDROLASE INHIBITOR 15-MAR-16 5ISM
TITLE HUMAN DPP4 IN COMPLEX WITH A NOVEL 5,5,6-TRICYCLIC PYRROLIDINE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADABP,ADENOSINE DEAMINASE COMPLEXING PROTEIN 2,ADCP-2,
COMPND 5 DIPEPTIDYL PEPTIDASE IV,DPP IV,T-CELL ACTIVATION ANTIGEN CD26,TP103;
COMPND 6 EC: 3.4.14.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS STRUCTURE-BASED DRUG DESIGN, DIABETES, DPP4 INHIBITORS, HYDROLASE,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SCAPIN
REVDAT 1 11-MAY-16 5ISM 0
JRNL AUTH J.M.COX,H.D.CHU,J.T.KUETHE,Y.D.GAO,G.SCAPIN,G.EIERMANN,H.HE,
JRNL AUTH 2 X.LI,K.A.LYONS,J.METZGER,A.PETROV,J.K.WU,S.XU,R.SINHA-ROY,
JRNL AUTH 3 A.E.WEBER,T.BIFTU
JRNL TITL THE DISCOVERY OF NOVEL 5,6,5- AND 5,5,6-TRICYCLIC
JRNL TITL 2 PYRROLIDINES AS POTENT AND SELECTIVE DPP-4 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. 2016
JRNL REFN ESSN 1464-3405
JRNL PMID 27106708
JRNL DOI 10.1016/J.BMCL.2016.04.020
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 131330
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6939
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9611
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.1930
REMARK 3 BIN FREE R VALUE SET COUNT : 489
REMARK 3 BIN FREE R VALUE : 0.2140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 307
REMARK 3 SOLVENT ATOMS : 1665
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : 0.00000
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): 0.146
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.118
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12768 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 11460 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17438 ; 1.368 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 26297 ; 1.226 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1454 ; 6.158 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 631 ;34.123 ;23.978
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2040 ;12.808 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 63 ;17.904 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1865 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14605 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3134 ; 0.001 ; 0.020
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): 5822 ; 1.289 ; 2.176
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5821 ; 1.288 ; 2.175
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7274 ; 2.093 ; 3.255
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7275 ; 2.093 ; 3.256
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6946 ; 1.812 ; 2.495
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6947 ; 1.812 ; 2.494
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 10122 ; 2.967 ; 3.652
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 16325 ; 5.694 ;19.467
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 15360 ; 5.186 ;18.726
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5ISM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219333.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-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) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140437
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.28100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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 (%): 59.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG4000, 200 MM SODIUM ACETATE,
REMARK 280 100 MM TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 59.13700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.63650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.01450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.63650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.13700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.01450
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: 9840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 SG CYS A 472 O HOH A 1374 1.91
REMARK 500 ND2 ASN A 150 O5 NAG A 802 2.05
REMARK 500 ND2 ASN A 229 O5 NAG A 805 2.07
REMARK 500 O HOH A 1024 O HOH B 1659 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 184 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 471 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 VAL B 160 CG1 - CB - CG2 ANGL. DEV. = 11.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 64 -169.16 -167.57
REMARK 500 GLN A 123 -100.46 -109.09
REMARK 500 TRP A 124 -142.95 -98.78
REMARK 500 HIS A 162 33.55 -157.74
REMARK 500 ILE A 193 -57.59 -132.10
REMARK 500 SER A 242 -164.89 67.65
