HEADER HYDROLASE 01-AUG-05 2AJ8
TITLE PORCINE DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH 7-BENZYL-1,3-
TITLE 2 DIMETHYL-8-PIPERAZIN-1-YL-3,7-DIHYDRO-PURINE-2,6-DIONE (BDPX)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN
COMPND 6 CD26;
COMPND 7 EC: 3.4.14.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: KIDNEY
KEYWDS SERINE PROTEASE, DIPEPTIDYL PEPTIDASE, OXYANION HOLE, SUBSTRATE
KEYWDS 2 CHANNELING, DRUG DESIGN, DIABETES MELLITUS, FLEXIBILITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ENGEL,T.HOFFMANN,S.MANHART,U.HEISER,S.CHAMBRE,R.HUBER,H.U.DEMUTH,
AUTHOR 2 W.BODE
REVDAT 6 23-AUG-23 2AJ8 1 REMARK HETSYN
REVDAT 5 29-JUL-20 2AJ8 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 11-OCT-17 2AJ8 1 REMARK
REVDAT 3 13-JUL-11 2AJ8 1 VERSN
REVDAT 2 24-FEB-09 2AJ8 1 VERSN
REVDAT 1 28-FEB-06 2AJ8 0
JRNL AUTH M.ENGEL,T.HOFFMANN,S.MANHART,U.HEISER,S.CHAMBRE,R.HUBER,
JRNL AUTH 2 H.U.DEMUTH,W.BODE
JRNL TITL RIGIDITY AND FLEXIBILITY OF DIPEPTIDYL PEPTIDASE IV: CRYSTAL
JRNL TITL 2 STRUCTURES OF AND DOCKING EXPERIMENTS WITH DPIV.
JRNL REF J.MOL.BIOL. V. 355 768 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16330047
JRNL DOI 10.1016/J.JMB.2005.11.014
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2477356.500
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 210621
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 SET) : 0.197
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9993
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.11
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 31362
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1678
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23864
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 712
REMARK 3 SOLVENT ATOMS : 1646
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.75000
REMARK 3 B22 (A**2) : -2.32000
REMARK 3 B33 (A**2) : -4.42000
REMARK 3 B12 (A**2) : -0.85000
REMARK 3 B13 (A**2) : -5.12000
REMARK 3 B23 (A**2) : 1.65000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.930
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.360 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.090 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.100 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.990 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 48.50
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN.TOP
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.TOP
REMARK 3 PARAMETER FILE 3 : WATER.TOP
REMARK 3 PARAMETER FILE 4 : ION.TOP
REMARK 3 PARAMETER FILE 5 : SUL.TOP
REMARK 3 PARAMETER FILE 6 : SC3-2.TOP
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 4 : ION.PARAM
REMARK 3 TOPOLOGY FILE 5 : SUL.PARAM
REMARK 3 TOPOLOGY FILE 6 : SC3-2.PAR
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033957.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-04
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 : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 212238
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 39.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1ORV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 2000, 0.1 M AMMONIUM SULFATE,
REMARK 280 0.1 M TRIS/HCL PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 11430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, G, H
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
REMARK 350 BIOMOLECULE: 2
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: 11640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, I, J, K, L, M
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 111640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 114720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, I, J, K, L, M
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 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, G, H
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -14.68593
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 66.99001
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 122.52606
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 145 CB CG CD OE1 OE2
REMARK 480 ARG A 147 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 391 NZ
REMARK 480 LYS A 399 CD CE NZ
REMARK 480 LYS A 464 CG CD CE NZ
REMARK 480 SER A 484 CB OG
REMARK 480 LYS A 489 CD CE NZ
REMARK 480 LYS A 513 CG CD CE NZ
REMARK 480 LYS A 523 CG CD CE NZ
REMARK 480 LYS A 539 CD CE NZ
