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HEADER COMPLEX (HYDROLASE/INHIBITOR) 09-JUN-05 2BUB
TITLE CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (CD26)
TITLE 2 IN COMPLEX WITH A REVERSED AMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL
COMPND 4 ACTIVATION ANTIGEN CD26, TP103, ADENOSINE DEAMINASE
COMPND 5 COMPLEXING PROTEIN-2;
COMPND 6 CHAIN: A, B;
COMPND 7 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 39-766;
COMPND 8 EC: 3.4.14.5;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: PICHIA METHANOLICA;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN
KEYWDS DPP-IV, DIABETES MELLITUS, DRUG DESIGN, HYDROLASE, SERINE
KEYWDS 2 PROTEASE, AMINOPEPTIDASE, GLYCOPROTEIN, PROTEASE,
KEYWDS 3 SIGNAL-ANCHOR, TRANSMEMBRANE, COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NORDHOFF,S.CEREZO-GALVEZ,A.FEURER,O.HILL,V.G.MATASSA,
AUTHOR 2 G.METZ,C.RUMMEY,M.THIEMANN,P.J.EDWARDS
REVDAT 1 23-JAN-06 2BUB 0
JRNL AUTH S.NORDHOFF,S.CEREZO-GALVEZ,A.FEURER,O.HILL,
JRNL AUTH 2 V.G.MATASSA,G.METZ,C.RUMMEY,M.THIEMANN,P.J.EDWARDS
JRNL TITL THE REVERSED BINDING OF B-PHENETHYLAMINE
JRNL TITL 2 INHIBITORS OF DPP-IV. X-RAY STRUCTURES AND
JRNL TITL 3 PROPERTIES OF NOVEL FRAGMENT AND ELABORATED
JRNL TITL 4 INHIBITORS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.62
REMARK 3 NUMBER OF REFLECTIONS : 51392
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) : 0.26006
REMARK 3 R VALUE (WORKING SET) : 0.25777
REMARK 3 FREE R VALUE : 0.32891
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1644
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) : 2.660
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.728
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3748
REMARK 3 BIN R VALUE (WORKING SET) : 0.336
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.417
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11926
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 168
REMARK 3 SOLVENT ATOMS : 320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.697
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.61
REMARK 3 B22 (A**2) : 8.12
REMARK 3 B33 (A**2) : -4.51
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.879
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.440
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.365
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.806
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.899
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.826
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 12460 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 16956 ; 1.532 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1454 ; 7.409 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1794 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 9590 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 6453 ; 0.322 ; 1.000
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 632 ; 0.209 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 46 ; 0.330 ; 1.000
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 7 ; 0.179 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 7252 ; 0.583 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 11766 ; 1.112 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 5208 ; 1.534 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 5190 ; 2.524 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF 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 : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2BUB COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 9-JUN-2005.
REMARK 100 THE EBI ID CODE IS EBI-24441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DESY-EMBL,HAMBURG
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97928
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53440
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.66
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 1.98
REMARK 200 R MERGE (I) : 0.00
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 32.74300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 212.70350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.38650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 212.70350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.74300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.38650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A
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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 INVOLVED IN T CELL ACTIVATION
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 60 CA - CB - CG ANGL. DEV. = 12.1 DEGREES
REMARK 500 LYS A 139 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 SER A 209 N - CA - C ANGL. DEV. = -12.0 DEGREES
REMARK 500 ILE A 375 N - CA - C ANGL. DEV. = -10.7 DEGREES
REMARK 500 LEU A 436 CA - CB - CG ANGL. DEV. = -15.8 DEGREES
REMARK 500 VAL A 546 CB - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 LEU B 57 CA - CB - CG ANGL. DEV. = 10.6 DEGREES
REMARK 500 ILE B 407 N - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500 SER B 458 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET B 348 SD MET B 348 CE 0.153
REMARK 500
REMARK 500 REMARK: NULL
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 OG1 THR A 42 OG1 THR A 570 2.18
REMARK 500 O ASP A 136 O LYS A 139 1.99
REMARK 500 O ARG A 597 CG2 THR A 600 1.92
REMARK 500 O HIS A 712 N GLN A 714 2.15
REMARK 500 N GLY B 84 NH2 ARG B 492 2.11
REMARK 500 ND2 ASN B 92 C1 NAG B 1770 1.45
REMARK 500 ND2 ASN B 150 C2 NAG B 1767 2.19
REMARK 500 OE2 GLU B 206 OD2 ASP B 663 2.19
REMARK 500 CD GLU B 361 O HOH Y 73 2.18
REMARK 500 OE2 GLU B 361 O HOH Y 73 1.72
REMARK 500 O GLY B 587 O HOH Y 127 2.17
REMARK 500 O ASN B 595 NE ARG B 597 2.17
REMARK 500 NH1 ARG B 684 O HOH Y 135 2.15
REMARK 500 O ASP B 708 O HOH Y 143 2.17
REMARK 500 O4 NAG B 1769 O HOH Y 159 2.16
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 40 -102.29 52.09
REMARK 500 GLU A 73 -116.05 36.60
REMARK 500 SER A 630 -126.47 84.31
REMARK 500 GLU B 521 -40.39 105.33
REMARK 500 SER B 630 -117.75 8.90
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 491 ARG A 492 211.51
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: FPB BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: FPB BINDING SITE FOR CHAIN B
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J2E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV
REMARK 900 RELATED ID: 1N1M RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN
REMARK 900 COMPLEX WITH ANINHIBITOR
REMARK 900 RELATED ID: 1NU6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPP-IV)
REMARK 900 RELATED ID: 1NU8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPP-IV)IN COMPLEX WITH
REMARK 900 DIPROTIN A (ILI)
REMARK 900 RELATED ID: 1PFQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL
REMARK 900 PEPTIDASE IV /CD26
REMARK 900 RELATED ID: 1R9M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV AT 2.1ANG. RESOLUTION.
