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HEADER HYDROLASE 28-FEB-07 2JID
TITLE HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH 1-(3,4-
TITLE 2 DIMETHOXY-PHENYL)-3-M-TOLYL-PIPERIDINE-4-YLAMINE
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, ADABP;
COMPND 6 CHAIN: A, B;
COMPND 7 EC: 3.4.14.5;
COMPND 8 FRAGMENT: RESIDUES 31-766;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN
KEYWDS DIABETES TYPE II, DIPEPTIDYL PEPTIDASE, PROTEASE, MEMBRANE,
KEYWDS 2 HYDROLASE, B-PROPELLER, STRUCTURE BASED DESIGN,
KEYWDS 3 GLYCOPROTEIN, SIGNAL-ANCHOR, TRANSMEMBRANE, HYDROLASE
KEYWDS 4 FOLD, AMINOPEPTIDASE, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HENNIG,M.STIHLE,T.LUEBBERS,R.THOMA
REVDAT 1 27-MAY-08 2JID 0
JRNL AUTH T.LUEBBERS,M.BOEHRINGER,L.GOBBI,M.HENNIG,
JRNL AUTH 2 D.HUNZIKER,B.KUHN,B.LOEFFLER,P.MATTEI,R.NARQUIZIAN,
JRNL AUTH 3 J.U.PETERS,Y.RUFF,H.P.WESSEL,P.WYSS
JRNL TITL 1,3-DISUBSTITUTED 4-AMINOPIPERIDINES AS USEFUL
JRNL TITL 2 TOOLS IN THE OPTIMIZATION OF THE 2-
JRNL TITL 3 AMINOBENZOAQUINOLIZINE DIPEPTIDYL PEPTIDASE IV
JRNL TITL 4 INHIBITORS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.36
REMARK 3 NUMBER OF REFLECTIONS : 43780
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) : 0.22722
REMARK 3 R VALUE (WORKING SET) : 0.22323
REMARK 3 FREE R VALUE : 0.30306
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2341
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.800
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.948
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6003
REMARK 3 BIN R VALUE (WORKING SET) : 0.287
REMARK 3 BIN FREE R VALUE SET COUNT : 350
REMARK 3 BIN FREE R VALUE : 0.418
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 : 160
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.535
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80
REMARK 3 B22 (A**2) : 1.12
REMARK 3 B33 (A**2) : -0.32
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.459
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.360
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.590
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.819
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 12448 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 16940 ; 1.612 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1454 ; 7.444 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 616 ;36.268 ;23.961
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1994 ;20.466 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;21.007 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1796 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 9572 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 6000 ; 0.247 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 8305 ; 0.323 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 466 ; 0.168 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 31 ; 0.280 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 1 ; 0.305 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 7384 ; 0.593 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 11766 ; 1.058 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 5917 ; 1.323 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 5174 ; 2.113 ; 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 : 1.20
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2JID COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 28-FEB-2007.
REMARK 100 THE EBI ID CODE IS EBI-31666.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-2002
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47000
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.6
REMARK 200 R MERGE (I) : 0.08
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 32.62550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 211.97400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.41050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 211.97400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.62550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.41050
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 GLY A 31
REMARK 465 THR A 32
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 ASP A 38
REMARK 465 GLY B 31
REMARK 465 THR B 32
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 ASP B 38