REMARK 480 LYS A 622 CD CE NZ
REMARK 480 GLN B 141 CG CD OE1 NE2
REMARK 480 ARG B 147 CG CD NE CZ NH1 NH2
REMARK 480 ASN B 150 CB CG OD1 ND2
REMARK 480 ILE B 295 CD1
REMARK 480 THR B 389 OG1
REMARK 480 GLU B 452 CG CD OE1 OE2
REMARK 480 LYS B 502 CD CE NZ
REMARK 480 ASP B 506 CG OD1 OD2
REMARK 480 ASP B 535 CB CG OD1 OD2
REMARK 480 LYS B 536 CB CG CD CE NZ
REMARK 480 LYS B 538 CG CD CE NZ
REMARK 480 LYS B 622 CD CE NZ
REMARK 480 GLU C 145 CB CG CD OE1 OE2
REMARK 480 ARG C 147 CG CD NE CZ NH1 NH2
REMARK 480 ASN C 150 CB CG OD1 ND2
REMARK 480 GLU C 378 CB CG CD OE1 OE2
REMARK 480 THR C 389 OG1
REMARK 480 LYS C 399 CD CE NZ
REMARK 480 GLU C 452 CG CD OE1 OE2
REMARK 480 ASP C 535 CB CG OD1 OD2
REMARK 480 LYS C 589 CD CE NZ
REMARK 480 LYS C 615 CE NZ
REMARK 480 LYS C 622 CD CE NZ
REMARK 480 ARG C 684 CG CD NE CZ NH1 NH2
REMARK 480 GLU D 378 CG CD OE1 OE2
REMARK 480 THR D 389 OG1
REMARK 480 LYS D 399 CD CE NZ
REMARK 480 GLU D 452 CG CD OE1 OE2
REMARK 480 LYS D 464 CG CD CE NZ
REMARK 480 LYS D 489 CB CG CD CE NZ
REMARK 480 LYS D 513 CG CD CE NZ
REMARK 480 HIS D 520 CG ND1 CD2 CE1 NE2
REMARK 480 LYS D 589 CD CE NZ
REMARK 480 LYS D 622 CD CE NZ
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 NE ARG C 691 O HOH C 1620 2.03
REMARK 500 O LEU B 482 O GLU B 490 2.14
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 669 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 669 NE - CZ - NH2 ANGL. DEV. = -3.6 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 ARG A 40 -165.76 -63.60
REMARK 500 ASN A 74 -6.22 76.04
REMARK 500 GLN A 123 -102.18 -113.52
REMARK 500 TRP A 124 -145.61 -92.39
REMARK 500 HIS A 162 41.02 -147.31
REMARK 500 VAL A 193 -51.34 -131.54
REMARK 500 VAL A 207 -64.22 -106.26
REMARK 500 ALA A 213 47.70 -151.49
REMARK 500 SER A 242 -165.12 61.73
REMARK 500 ASN A 377 -179.72 -69.59
REMARK 500 LYS A 423 13.71 58.35
REMARK 500 ASP A 438 94.57 -171.43
REMARK 500 TYR A 439 6.13 -65.85
REMARK 500 ASN A 450 68.40 -158.04
REMARK 500 LEU A 491 -65.38 58.24
REMARK 500 TYR A 547 -76.15 -122.69
REMARK 500 ARG A 596 11.18 56.98
REMARK 500 ARG A 597 52.42 -145.84
REMARK 500 THR A 600 -89.60 -116.02
REMARK 500 SER A 630 -121.71 64.30
REMARK 500 ASP A 678 -96.90 -118.51
REMARK 500 ASN A 710 -73.51 -91.63
REMARK 500 ASP A 737 2.88 58.95
REMARK 500 ASP A 739 -154.36 -100.09
REMARK 500 ILE A 742 49.62 37.83
REMARK 500 ARG B 40 143.66 52.33
REMARK 500 SER B 64 -171.57 -170.26
REMARK 500 HIS B 66 13.71 -149.79
REMARK 500 GLU B 82 -80.94 -46.61
REMARK 500 GLN B 123 -101.30 -118.18
REMARK 500 TRP B 124 -150.64 -92.02
REMARK 500 ARG B 140 54.24 28.38
REMARK 500 HIS B 162 37.27 -148.96
REMARK 500 VAL B 193 -58.06 -130.95
REMARK 500 VAL B 207 -60.52 -108.48
REMARK 500 ALA B 213 45.07 -145.58
REMARK 500 SER B 242 -162.81 63.39
REMARK 500 ASP B 438 83.45 -161.05
REMARK 500 ASN B 450 69.28 -161.51
REMARK 500 LEU B 491 -67.74 55.52
REMARK 500 TYR B 547 -72.44 -122.43
REMARK 500 ARG B 596 17.41 53.60
REMARK 500 ARG B 597 53.49 -148.15
REMARK 500 THR B 600 -89.88 -108.36
REMARK 500 SER B 630 -121.30 56.95
REMARK 500 ASP B 678 -99.40 -103.49
REMARK 500 ASN B 710 -70.46 -95.97
REMARK 500 ASP B 739 -158.46 -100.06
REMARK 500 GLU C 73 -70.74 62.91
REMARK 500 ASN C 74 3.40 -164.14
REMARK 500
REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 700 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NAG A 771A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AJB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH TRIPEPTIDE TERT-BUTYL-GLY-L-PRO-L-
REMARK 900 ILE (TBU-GPI)
REMARK 900 RELATED ID: 2AJC RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH 4-(2-AMINOETHYL)-BENZENE SULPHONYL
REMARK 900 FLUORIDE (AEBSF)
REMARK 900 RELATED ID: 2AJD RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH L-PRO-BORO-L-PRO (BOROPRO)
DBREF 2AJ8 A 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2AJ8 B 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2AJ8 C 39 766 UNP P22411 DPP4_PIG 39 766
DBREF 2AJ8 D 39 766 UNP P22411 DPP4_PIG 39 766
SEQRES 1 A 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 A 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 A 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
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 ILE
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 ASN GLU PRO ASN LEU SER