REMARK 900 RELATED ID: 1R9N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV INCOMPLEX WITH A DECAPEPTIDE (
REMARK 900 TNPY) AT 2.3 ANG. RESOLUTION
REMARK 900 RELATED ID: 1RWQ RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH 5-AMINOMETHYL-6-(2,4-DICHLORO-PHENYL
REMARK 900 )-2-(3,5-DIMETHOXY-PHENYL)-PYRIMIDIN-4-
REMARK 900 YLAMINE
REMARK 900 RELATED ID: 1TK3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL
REMARK 900 PEPTIDASE IV/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: 1U8E RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 MUTANT
REMARK 900 Y547F
REMARK 900 RELATED ID: 1W1I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV
REMARK 900 (DPPIV OR CD26) IN COMPLEX WITH ADENOSINE
REMARK 900 DEAMINASE
REMARK 900 RELATED ID: 1WCY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPPIV)COMPLEX WITH DIPROTIN A
REMARK 900 RELATED ID: 1X70 RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH A BETA AMINOACID INHIBITOR
REMARK 900 RELATED ID: 2AJL RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF NOVEL BIARYL-BASED
REMARK 900 DIPEPTIDYL PEPTIDASEIV INHIBITOR
REMARK 900 RELATED ID: 2BGN RELATED DB: PDB
REMARK 900 HIV-1 TAT PROTEIN DERIVED N-TERMINAL
REMARK 900 NONAPEPTIDE TRP2-TAT(1-9) BOUND TO THE
REMARK 900 ACTIVE SITE OF DIPEPTIDYL PEPTIDASE IV (CD26
REMARK 900 )
REMARK 900 RELATED ID: 2BGR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 TAT DERIVED
REMARK 900 NONAPEPTIDES TAT(1-9) BOUND TO THE ACTIVE
REMARK 900 SITE OF DIPEPTIDYL PEPTIDASE IV (CD26)
DBREF 2BUB A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2BUB B 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQRES 1 A 728 SER 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 SER 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 A1767 14
HET NAG A1768 14
HET NDG A1769 14
HET NAG A1770 14
HET NAG B1767 14
HET NAG B1768 14
HET NAG B1769 14
HET NDG B1770 14
HET FPB A1771 28
HET FPB B1771 28
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM FPB N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)
HETNAM 2 FPB BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE
FORMUL 3 FPB 2(C22 H26 N3 O2 F1)
FORMUL 4 NAG 6(C8 H15 N1 O6)
FORMUL 5 NDG 2(C8 H15 N1 O6)
FORMUL 6 HOH *320(H2 O1)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 GLU A 206 1 7
HELIX 3 3 ASP A 274 LEU A 276 5 3
HELIX 4 4 GLU A 421 MET A 425 5 5
HELIX 5 5 LYS A 463 ALA A 465 5 3
HELIX 6 6 ASN A 497 GLN A 505 1 9
HELIX 7 7 TRP A 563 THR A 570 1 8
HELIX 8 8 GLY A 587 HIS A 592 1 6
HELIX 9 9 THR A 600 LYS A 615 1 16
HELIX 10 10 SER A 630 SER A 642 1 13
HELIX 11 11 ARG A 658 TYR A 662 5 5
HELIX 12 12 ASP A 663 GLY A 672 1 10
HELIX 13 13 ASN A 679 ASN A 685 1 7
HELIX 14 14 THR A 687 VAL A 698 5 12
HELIX 15 15 HIS A 712 GLY A 727 1 16
HELIX 16 16 SER A 744 PHE A 763 1 20
HELIX 17 17 THR B 44 ASN B 51 1 8
HELIX 18 18 ASP B 200 VAL B 207 1 8
HELIX 19 19 PRO B 290 ILE B 295 1 6
HELIX 20 20 LEU B 340 GLN B 344 5 5
HELIX 21 21 GLU B 421 MET B 425 5 5
HELIX 22 22 LYS B 463 ALA B 465 5 3
HELIX 23 23 ASN B 497 ASN B 506 1 10
HELIX 24 24 ASN B 562 THR B 570 1 9
HELIX 25 25 GLY B 587 HIS B 592 1 6
HELIX 26 26 THR B 600 MET B 616 1 17
HELIX 27 27 TRP B 629 GLY B 641 1 13
HELIX 28 28 ARG B 658 TYR B 662 5 5
HELIX 29 29 ASP B 663 GLY B 672 1 10
HELIX 30 30 ASN B 679 ARG B 684 1 6
HELIX 31 31 VAL B 688 ALA B 692 5 5
HELIX 32 32 ALA B 692 VAL B 698 5 7
HELIX 33 33 HIS B 712 VAL B 726 1 15
HELIX 34 34 SER B 744 PHE B 763 1 20
SHEET 1 AA 4 ARG A 61 TRP A 62 0