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, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 60 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 LEU A 500 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 LEU B 60 CA - CB - CG ANGL. DEV. = 15.4 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 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 ARG A 40 -70.89 62.52
REMARK 500 TYR A 58 60.90 -151.84
REMARK 500 SER A 64 -157.35 -176.96
REMARK 500 HIS A 66 32.78 -158.91
REMARK 500 GLU A 73 -84.40 55.41
REMARK 500 PHE A 95 58.64 -115.38
REMARK 500 GLU A 97 57.28 -96.40
REMARK 500 ASP A 110 22.11 -175.93
REMARK 500 GLN A 123 -114.16 -114.21
REMARK 500 TRP A 124 -150.79 -80.99
REMARK 500 SER A 127 150.65 -47.34
REMARK 500 HIS A 162 49.27 -140.98
REMARK 500 ASN A 170 17.10 51.63
REMARK 500 ILE A 176 -72.32 -63.41
REMARK 500 PRO A 178 -35.41 -37.64
REMARK 500 ASP A 192 -5.68 62.89
REMARK 500 VAL A 207 -70.69 -128.58
REMARK 500 ALA A 210 142.02 -179.67
REMARK 500 THR A 231 -57.68 -28.56
REMARK 500 SER A 242 -167.18 64.72
REMARK 500 SER A 292 0.94 -61.89
REMARK 500 GLU A 309 4.60 -154.73
REMARK 500 PRO A 359 131.47 -32.16
REMARK 500 ASN A 377 -176.13 -65.46
REMARK 500 ASP A 393 -162.68 52.51
REMARK 500 ASN A 450 67.22 -175.71
REMARK 500 GLN A 455 -3.37 -141.75
REMARK 500 PRO A 478 124.95 -34.94
REMARK 500 VAL A 486 -73.28 -12.58
REMARK 500 ASP A 488 95.49 -62.29
REMARK 500 LEU A 504 -9.88 -58.77
REMARK 500 LEU A 514 65.54 -151.70
REMARK 500 ASP A 515 -142.17 -95.99
REMARK 500 ASN A 520 -83.16 -105.39
REMARK 500 HIS A 533 55.82 35.89
REMARK 500 TYR A 547 -64.19 -127.30
REMARK 500 ARG A 597 36.46 -145.31
REMARK 500 THR A 600 -88.05 -113.95
REMARK 500 VAL A 603 -77.23 -59.23
REMARK 500 GLU A 604 -34.67 -32.11
REMARK 500 SER A 630 -131.89 45.02
REMARK 500 PRO A 674 23.30 -69.21
REMARK 500 ASP A 678 -116.15 -92.07
REMARK 500 SER A 686 55.83 -115.98
REMARK 500 ALA A 692 -48.58 -29.61
REMARK 500 ASN A 710 -83.40 -102.61
REMARK 500 TYR A 735 77.86 -118.25
REMARK 500 THR A 736 123.75 -28.51
REMARK 500 ASP A 737 -14.63 75.98
REMARK 500 SER A 764 46.11 76.08
REMARK 500 LYS B 41 -178.09 -68.15
REMARK 500 SER B 64 -153.55 -148.93
REMARK 500 GLU B 73 47.25 38.18
REMARK 500 ASN B 74 -1.09 73.26
REMARK 500 THR B 94 144.50 -30.87
REMARK 500 SER B 106 118.83 -164.26
REMARK 500 GLN B 123 -106.85 -90.42
REMARK 500 TRP B 124 -142.60 -87.57
REMARK 500 ARG B 140 72.02 -63.49
REMARK 500 ASN B 151 57.68 36.75
REMARK 500 HIS B 162 36.39 -150.10
REMARK 500 GLU B 191 140.28 -39.06
REMARK 500 ASP B 192 17.68 50.07
REMARK 500 ILE B 193 -50.79 -137.59
REMARK 500 ASP B 200 -168.46 -102.31
REMARK 500 SER B 209 48.60 37.20
REMARK 500 SER B 242 -169.10 59.90
REMARK 500 GLU B 244 -11.56 -48.82
REMARK 500 PRO B 249 132.75 -39.82
REMARK 500 ASN B 281 151.84 -48.32
REMARK 500 ASP B 302 137.42 -173.31
REMARK 500 GLN B 320 40.02 -66.13
REMARK 500 ALA B 342 -13.80 -40.87
REMARK 500 THR B 401 49.44 -104.20
REMARK 500 ALA B 409 141.28 -175.93
REMARK 500 LYS B 423 12.47 58.97
REMARK 500 ASP B 438 106.30 -160.48
REMARK 500 GLN B 455 18.07 -149.98
REMARK 500 ALA B 465 51.76 31.23
REMARK 500 ASN B 497 10.07 57.53
REMARK 500 ASN B 520 63.10 37.51
REMARK 500 GLU B 521 15.91 56.12
REMARK 500 TYR B 547 -68.14 -123.21
REMARK 500 CYS B 551 38.00 93.61
REMARK 500 ASN B 562 -155.31 -131.03
REMARK 500 ARG B 597 42.85 -151.44
REMARK 500 THR B 600 -90.28 -113.33
REMARK 500 LYS B 615 58.04 -66.18
REMARK 500 SER B 630 -135.01 56.52
REMARK 500 PRO B 674 48.25 -88.24
REMARK 500 ASP B 678 -107.30 -112.47
REMARK 500 PHE B 695 -17.08 -48.44
REMARK 500 ASP B 708 94.34 -65.35
REMARK 500 ASN B 710 -77.14 -72.44
REMARK 500 GLN B 714 -52.69 -24.59
REMARK 500 ASP B 725 -7.65 -49.19
REMARK 500 MET B 733 110.33 -165.15
REMARK 500 ASP B 737 -3.31 70.02
REMARK 500 ASP B 739 -151.76 -113.10
REMARK 500 ILE B 742 59.07 23.82
REMARK 500
REMARK 500 REMARK: NULL
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 GLY B 111 GLN B 112 0 -144.15
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 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 1767
REMARK 610 NAG A 1768
REMARK 610 NAG A 1769
REMARK 610 NAG B 1769
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: BINDING SITE FOR RESIDUE NAG A 1767
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1768
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1769
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1770
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVB A 1771
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1767