SEQRES 12 A 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 A 728 TYR ASN GLY VAL 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 ILE PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 A 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 A 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 A 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 A 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 A 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 A 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA 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 HIS LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN 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 ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 A 728 HIS GLY 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 ILE GLU
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU SER 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 THR
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP 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 ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER LYS 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 TYR 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 LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 A 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 B 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 B 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
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 ILE
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 ASN GLU PRO ASN LEU SER
SEQRES 12 B 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 B 728 TYR ASN GLY VAL 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 ILE PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 B 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 B 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 B 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 B 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 B 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 B 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA 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 HIS LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN 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 ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 B 728 HIS GLY 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 ILE GLU
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU SER 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 THR
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP 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 ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER LYS 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 TYR 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 LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 B 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 C 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 C 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 C 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 C 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 C 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
SEQRES 7 C 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 C 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 C 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 C 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 C 728 ASN ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER
SEQRES 12 C 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 C 728 TYR ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 C 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 C 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 C 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 C 728 GLN TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA
SEQRES 18 C 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 C 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 C 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 C 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 C 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 C 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 C 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 C 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 C 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 C 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 C 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP
SEQRES 29 C 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 C 728 TYR TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY
SEQRES 31 C 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS
SEQRES 32 C 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 C 728 GLN TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 C 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 C 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 C 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 C 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 C 728 HIS GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 C 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU
SEQRES 40 C 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 C 728 PHE ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 C 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 C 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 C 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR
SEQRES 45 C 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG
SEQRES 46 C 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 C 728 SER MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 C 728 GLY ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR
SEQRES 49 C 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 C 728 PRO GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL
SEQRES 51 C 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 C 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 C 728 GLN SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 C 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 C 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 C 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 728 SER ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER
SEQRES 2 D 728 THR PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER
SEQRES 3 D 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 D 728 LEU PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU
SEQRES 5 D 728 GLU ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN
SEQRES 6 D 728 ASP TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE
SEQRES 7 D 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 D 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 D 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE
SEQRES 10 D 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 D 728 ASN ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER
SEQRES 12 D 728 SER GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE
SEQRES 13 D 728 TYR ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 D 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 D 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 D 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 D 728 GLN TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA
SEQRES 18 D 728 GLY ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP
SEQRES 19 D 728 THR ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR
SEQRES 20 D 728 GLN ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS
SEQRES 21 D 728 TYR LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE
SEQRES 22 D 728 SER LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE
SEQRES 23 D 728 ILE ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP
SEQRES 24 D 728 ILE SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR
SEQRES 25 D 728 THR GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS
SEQRES 26 D 728 PHE THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 D 728 ASN GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR
SEQRES 28 D 728 ASP LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP
SEQRES 29 D 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 D 728 TYR TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY
SEQRES 31 D 728 ARG ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS
SEQRES 32 D 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 D 728 GLN TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR
SEQRES 34 D 728 TYR GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 D 728 THR LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL
SEQRES 36 D 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP
SEQRES 37 D 728 VAL GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU
SEQRES 38 D 728 HIS GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 D 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU
SEQRES 40 D 728 VAL TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL
SEQRES 41 D 728 PHE ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 D 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 D 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 D 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR
SEQRES 45 D 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG
SEQRES 46 D 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 D 728 SER MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS
SEQRES 48 D 728 GLY ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR
SEQRES 49 D 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 D 728 PRO GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL
SEQRES 51 D 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 D 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 D 728 GLN SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY
SEQRES 54 D 728 VAL ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 D 728 GLY ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR
SEQRES 56 D 728 HIS MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
MODRES 2AJ8 ASN A 229 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN A 685 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN B 92 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN B 685 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN C 685 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN D 92 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN D 229 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN D 321 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN D 685 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN A 85 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN A 92 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN A 279 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN A 321 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN B 85 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN B 229 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN B 279 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN B 321 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN C 85 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN C 92 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN C 229 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN C 279 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN C 321 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN D 85 ASN GLYCOSYLATION SITE
MODRES 2AJ8 ASN D 279 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET NAG A 767A 14
HET NAG A 768A 14
HET NAG A 771A 14
HET NAG A 772A 14
HET SO4 A1500 5
HET SC3 A1601 26
HET SC3 A1608 26
HET NAG B 767A 14
HET NAG B 771A 14
HET NAG B 772A 14
HET NAG B 773A 14
HET SO4 B1501 5
HET SC3 B1602 26
HET SC3 B1605 26
HET NAG C 767A 14
HET NAG C 768A 14
HET NAG C 769A 14
HET NAG C 770A 14
HET NAG C 771A 14
HET SO4 C1502 5
HET SC3 C1603 26
HET SC3 C1607 26
HET NAG D 767A 14
HET NAG D 773A 14
HET SO4 D1503 5
HET SC3 D1604 26
HET SC3 D1606 26
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM SC3 7-BENZYL-1,3-DIMETHYL-8-PIPERAZIN-1-YL-3,7-DIHYDRO-
HETNAM 2 SC3 PURINE-2,6-DIONE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 5 NAG 33(C8 H15 N O6)
FORMUL 7 BMA 2(C6 H12 O6)
FORMUL 18 SO4 4(O4 S 2-)
FORMUL 19 SC3 8(C18 H23 N6 O2 1+)
FORMUL 41 HOH *1646(H2 O)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 GLU A 91 GLU A 97 1 7
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 ARG A 274 LEU A 276 5 3
HELIX 5 5 PRO A 290 ILE A 295 1 6
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 GLN A 505 1 9
HELIX 8 8 SER A 562 THR A 570 1 9
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
HELIX 11 11 THR A 600 MET A 616 1 17
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 LYS A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 GLY A 672 1 10
HELIX 15 15 ASN A 679 ASN A 685 1 7
HELIX 16 16 SER A 686 THR A 687 5 2
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 HIS A 712 ALA A 726 1 15
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 THR B 44 LYS B 50 1 7
HELIX 21 21 GLU B 91 GLY B 99 1 9
HELIX 22 22 ASP B 200 VAL B 207 1 8
HELIX 23 23 ARG B 274 LEU B 276 5 3
HELIX 24 24 PRO B 290 ILE B 295 1 6
HELIX 25 25 SER B 340 ALA B 342 5 3
HELIX 26 26 GLU B 421 MET B 425 5 5