SHEET 2 AA 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AA 4 ASN A 75 ASN A 80 -1 N ASN A 75 O GLN A 72
SHEET 4 AA 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AB 4 ASP A 104 ILE A 107 0
SHEET 2 AB 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AB 4 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 4 AB 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AC 4 TRP A 154 TRP A 157 0
SHEET 2 AC 4 LEU A 164 VAL A 167 -1 O ALA A 165 N THR A 156
SHEET 3 AC 4 ILE A 172 VAL A 174 -1 O TYR A 173 N TYR A 166
SHEET 4 AC 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AD 3 ILE A 194 ASN A 196 0
SHEET 2 AD 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AD 3 LEU A 214 TRP A 216 -1 O TRP A 215 N ALA A 224
SHEET 1 AE 4 ILE A 194 ASN A 196 0
SHEET 2 AE 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AE 4 THR A 265 ASN A 272 -1 O THR A 265 N ASN A 229
SHEET 4 AE 4 ILE A 285 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 AF 2 LEU A 235 PHE A 240 0
SHEET 2 AF 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AG 4 HIS A 298 THR A 307 0
SHEET 2 AG 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AG 4 TYR A 322 TYR A 330 -1 O TYR A 322 N ARG A 317
SHEET 4 AG 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 AH 4 HIS A 298 THR A 307 0
SHEET 2 AH 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 AH 4 TYR A 322 TYR A 330 -1 O TYR A 322 N ARG A 317
SHEET 4 AH 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 AI 4 HIS A 363 PHE A 364 0
SHEET 2 AI 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AI 4 ARG A 382 GLN A 388 -1 O HIS A 383 N ILE A 375
SHEET 4 AI 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AJ 4 VAL A 404 LEU A 410 0
SHEET 2 AJ 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 AJ 4 ASN A 430 GLN A 435 -1 O ASN A 430 N SER A 419
SHEET 4 AJ 4 ASP A 438 CYS A 444 -1 N ASP A 438 O GLN A 435
SHEET 1 AK 4 TYR A 457 PHE A 461 0
SHEET 2 AK 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 AK 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AK 4 LYS A 489 GLU A 495 -1 O LYS A 489 N SER A 484
SHEET 1 AL 8 SER A 511 ILE A 518 0
SHEET 2 AL 8 LYS A 523 LEU A 530 -1 O PHE A 524 N ILE A 517
SHEET 3 AL 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AL 8 TYR A 540 VAL A 546 1 O PRO A 541 N ILE A 574
SHEET 5 AL 8 VAL A 619 TRP A 629 1 N ASP A 620 O TYR A 540
SHEET 6 AL 8 CYS A 649 VAL A 653 1 O CYS A 649 N ILE A 626
SHEET 7 AL 8 GLU A 699 GLY A 705 1 O GLU A 699 N GLY A 650
SHEET 8 AL 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 BA 4 ARG B 61 TRP B 62 0
SHEET 2 BA 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 BA 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 BA 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 BB 4 ILE B 102 ILE B 107 0
SHEET 2 BB 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 BB 4 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 4 BB 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 BC 4 THR B 152 TRP B 157 0
SHEET 2 BC 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 BC 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 BC 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 BD 3 ILE B 194 ASN B 196 0
SHEET 2 BD 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BD 3 LEU B 214 TRP B 216 -1 O TRP B 215 N ALA B 224
SHEET 1 BE 4 ILE B 194 ASN B 196 0
SHEET 2 BE 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BE 4 THR B 265 ASN B 272 -1 O THR B 265 N ASN B 229