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1768
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1769
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1770
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVB B 1771
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 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)
REMARK 900 RELATED ID: 2BUB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPDIDASE IV (CD26) IN COMPLEX WITH A
REMARK 900 REVERSED AMIDE INHIBITOR
REMARK 900 RELATED ID: 2G5P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPPIV)COMPLEXED WITH
REMARK 900 CYANOPYRROLIDINE (C5-PRO-PRO) INHIBITOR 21AC
REMARK 900 RELATED ID: 2G5T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPPIV)COMPLEXED WITH
REMARK 900 CYANOPYRROLIDINE (C5-PRO-PRO) INHIBITOR 21AG
REMARK 900 RELATED ID: 2G63 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPPIV)COMPLEXED WITH
REMARK 900 CYANOPYRROLIDINE (C5-PRO-PRO) INHIBITOR 24B
DBREF 2JID A 31 766 UNP P27487 DPP4_HUMAN 31 766
DBREF 2JID B 31 766 UNP P27487 DPP4_HUMAN 31 766
SEQRES 1 A 736 GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR
SEQRES 2 A 736 THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS
SEQRES 3 A 736 LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU
SEQRES 4 A 736 TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU
SEQRES 5 A 736 TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER THR PHE
SEQRES 6 A 736 ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER
SEQRES 7 A 736 PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL
SEQRES 8 A 736 LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE
SEQRES 9 A 736 TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG
SEQRES 10 A 736 ILE PRO ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL
SEQRES 11 A 736 GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR
SEQRES 12 A 736 VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR
SEQRES 13 A 736 TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR
SEQRES 14 A 736 ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER
SEQRES 15 A 736 ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR
SEQRES 16 A 736 ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR
SEQRES 17 A 736 SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR
SEQRES 18 A 736 VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO
SEQRES 19 A 736 THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER
SEQRES 20 A 736 SER VAL THR ASN ALA THR SER ILE GLN ILE THR ALA PRO
SEQRES 21 A 736 ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL
SEQRES 22 A 736 THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU
SEQRES 23 A 736 ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP
SEQRES 24 A 736 TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA
SEQRES 25 A 736 ARG GLN HIS ILE GLU MET SER THR THR GLY TRP VAL GLY
SEQRES 26 A 736 ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY
SEQRES 27 A 736 ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR
SEQRES 28 A 736 ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS
SEQRES 29 A 736 THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE
SEQRES 30 A 736 GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN
SEQRES 31 A 736 GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS
SEQRES 32 A 736 ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS LEU SER
SEQRES 33 A 736 CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL
SEQRES 34 A 736 SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS
SEQRES 35 A 736 SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER
SEQRES 36 A 736 VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER
SEQRES 37 A 736 ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER
SEQRES 38 A 736 LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE
SEQRES 39 A 736 TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER
SEQRES 40 A 736 LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO
SEQRES 41 A 736 CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP
SEQRES 42 A 736 ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA
SEQRES 43 A 736 SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS
SEQRES 44 A 736 ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU
SEQRES 45 A 736 VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS
SEQRES 46 A 736 MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY
SEQRES 47 A 736 TRP SER TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY
SEQRES 48 A 736 SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA
SEQRES 49 A 736 PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR
SEQRES 50 A 736 GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU
SEQRES 51 A 736 ASP HIS TYR ARG ASN SER THR VAL MET SER ARG ALA GLU
SEQRES 52 A 736 ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR
SEQRES 53 A 736 ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE
SEQRES 54 A 736 SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA
SEQRES 55 A 736 MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER
SEQRES 56 A 736 THR ALA HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE
SEQRES 57 A 736 ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 736 GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR
SEQRES 2 B 736 THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS
SEQRES 3 B 736 LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU
SEQRES 4 B 736 TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU
SEQRES 5 B 736 TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER THR PHE
SEQRES 6 B 736 ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER
SEQRES 7 B 736 PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL
SEQRES 8 B 736 LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE
SEQRES 9 B 736 TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG
SEQRES 10 B 736 ILE PRO ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL
SEQRES 11 B 736 GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR
SEQRES 12 B 736 VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR
SEQRES 13 B 736 TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR
SEQRES 14 B 736 ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER
SEQRES 15 B 736 ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR
SEQRES 16 B 736 ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR
SEQRES 17 B 736 SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR
SEQRES 18 B 736 VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO
SEQRES 19 B 736 THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER
SEQRES 20 B 736 SER VAL THR ASN ALA THR SER ILE GLN ILE THR ALA PRO
SEQRES 21 B 736 ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL
SEQRES 22 B 736 THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU
SEQRES 23 B 736 ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP
SEQRES 24 B 736 TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA
SEQRES 25 B 736 ARG GLN HIS ILE GLU MET SER THR THR GLY TRP VAL GLY
SEQRES 26 B 736 ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY
SEQRES 27 B 736 ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR
SEQRES 28 B 736 ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS
SEQRES 29 B 736 THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE
SEQRES 30 B 736 GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN
SEQRES 31 B 736 GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS
SEQRES 32 B 736 ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS LEU SER
SEQRES 33 B 736 CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL
SEQRES 34 B 736 SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS
SEQRES 35 B 736 SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER
SEQRES 36 B 736 VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER
SEQRES 37 B 736 ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER
SEQRES 38 B 736 LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE
SEQRES 39 B 736 TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER
SEQRES 40 B 736 LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO
SEQRES 41 B 736 CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP
SEQRES 42 B 736 ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA
SEQRES 43 B 736 SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS
SEQRES 44 B 736 ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU
SEQRES 45 B 736 VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS
SEQRES 46 B 736 MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY
SEQRES 47 B 736 TRP SER TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY
SEQRES 48 B 736 SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA
SEQRES 49 B 736 PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR
SEQRES 50 B 736 GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU
SEQRES 51 B 736 ASP HIS TYR ARG ASN SER THR VAL MET SER ARG ALA GLU
SEQRES 52 B 736 ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR
SEQRES 53 B 736 ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE
SEQRES 54 B 736 SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA
SEQRES 55 B 736 MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER
SEQRES 56 B 736 THR ALA HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE
SEQRES 57 B 736 ILE LYS GLN CYS PHE SER LEU PRO
HET NAG A1767 14
HET NAG A1768 14
HET NAG A1769 14
HET NAG A1770 14
HET GVB A1771 24
HET NAG B1767 14
HET NAG B1768 14
HET NAG B1769 14
HET NAG B1770 14
HET GVB B1771 24
HETNAM GVB (3R,4S)-1-(3,4-DIMETHOXYPHENYL)-3-(3-
HETNAM 2 GVB METHYLPHENYL)PIPERIDIN-4-AMINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN GVB 1-(3,4-DIMETHOXY-PHENYL)-3-M-TOLYL-
HETSYN 2 GVB PIPERIDINE-4-YLAMINE
HETSYN NAG NAG
FORMUL 3 GVB 2(C20 H26 N2 O2)
FORMUL 4 NAG 8(C8 H15 N O6)
FORMUL 5 HOH *128(H2 O1)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 ASP A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 VAL A 341 GLN A 344 5 4
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 SER A 446 ASN A 450 5 5
HELIX 8 8 LYS A 463 ALA A 465 5 3
HELIX 9 9 ASN A 497 LEU A 504 1 8
HELIX 10 10 ASN A 562 THR A 570 1 9
HELIX 11 11 GLY A 587 HIS A 592 1 6
HELIX 12 12 ALA A 593 ASN A 595 5 3
HELIX 13 13 THR A 600 MET A 616 1 17
HELIX 14 14 SER A 630 GLY A 641 1 12
HELIX 15 15 ARG A 658 TYR A 662 5 5
HELIX 16 16 ASP A 663 GLY A 672 1 10
HELIX 17 17 ASN A 679 SER A 686 1 8
HELIX 18 18 VAL A 688 VAL A 698 5 11
HELIX 19 19 HIS A 712 VAL A 726 1 15
HELIX 20 20 SER A 744 SER A 764 1 21
HELIX 21 21 THR B 44 LYS B 50 1 7
HELIX 22 22 ASP B 200 VAL B 207 1 8
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 LYS B 463 ALA B 465 5 3
HELIX 26 26 ASN B 497 GLN B 505 1 9
HELIX 27 27 ASN B 562 THR B 570 1 9
HELIX 28 28 GLY B 587 HIS B 592 1 6
HELIX 29 29 ALA B 593 ASN B 595 5 3
HELIX 30 30 THR B 600 LYS B 615 1 16
HELIX 31 31 SER B 630 GLY B 641 1 12
HELIX 32 32 ARG B 658 TYR B 662 5 5
HELIX 33 33 ASP B 663 GLY B 672 1 10
HELIX 34 34 ASN B 679 SER B 686 1 8
HELIX 35 35 VAL B 688 GLN B 697 5 10
HELIX 36 36 HIS B 712 ASP B 725 1 14
HELIX 37 37 SER B 744 PHE B 763 1 20
SHEET 1 AA 2 LYS A 41 THR A 42 0
SHEET 2 AA 2 VAL A 507 GLN A 508 1 N GLN A 508 O LYS A 41
SHEET 1 AB 4 ARG A 61 TRP A 62 0
SHEET 2 AB 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AB 4 ASN A 75 ASN A 80 -1 O ASN A 75 N GLN A 72
SHEET 4 AB 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AC 4 ASP A 104 ILE A 107 0
SHEET 2 AC 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AC 4 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 4 AC 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AD 4 TRP A 154 TRP A 157 0
SHEET 2 AD 4 LEU A 164 VAL A 167 -1 O ALA A 165 N THR A 156
SHEET 3 AD 4 ILE A 172 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 AD 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AE 3 ILE A 194 ASN A 196 0
SHEET 2 AE 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AE 3 LEU A 214 TRP A 216 -1 O TRP A 215 N ALA A 224
SHEET 1 AF 4 ILE A 194 ASN A 196 0
SHEET 2 AF 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AF 4 THR A 265 ASN A 272 -1 O THR A 265 N ASN A 229
SHEET 4 AF 4 ILE A 285 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 AG 2 LEU A 235 PHE A 240 0
SHEET 2 AG 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AH 4 HIS A 298 TRP A 305 0
SHEET 2 AH 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AH 4 SER A 323 TYR A 330 -1 O VAL A 324 N TRP A 315
SHEET 4 AH 4 HIS A 345 GLU A 347 -1 O HIS A 345 N MET A 325
SHEET 1 AI 4 HIS A 298 TRP A 305 0
SHEET 2 AI 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AI 4 SER A 323 TYR A 330 -1 O VAL A 324 N TRP A 315
SHEET 4 AI 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 AJ 4 PRO A 362 PHE A 364 0
SHEET 2 AJ 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AJ 4 ARG A 382 GLN A 388 -1 O HIS A 383 N ILE A 375
SHEET 4 AJ 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AK 4 VAL A 404 LEU A 410 0
SHEET 2 AK 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 AK 4 ASN A 430 GLN A 435 -1 O ASN A 430 N SER A 419
SHEET 4 AK 4 VAL A 442 CYS A 444 -1 N THR A 443 O LYS A 433
SHEET 1 AL 4 TYR A 457 PHE A 461 0