HELIX 27 27 ASN B 463 ALA B 465 5 3
HELIX 28 28 ASN B 497 ASP B 506 1 10
HELIX 29 29 SER B 562 THR B 570 1 9
HELIX 30 30 GLY B 587 HIS B 592 1 6
HELIX 31 31 ALA B 593 ASN B 595 5 3
HELIX 32 32 THR B 600 SER B 614 1 15
HELIX 33 33 SER B 630 GLY B 641 1 12
HELIX 34 34 LYS B 658 TYR B 662 5 5
HELIX 35 35 ASP B 663 GLY B 672 1 10
HELIX 36 36 ASN B 679 ASN B 685 1 7
HELIX 37 37 SER B 686 THR B 687 5 2
HELIX 38 38 VAL B 688 VAL B 698 5 11
HELIX 39 39 HIS B 712 ALA B 726 1 15
HELIX 40 40 SER B 744 PHE B 763 1 20
HELIX 41 41 THR C 44 SER C 51 1 8
HELIX 42 42 ASN C 92 GLU C 97 1 6
HELIX 43 43 ASP C 200 VAL C 207 1 8
HELIX 44 44 ARG C 274 LEU C 276 5 3
HELIX 45 45 PRO C 290 ILE C 295 1 6
HELIX 46 46 SER C 340 ALA C 342 5 3
HELIX 47 47 GLU C 421 MET C 425 5 5
HELIX 48 48 ASN C 463 ALA C 465 5 3
HELIX 49 49 ASN C 497 GLN C 505 1 9
HELIX 50 50 SER C 562 THR C 570 1 9
HELIX 51 51 GLY C 587 HIS C 592 1 6
HELIX 52 52 ALA C 593 ASN C 595 5 3
HELIX 53 53 THR C 600 MET C 616 1 17
HELIX 54 54 SER C 630 GLY C 641 1 12
HELIX 55 55 LYS C 658 TYR C 662 5 5
HELIX 56 56 ASP C 663 GLY C 672 1 10
HELIX 57 57 ASN C 679 ASN C 685 1 7
HELIX 58 58 SER C 686 THR C 687 5 2
HELIX 59 59 VAL C 688 VAL C 698 5 11
HELIX 60 60 HIS C 712 ALA C 726 1 15
HELIX 61 61 SER C 744 PHE C 763 1 20
HELIX 62 62 THR D 44 LYS D 50 1 7
HELIX 63 63 GLU D 91 LEU D 98 1 8
HELIX 64 64 ASP D 200 VAL D 207 1 8
HELIX 65 65 ARG D 274 LEU D 276 5 3
HELIX 66 66 PRO D 290 ILE D 295 1 6
HELIX 67 67 SER D 340 ALA D 342 5 3
HELIX 68 68 GLU D 421 MET D 425 5 5
HELIX 69 69 ASN D 497 GLN D 505 1 9
HELIX 70 70 SER D 562 ASN D 572 1 11
HELIX 71 71 GLY D 587 HIS D 592 1 6
HELIX 72 72 ALA D 593 ASN D 595 5 3
HELIX 73 73 THR D 600 MET D 616 1 17
HELIX 74 74 SER D 630 GLY D 641 1 12
HELIX 75 75 LYS D 658 TYR D 662 5 5
HELIX 76 76 ASP D 663 GLY D 672 1 10
HELIX 77 77 ASN D 679 ASN D 685 1 7
HELIX 78 78 VAL D 688 VAL D 698 5 11
HELIX 79 79 HIS D 712 ALA D 726 1 15
HELIX 80 80 SER D 744 PHE D 763 1 20
SHEET 1 A 2 ARG A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N ARG A 41
SHEET 1 B 4 LEU A 60 TRP A 62 0
SHEET 2 B 4 GLU A 67 GLN A 72 -1 O LEU A 69 N GLN A 61
SHEET 3 B 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 B 4 SER A 86 LEU A 90 -1 O SER A 87 N LEU A 78
SHEET 1 C 4 ASP A 104 VAL A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O GLU A 117 N ASP A 104
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 TRP A 154 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 D 4 GLN A 183 ARG A 184 -1 O GLN A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASP A 272 -1 O LYS A 267 N GLN A 227
SHEET 4 F 4 THR A 283 ILE A 287 -1 O THR A 283 N ASP A 272
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 TRP A 337 ILE A 348 -1 O ILE A 338 N ASP A 329
SHEET 1 I 4 HIS A 363 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 LYS A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 THR A 395 PHE A 396 -1 O THR A 395 N HIS A 386
SHEET 1 J 4 VAL A 404 LEU A 410 0
SHEET 2 J 4 TYR A 414 SER A 419 -1 O ILE A 418 N ILE A 405
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 ASP A 438 CYS A 444 -1 O THR A 443 N ARG A 433
SHEET 1 K 4 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 K 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 K 4 ARG A 492 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 L 8 SER A 511 LEU A 519 0
SHEET 2 L 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 L 8 TYR A 540 GLU A 545 1 N LEU A 543 O ILE A 574
SHEET 5 L 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 L 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 L 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 M 2 ARG B 41 THR B 42 0
SHEET 2 M 2 VAL B 507 GLN B 508 1 O GLN B 508 N ARG B 41
SHEET 1 N 4 GLN B 61 TRP B 62 0
SHEET 2 N 4 GLU B 67 GLN B 72 -1 O LEU B 69 N GLN B 61
SHEET 3 N 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 N 4 SER B 86 LEU B 90 -1 O SER B 87 N LEU B 78
SHEET 1 O 4 ASP B 104 VAL B 107 0
SHEET 2 O 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 O 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 O 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 P 4 TRP B 154 TRP B 157 0
SHEET 2 P 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 P 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 P 4 GLN B 183 ARG B 184 -1 O GLN B 183 N VAL B 174
SHEET 1 Q 3 ILE B 194 ASN B 196 0
SHEET 2 Q 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 R 4 ILE B 194 ASN B 196 0