REMARK 500 GLN A 320 38.67 -83.44
REMARK 500 ASN A 450 82.39 -159.05
REMARK 500 TYR A 547 -74.20 -123.71
REMARK 500 ARG A 597 47.19 -142.70
REMARK 500 THR A 600 -92.62 -120.66
REMARK 500 SER A 630 -126.67 67.53
REMARK 500 ALA A 654 57.24 39.48
REMARK 500 ASP A 678 -96.78 -110.39
REMARK 500 ASN A 710 -69.32 -97.92
REMARK 500 GLN A 714 -47.11 -29.08
REMARK 500 ASP A 739 -159.47 -101.04
REMARK 500 ILE A 742 56.76 35.80
REMARK 500 SER B 64 -168.53 -160.18
REMARK 500 GLN B 123 -101.48 -112.91
REMARK 500 TRP B 124 -146.22 -96.79
REMARK 500 ASN B 151 30.76 70.34
REMARK 500 HIS B 162 33.90 -154.82
REMARK 500 ILE B 193 -60.28 -128.24
REMARK 500 SER B 242 -165.08 66.12
REMARK 500 GLN B 320 37.98 -86.75
REMARK 500 LYS B 423 18.63 58.40
REMARK 500 ASN B 450 81.76 -157.20
REMARK 500 TYR B 547 -74.34 -121.94
REMARK 500 ARG B 596 10.75 57.71
REMARK 500 ARG B 597 48.54 -140.27
REMARK 500 THR B 600 -93.51 -121.74
REMARK 500 SER B 630 -126.49 70.06
REMARK 500 ASP B 678 -96.30 -109.98
REMARK 500 ASN B 710 -66.69 -102.13
REMARK 500 ASP B 739 -157.37 -104.37
REMARK 500 ILE B 742 54.37 36.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1730 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A1731 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A1732 DISTANCE = 6.43 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 810 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 490 O
REMARK 620 2 LEU A 491 O 84.2
REMARK 620 3 LEU B 276 O 65.1 59.5
REMARK 620 4 VAL B 279 O 64.8 57.9 1.7
REMARK 620 5 HOH B1147 O 124.5 90.0 64.7 65.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6DG A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6DG B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 801 bound
REMARK 800 to ASN A 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound
REMARK 800 to ASN A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 803 through NAG A 804 bound to ASN A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 805 through NAG A 806 bound to ASN A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 807 bound
REMARK 800 to ASN A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 808 through NAG A 809 bound to ASN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 801 through NAG B 802 bound to ASN B 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 803 through NAG B 804 bound to ASN B 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 805 through NAG B 806 bound to ASN B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 807 through NAG B 808 bound to ASN B 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 809 bound
REMARK 800 to ASN B 321
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I7U RELATED DB: PDB
DBREF 5ISM A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 5ISM B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 5ISM THR A 39 UNP P27487 SER 39 ENGINEERED MUTATION
SEQADV 5ISM THR B 39 UNP P27487 SER 39 ENGINEERED MUTATION
SEQRES 1 A 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 B 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 28
HET NAG A 807 14
HET NAG A 808 14
HET NAG A 809 14
HET NA A 810 1
HET 6DG A 811 27
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 805 14
HET NAG B 806 14
HET NAG B 807 14
HET NAG B 808 14
HET NAG B 809 14
HET 6DG B 810 54
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NA SODIUM ION
HETNAM 6DG (2R,3S,5R)-2-(2,5-DIFLUOROPHENYL)-5-(7H-PYRROLO[3',
HETNAM 2 6DG 4':3,4]PYRAZOLO[1,5-A]PYRIMIDIN-8(9H)-YL)OXAN-3-AMINE
FORMUL 3 NAG 18(C8 H15 N O6)
FORMUL 9 NA NA 1+
FORMUL 10 6DG 2(C19 H19 F2 N5 O)
FORMUL 17 HOH *1665(H2 O)
HELIX 1 AA1 THR A 44 ASN A 51 1 8
HELIX 2 AA2 GLU A 91 ASP A 96 5 6
HELIX 3 AA3 ASP A 200 VAL A 207 1 8
HELIX 4 AA4 ASP A 274 LEU A 276 5 3
HELIX 5 AA5 PRO A 290 ILE A 295 1 6
HELIX 6 AA6 VAL A 341 GLN A 344 5 4
HELIX 7 AA7 GLU A 421 MET A 425 5 5
HELIX 8 AA8 ASN A 497 GLN A 505 1 9
HELIX 9 AA9 ASN A 562 THR A 570 1 9
HELIX 10 AB1 GLY A 587 HIS A 592 1 6
HELIX 11 AB2 ALA A 593 ASN A 595 5 3
HELIX 12 AB3 THR A 600 LYS A 615 1 16
HELIX 13 AB4 SER A 630 GLY A 641 1 12
HELIX 14 AB5 ARG A 658 TYR A 662 5 5
HELIX 15 AB6 ASP A 663 GLY A 672 1 10
HELIX 16 AB7 ASN A 679 SER A 686 1 8
HELIX 17 AB8 VAL A 688 VAL A 698 5 11
HELIX 18 AB9 PHE A 713 VAL A 726 1 14
HELIX 19 AC1 SER A 744 PHE A 763 1 20
HELIX 20 AC2 THR B 44 ASN B 51 1 8
HELIX 21 AC3 PHE B 95 GLY B 99 5 5
HELIX 22 AC4 ASP B 200 VAL B 207 1 8
HELIX 23 AC5 ASP B 274 LEU B 276 5 3
HELIX 24 AC6 PRO B 290 ILE B 295 1 6
HELIX 25 AC7 VAL B 341 GLN B 344 5 4
HELIX 26 AC8 GLU B 421 MET B 425 5 5
HELIX 27 AC9 ASN B 497 ASN B 506 1 10
HELIX 28 AD1 ASN B 562 THR B 570 1 9