SHEET 2 AL 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 AL 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AL 4 LYS A 489 GLU A 495 -1 N LYS A 489 O SER A 484
SHEET 1 AM 3 SER A 511 LYS A 513 0
SHEET 2 AM 3 LYS A 523 LEU A 530 -1 O MET A 528 N LYS A 513
SHEET 3 AM 3 PHE A 516 ILE A 518 -1 O ILE A 517 N PHE A 524
SHEET 1 AN 8 SER A 511 LYS A 513 0
SHEET 2 AN 8 LYS A 523 LEU A 530 -1 O MET A 528 N LYS A 513
SHEET 3 AN 8 ILE A 574 ASP A 579 -1 O VAL A 575 N ILE A 529
SHEET 4 AN 8 TYR A 540 VAL A 546 1 O PRO A 541 N ILE A 574
SHEET 5 AN 8 VAL A 619 TRP A 629 1 N ASP A 620 O TYR A 540
SHEET 6 AN 8 CYS A 649 VAL A 653 1 O CYS A 649 N ILE A 626
SHEET 7 AN 8 GLU A 699 HIS A 704 1 O GLU A 699 N GLY A 650
SHEET 8 AN 8 GLN A 731 TRP A 734 1 O GLN A 731 N LEU A 702
SHEET 1 BA 2 LYS B 41 THR B 42 0
SHEET 2 BA 2 VAL B 507 GLN B 508 1 N GLN B 508 O LYS B 41
SHEET 1 BB 4 ARG B 61 TRP B 62 0
SHEET 2 BB 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 BB 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 BB 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 BC 4 ILE B 102 ILE B 107 0
SHEET 2 BC 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 BC 4 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 4 BC 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 BD 4 TRP B 154 TRP B 157 0
SHEET 2 BD 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 BD 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 BD 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 BE 7 ILE B 194 ASN B 196 0
SHEET 2 BE 7 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BE 7 LEU B 214 TRP B 216 -1 O TRP B 215 N ALA B 224
SHEET 4 BE 7 PHE B 222 ASN B 229 -1 O ALA B 224 N TRP B 215
SHEET 5 BE 7 ILE B 285 ILE B 287
SHEET 6 BE 7 THR B 265 ASN B 272 -1 O PHE B 268 N ILE B 287
SHEET 7 BE 7 PHE B 222 ASN B 229 -1 O LEU B 223 N VAL B 271
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 SER B 323 TYR B 330 -1 O VAL B 324 N TRP B 315
SHEET 4 BG 7 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 5 BG 7 SER B 323 TYR B 330 -1 O ASP B 329 N ASN B 338
SHEET 6 BG 7 HIS B 345 GLU B 347 -1 O HIS B 345 N MET B 325
SHEET 7 BG 7 SER B 323 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 ASP B 438 CYS B 444 -1 N ASP B 438 O GLN B 435
SHEET 1 BJ 4 TYR B 457 PHE B 461 0
SHEET 2 BJ 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 BJ 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
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 ASP B 579 -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 TRP B 629 1 N ASP B 620 O TYR B 540
SHEET 6 BK 8 CYS B 649 VAL B 653 1 O CYS B 649 N ILE B 626
SHEET 7 BK 8 LEU B 701 GLY B 705 1 O LEU B 701 N ALA B 652
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 2.07
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.08
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.05
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.09
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.08
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.07
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.07
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.05
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.09
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.08
LINK ND2 ASN A 229 C1 NAG A1770 1555 1555 1.46
LINK ND2 ASN B 85 C1 NAG B1768 1555 1555 1.45
LINK ND2 ASN B 92 C1 NAG B1770 1555 1555 1.45
LINK ND2 ASN B 150 C1 NAG B1767 1555 1555 1.44
CISPEP 1 GLY A 474 PRO A 475 0 9.17
CISPEP 2 GLY B 474 PRO B 475 0 2.61
SITE 1 AC1 6 TYR A 118 ARG A 147 ASN A 150 PHE A 516
SITE 2 AC1 6 ILE A 518 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 AC3 2 TRP A 187 ASN A 281
SITE 1 AC4 4 ASN A 229 THR A 231 GLU A 232 HOH A2055
SITE 1 AC5 6 ARG A 125 GLU A 205 GLU A 206 SER A 630
SITE 2 AC5 6 TYR A 662 TYR A 666
SITE 1 AC6 3 ASN B 150 ASP B 515 PHE B 516
SITE 1 AC7 5 ASN B 85 SER B 87 TYR B 386 GLN B 388
SITE 2 AC7 5 THR B 395
SITE 1 AC8 6 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 AC8 6 HOH B2071 HOH B2072
SITE 1 AC9 3 GLU B 73 ASN B 75 ASN B 92
SITE 1 BC1 7 GLU B 205 GLU B 206 SER B 630 TYR B 662
SITE 2 BC1 7 TYR B 666 HIS B 740 HOH B2073
CRYST1 65.251 66.821 423.948 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 0.015325 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014965 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002359 0.00000
TER 5964 PRO A 766
TER 11928 PRO B 766
MASTER 523 0 10 37 104 0 16 612214 2 184 114
END |