SHEET 2 R 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 4 THR B 265 ASP B 272 -1 O LYS B 267 N GLN B 227
SHEET 4 R 4 SER B 284 ILE B 287 -1 O ILE B 287 N PHE B 268
SHEET 1 S 2 LEU B 235 PHE B 240 0
SHEET 2 S 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 T 4 HIS B 298 THR B 307 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O GLN B 314 N GLY B 302
SHEET 3 T 4 TYR B 322 TYR B 330 -1 O CYS B 328 N ILE B 311
SHEET 4 T 4 TRP B 337 ILE B 338 -1 O ILE B 338 N ASP B 329
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O GLN B 314 N GLY B 302
SHEET 3 U 4 TYR B 322 TYR B 330 -1 O CYS B 328 N ILE B 311
SHEET 4 U 4 GLN B 344 ILE B 348 -1 O GLU B 347 N SER B 323
SHEET 1 V 4 HIS B 363 PHE B 364 0
SHEET 2 V 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 V 4 LYS B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 V 4 CYS B 394 PHE B 396 -1 O THR B 395 N HIS B 386
SHEET 1 W 4 VAL B 404 LEU B 410 0
SHEET 2 W 4 TYR B 414 SER B 419 -1 O ILE B 418 N ILE B 405
SHEET 3 W 4 ASN B 430 GLN B 435 -1 O ILE B 434 N LEU B 415
SHEET 4 W 4 VAL B 442 CYS B 444 -1 O THR B 443 N ARG B 433
SHEET 1 X 4 TYR B 457 PHE B 461 0
SHEET 2 X 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 X 4 LEU B 479 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 X 4 VAL B 493 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Y 8 SER B 511 LEU B 519 0
SHEET 2 Y 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Y 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Y 8 TYR B 540 GLU B 545 1 N LEU B 543 O ILE B 574
SHEET 5 Y 8 VAL B 619 TRP B 629 1 O ASP B 620 N TYR B 540
SHEET 6 Y 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Y 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Y 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 Z 2 ARG C 41 THR C 42 0
SHEET 2 Z 2 VAL C 507 GLN C 508 1 O GLN C 508 N ARG C 41
SHEET 1 AA 4 LEU C 60 TRP C 62 0
SHEET 2 AA 4 GLU C 67 GLN C 72 -1 O LEU C 69 N GLN C 61
SHEET 3 AA 4 ASN C 75 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 4 AA 4 SER C 86 LEU C 90 -1 O PHE C 89 N ILE C 76
SHEET 1 AB 4 THR C 102 VAL C 107 0
SHEET 2 AB 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AB 4 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 4 AB 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AC 4 TRP C 154 TRP C 157 0
SHEET 2 AC 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AC 4 ASP C 171 LYS C 175 -1 O TYR C 173 N TYR C 166
SHEET 4 AC 4 GLN C 183 ARG C 184 -1 O GLN C 183 N VAL C 174
SHEET 1 AD 3 ILE C 194 ASN C 196 0
SHEET 2 AD 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AE 4 ILE C 194 ASN C 196 0
SHEET 2 AE 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AE 4 THR C 265 ASP C 272 -1 O VAL C 271 N LEU C 223
SHEET 4 AE 4 THR C 283 ILE C 287 -1 O ILE C 287 N PHE C 268
SHEET 1 AF 2 LEU C 235 PHE C 240 0
SHEET 2 AF 2 LYS C 250 PRO C 255 -1 O VAL C 252 N TYR C 238
SHEET 1 AG 4 HIS C 298 THR C 307 0
SHEET 2 AG 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AG 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AG 4 TRP C 337 ILE C 338 -1 O ILE C 338 N ASP C 329
SHEET 1 AH 4 HIS C 298 THR C 307 0
SHEET 2 AH 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AH 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AH 4 GLN C 344 ILE C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AI 4 HIS C 363 PHE C 364 0
SHEET 2 AI 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AI 4 LYS C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AI 4 CYS C 394 PHE C 396 -1 O THR C 395 N HIS C 386
SHEET 1 AJ 4 VAL C 404 LEU C 410 0
SHEET 2 AJ 4 TYR C 414 SER C 419 -1 O TYR C 416 N GLU C 408
SHEET 3 AJ 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AJ 4 ASP C 438 CYS C 444 -1 O THR C 443 N ARG C 433
SHEET 1 AK 4 TYR C 457 PHE C 461 0
SHEET 2 AK 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AK 4 LEU C 479 SER C 484 -1 O HIS C 483 N TYR C 468
SHEET 4 AK 4 GLU C 490 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AL 8 SER C 511 LEU C 519 0
SHEET 2 AL 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AL 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AL 8 TYR C 540 VAL C 546 1 N LEU C 543 O ILE C 574
SHEET 5 AL 8 VAL C 619 TRP C 629 1 O TRP C 627 N VAL C 546
SHEET 6 AL 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AL 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 652