HELIX 29 AD2 GLY B 587 HIS B 592 1 6
HELIX 30 AD3 ALA B 593 ASN B 595 5 3
HELIX 31 AD4 THR B 600 LYS B 615 1 16
HELIX 32 AD5 SER B 630 GLY B 641 1 12
HELIX 33 AD6 ARG B 658 TYR B 662 5 5
HELIX 34 AD7 ASP B 663 GLY B 672 1 10
HELIX 35 AD8 ASN B 679 SER B 686 1 8
HELIX 36 AD9 VAL B 688 VAL B 698 5 11
HELIX 37 AE1 HIS B 712 VAL B 726 1 15
HELIX 38 AE2 SER B 744 PHE B 763 1 20
SHEET 1 AA1 2 LYS A 41 THR A 42 0
SHEET 2 AA1 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 AA2 4 ARG A 61 TRP A 62 0
SHEET 2 AA2 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AA2 4 ASN A 75 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 AA2 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 AA3 4 ILE A 102 ILE A 107 0
SHEET 2 AA3 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AA3 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 AA3 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AA4 4 TRP A 154 TRP A 157 0
SHEET 2 AA4 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 AA4 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 AA4 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA5 3 ILE A 194 ASN A 196 0
SHEET 2 AA5 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA6 4 ILE A 194 ASN A 196 0
SHEET 2 AA6 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA6 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 AA6 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 AA7 2 LEU A 235 PHE A 240 0
SHEET 2 AA7 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 AA8 4 HIS A 298 THR A 307 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AA8 4 TYR A 322 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 AA8 4 ARG A 336 CYS A 339 -1 O ARG A 336 N ASP A 331
SHEET 1 AA9 4 HIS A 298 THR A 307 0
SHEET 2 AA9 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AA9 4 TYR A 322 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 AA9 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 AB1 4 HIS A 363 PHE A 364 0
SHEET 2 AB1 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AB1 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 AB1 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB2 4 VAL A 404 LEU A 410 0
SHEET 2 AB2 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 AB2 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB2 4 ASP A 438 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB3 4 TYR A 457 PHE A 461 0
SHEET 2 AB3 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 AB3 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AB3 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB4 8 SER A 511 LEU A 519 0
SHEET 2 AB4 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 AB4 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AB4 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 AB4 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB4 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 AB4 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB5 2 LYS B 41 THR B 42 0
SHEET 2 AB5 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 AB6 4 ARG B 61 TRP B 62 0
SHEET 2 AB6 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 AB6 4 ASN B 75 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 AB6 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 AB7 4 ILE B 102 ILE B 107 0
SHEET 2 AB7 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 AB7 4 TYR B 128 ASP B 136 -1 O ASP B 133 N LEU B 116
SHEET 4 AB7 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 AB8 4 THR B 152 TRP B 157 0
SHEET 2 AB8 4 LEU B 164 TRP B 168 -1 O VAL B 167 N GLN B 153
SHEET 3 AB8 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 AB8 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 AB9 3 ILE B 194 ASN B 196 0
SHEET 2 AB9 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB9 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AC1 4 ILE B 194 ASN B 196 0
SHEET 2 AC1 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AC1 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 AC1 4 SER B 284 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 AC2 2 LEU B 235 PHE B 240 0
SHEET 2 AC2 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 AC3 4 HIS B 298 THR B 307 0
SHEET 2 AC3 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 AC3 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 AC3 4 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 1 AC4 4 HIS B 298 THR B 307 0
SHEET 2 AC4 4 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 AC4 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 AC4 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 AC5 4 HIS B 363 PHE B 364 0