SHEET 4 BE 4 ILE B 285 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 BF 2 LEU B 235 PHE B 240 0
SHEET 2 BF 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 BG 7 HIS B 298 THR B 307 0
SHEET 2 BG 7 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 BG 7 TYR B 322 TYR B 330 -1 O TYR B 322 N ARG B 317
SHEET 4 BG 7 TRP B 337 ASN B 338 -1 O ASN B 338 N ASP B 329
SHEET 5 BG 7 TYR B 322 TYR B 330 -1 O ASP B 329 N ASN B 338
SHEET 6 BG 7 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 7 BG 7 TYR B 322 TYR B 330 -1 O SER B 323 N GLU B 347
SHEET 1 BH 4 HIS B 363 PHE B 364 0
SHEET 2 BH 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 BH 4 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 BH 4 CYS B 394 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 BI 4 VAL B 404 LEU B 410 0
SHEET 2 BI 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 BI 4 ASN B 430 GLN B 435 -1 O ASN B 430 N SER B 419
SHEET 4 BI 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 BJ 4 SER B 458 PHE B 461 0
SHEET 2 BJ 4 TYR B 467 ARG B 471 -1 O GLN B 469 N SER B 460
SHEET 3 BJ 4 TYR B 480 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 BJ 4 LYS B 489 GLU B 495 -1 O LYS B 489 N SER B 484
SHEET 1 BK 8 SER B 511 LEU B 519 0
SHEET 2 BK 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 BK 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 BK 8 TYR B 540 ASP B 545 1 O PRO B 541 N ILE B 574
SHEET 5 BK 8 VAL B 619 GLY B 628 1 N ASP B 620 O TYR B 540
SHEET 6 BK 8 CYS B 649 VAL B 653 1 N CYS B 649 O ILE B 624
SHEET 7 BK 8 GLU B 699 GLY B 705 1 O GLU B 699 N GLY B 650
SHEET 8 BK 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
SSBOND 2 CYS A 385 CYS A 394 1555 1555
SSBOND 3 CYS A 444 CYS A 447 1555 1555
SSBOND 4 CYS A 454 CYS A 472 1555 1555
SSBOND 5 CYS A 649 CYS A 762 1555 1555
SSBOND 6 CYS B 328 CYS B 339 1555 1555
SSBOND 7 CYS B 385 CYS B 394 1555 1555
SSBOND 8 CYS B 444 CYS B 447 1555 1555
SSBOND 9 CYS B 454 CYS B 472 1555 1555
SSBOND 10 CYS B 649 CYS B 762 1555 1555
LINK ND2 ASN A 85 C1 NAG A1768 1555 1555
LINK ND2 ASN A 150 C1 NAG A1767 1555 1555
LINK ND2 ASN A 229 C1 NAG A1770 1555 1555
LINK ND2 ASN A 281 C1 NDG A1769 1555 1555
LINK ND2 ASN B 85 C1 NAG B1768 1555 1555
LINK ND2 ASN B 92 C1 NDG B1770 1555 1555
LINK ND2 ASN B 150 C1 NAG B1767 1555 1555
LINK ND2 ASN B 229 C1 NAG B1769 1555 1555
CISPEP 1 GLY A 474 PRO A 475 0 4.65
CISPEP 2 GLY B 474 PRO B 475 0 0.54
SITE 1 AC1 5 ARG A 147 ASN A 150 PHE A 516 ILE A 518
SITE 2 AC1 5 LYS A 523
SITE 1 AC2 5 ASN A 85 SER A 86 SER A 87 GLN A 388
SITE 2 AC2 5 THR A 395
SITE 1 AC4 3 ASN A 229 GLU A 232 HOH Z 159
SITE 1 AC5 3 HIS B 100 ASN B 150 ASP B 515
SITE 1 AC6 7 ASN B 80 ASN B 85 SER B 86 SER B 87
SITE 2 AC6 7 TYR B 386 GLN B 388 THR B 395
SITE 1 AC7 5 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 AC7 5 HOH Y 159
SITE 1 AC8 4 GLU B 73 ASN B 74 ASN B 75 ASN B 92
SITE 1 AC9 12 ARG A 125 GLU A 205 GLU A 206 SER A 209
SITE 2 AC9 12 PHE A 357 TYR A 547 SER A 630 TYR A 662
SITE 3 AC9 12 TYR A 666 ASN A 710 HOH Z 133 HOH Z 160
SITE 1 BC1 12 ARG B 125 GLU B 205 GLU B 206 SER B 209
SITE 2 BC1 12 PHE B 357 TYR B 547 SER B 630 TYR B 662
SITE 3 BC1 12 TYR B 666 ASN B 710 HOH Y 55 HOH Y 130
CRYST1 65.486 66.773 425.407 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 0.015270 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014976 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002351 0.00000
TER 5964 PRO A 766
TER 11928 PRO B 766
MASTER 419 0 10 34 97 0 17 612414 2 196 112
END |