SHEET 2 AC5 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC5 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 AC5 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 AC6 4 VAL B 404 LEU B 410 0
SHEET 2 AC6 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 AC6 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC6 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AC7 4 TYR B 457 PHE B 461 0
SHEET 2 AC7 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 AC7 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 AC7 4 LYS B 489 GLU B 495 -1 O LEU B 491 N LEU B 482
SHEET 1 AC8 8 SER B 511 LEU B 519 0
SHEET 2 AC8 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 AC8 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 AC8 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 AC8 8 VAL B 619 TRP B 629 1 O TRP B 627 N VAL B 546
SHEET 6 AC8 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 AC8 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 AC8 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.07
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.10
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.01
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.11
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.10
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.08
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.05
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.11
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.09
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A 802 1555 1555 1.35
LINK ND2 ASN A 219 C1 NAG A 803 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG A 805 1555 1555 1.23
LINK ND2 ASN A 281 C1 NAG A 807 1555 1555 1.45
LINK ND2 ASN A 321 C1 NAG A 808 1555 1555 1.44
LINK O GLY A 490 NA NA A 810 1555 1555 2.39
LINK O LEU A 491 NA NA A 810 1555 1555 2.54
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.45
LINK ND2 ASN B 219 C1 NAG B 803 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG B 805 1555 1555 1.44
LINK ND2 ASN B 281 C1 NAG B 807 1555 1555 1.46
LINK ND2 ASN B 321 C1 NAG B 809 1555 1555 1.45
LINK O4 NAG A 803 C1 NAG A 804 1555 1555 1.44
LINK O4 NAG A 805 C1 NAG A 806 1555 1555 1.40
LINK O4 NAG A 808 C1 NAG A 809 1555 1555 1.44
LINK O4 NAG B 801 C1 NAG B 802 1555 1555 1.45
LINK O4 NAG B 803 C1 NAG B 804 1555 1555 1.44
LINK O4 NAG B 805 C1 NAG B 806 1555 1555 1.44
LINK O4 NAG B 807 C1 NAG B 808 1555 1555 1.43
LINK O LEU B 276 NA NA A 810 1555 2564 2.27
LINK O VAL B 279 NA NA A 810 1555 2564 2.24
LINK NA NA A 810 O HOH B1147 1555 2565 2.46
CISPEP 1 GLY A 474 PRO A 475 0 8.53
CISPEP 2 GLY B 474 PRO B 475 0 7.38
SITE 1 AC1 5 GLY A 490 LEU A 491 LEU B 276 VAL B 279
SITE 2 AC1 5 HOH B1147
SITE 1 AC2 16 ARG A 125 GLU A 205 GLU A 206 PHE A 357
SITE 2 AC2 16 TYR A 547 SER A 630 TYR A 631 TYR A 662
SITE 3 AC2 16 TYR A 666 ASN A 710 VAL A 711 HIS A 740
SITE 4 AC2 16 HOH A 949 HOH A1018 HOH A1058 HOH A1100
SITE 1 AC3 16 ARG B 125 GLU B 205 GLU B 206 PHE B 357
SITE 2 AC3 16 ARG B 358 TYR B 547 SER B 630 TYR B 631
SITE 3 AC3 16 TRP B 659 TYR B 662 TYR B 666 ASN B 710
SITE 4 AC3 16 VAL B 711 HIS B 740 HOH B 960 HOH B 989
SITE 1 AC4 8 GLU A 67 VAL A 78 ASN A 85 SER A 86
SITE 2 AC4 8 SER A 87 HOH A 914 HOH A1101 HOH A1241
SITE 1 AC5 4 ILE A 148 PRO A 149 ASN A 150 HOH A 934
SITE 1 AC6 11 ASN A 219 THR A 221 PHE A 222 GLN A 308
SITE 2 AC6 11 GLU A 309 TYR A 330 GLU A 332 HOH A1059
SITE 3 AC6 11 HOH A1152 HOH A1259 HOH A1510
SITE 1 AC7 7 ASN A 229 THR A 231 GLU A 232 HOH A 937
SITE 2 AC7 7 HOH A1303 HOH A1409 HOH A1431
SITE 1 AC8 3 VAL A 279 ASN A 281 HOH A 903
SITE 1 AC9 4 ASN A 321 SER A 349 HOH A1104 HOH A1486
SITE 1 AD1 7 VAL B 78 ASN B 85 SER B 86 SER B 87
SITE 2 AD1 7 HOH B 963 HOH B1013 HOH B1438
SITE 1 AD2 11 ASN B 219 THR B 221 ASN B 272 GLN B 308
SITE 2 AD2 11 GLU B 309 TYR B 330 HOH B 964 HOH B1041
SITE 3 AD2 11 HOH B1116 HOH B1269 HOH B1395
SITE 1 AD3 8 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 AD3 8 HOH B 932 HOH B 965 HOH B1004 HOH B1408
SITE 1 AD4 10 ASN A 450 TRP B 187 THR B 188 ASN B 281
SITE 2 AD4 10 HOH B 903 HOH B 915 HOH B 921 HOH B 957
SITE 3 AD4 10 HOH B1297 HOH B1318
SITE 1 AD5 5 ASN B 321 SER B 349 THR B 350 HOH B1023
SITE 2 AD5 5 HOH B1393
CRYST1 118.274 126.029 137.273 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 0.008455 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007935 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007285 0.00000
TER 6013 PRO A 766
TER 12020 PRO B 766
MASTER 427 0 21 38 102 0 32 613902 2 382 112
END |