SHEET 8 AL 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AM 2 ARG D 41 THR D 42 0
SHEET 2 AM 2 VAL D 507 GLN D 508 1 O GLN D 508 N ARG D 41
SHEET 1 AN 4 GLN D 61 TRP D 62 0
SHEET 2 AN 4 GLU D 67 GLN D 72 -1 O LEU D 69 N GLN D 61
SHEET 3 AN 4 ASN D 75 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 4 AN 4 SER D 86 LEU D 90 -1 O LEU D 90 N ILE D 76
SHEET 1 AO 4 ASP D 104 VAL D 107 0
SHEET 2 AO 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AO 4 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 4 AO 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AP 4 TRP D 154 TRP D 157 0
SHEET 2 AP 4 LEU D 164 TRP D 168 -1 O VAL D 167 N TRP D 154
SHEET 3 AP 4 ASP D 171 LYS D 175 -1 O TYR D 173 N TYR D 166
SHEET 4 AP 4 GLN D 183 ARG D 184 -1 O GLN D 183 N VAL D 174
SHEET 1 AQ 3 ILE D 194 ASN D 196 0
SHEET 2 AQ 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AQ 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AR 4 ILE D 194 ASN D 196 0
SHEET 2 AR 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AR 4 THR D 265 ASP D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AR 4 SER D 284 ILE D 287 -1 O TYR D 285 N VAL D 270
SHEET 1 AS 2 LEU D 235 PHE D 240 0
SHEET 2 AS 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AT 4 HIS D 298 THR D 307 0
SHEET 2 AT 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AT 4 TYR D 322 TYR D 330 -1 O ILE D 324 N TRP D 315
SHEET 4 AT 4 TRP D 337 ILE D 338 -1 O ILE D 338 N ASP D 329
SHEET 1 AU 4 HIS D 298 THR D 307 0
SHEET 2 AU 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AU 4 TYR D 322 TYR D 330 -1 O ILE D 324 N TRP D 315
SHEET 4 AU 4 GLN D 344 ILE D 348 -1 O GLU D 347 N SER D 323
SHEET 1 AV 4 HIS D 363 PHE D 364 0
SHEET 2 AV 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AV 4 LYS D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AV 4 THR D 395 PHE D 396 -1 O THR D 395 N HIS D 386
SHEET 1 AW 4 VAL D 404 LEU D 410 0
SHEET 2 AW 4 TYR D 414 SER D 419 -1 O ILE D 418 N ILE D 405
SHEET 3 AW 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AW 4 ASP D 438 CYS D 444 -1 O THR D 443 N ARG D 433
SHEET 1 AX 4 TYR D 457 PHE D 461 0
SHEET 2 AX 4 TYR D 467 CYS D 472 -1 O GLN D 469 N SER D 460
SHEET 3 AX 4 LEU D 479 SER D 484 -1 O HIS D 483 N TYR D 468
SHEET 4 AX 4 LYS D 489 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AY 8 SER D 511 LEU D 519 0
SHEET 2 AY 8 THR D 522 LEU D 530 -1 O LEU D 530 N SER D 511
SHEET 3 AY 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AY 8 TYR D 540 VAL D 546 1 N GLU D 545 O ALA D 576
SHEET 5 AY 8 VAL D 619 TRP D 629 1 O ASP D 620 N TYR D 540
SHEET 6 AY 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AY 8 GLU D 699 GLY D 705 1 O LEU D 701 N ALA D 652
SHEET 8 AY 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 2 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 3 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 4 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 5 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 6 CYS B 444 CYS B 447 1555 1555 2.02
SSBOND 7 CYS B 454 CYS B 472 1555 1555 2.05
SSBOND 8 CYS B 649 CYS B 762 1555 1555 2.06
SSBOND 9 CYS C 385 CYS C 394 1555 1555 2.05
SSBOND 10 CYS C 444 CYS C 447 1555 1555 2.02
SSBOND 11 CYS C 454 CYS C 472 1555 1555 2.06
SSBOND 12 CYS C 649 CYS C 762 1555 1555 2.06
SSBOND 13 CYS D 385 CYS D 394 1555 1555 2.04
SSBOND 14 CYS D 444 CYS D 447 1555 1555 2.03
SSBOND 15 CYS D 454 CYS D 472 1555 1555 2.05
SSBOND 16 CYS D 649 CYS D 762 1555 1555 2.06
LINK ND2 ASN A 85 C1 NAG A 767A 1555 1555 1.46
LINK ND2 ASN A 92 C1 NAG A 768A 1555 1555 1.46
LINK ND2 ASN A 229 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 279 C1 NAG A 771A 1555 1555 1.45
LINK ND2 ASN A 321 C1 NAG A 772A 1555 1555 1.45
LINK ND2 ASN A 685 C1 NAG F 1 1555 1555 1.46
LINK ND2 ASN B 85 C1 NAG B 767A 1555 1555 1.45
LINK ND2 ASN B 92 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN B 229 C1 NAG B 771A 1555 1555 1.45
LINK ND2 ASN B 279 C1 NAG B 772A 1555 1555 1.45
LINK ND2 ASN B 321 C1 NAG B 773A 1555 1555 1.46
LINK ND2 ASN B 685 C1 NAG H 1 1555 1555 1.46
LINK ND2 ASN C 85 C1 NAG C 767A 1555 1555 1.45
LINK ND2 ASN C 92 C1 NAG C 768A 1555 1555 1.45
LINK ND2 ASN C 229 C1 NAG C 769A 1555 1555 1.45
LINK ND2 ASN C 279 C1 NAG C 770A 1555 1555 1.45
LINK ND2 ASN C 321 C1 NAG C 771A 1555 1555 1.45
LINK ND2 ASN C 685 C1 NAG I 1 1555 1555 1.45
LINK ND2 ASN D 85 C1 NAG D 767A 1555 1555 1.46
LINK ND2 ASN D 92 C1 NAG J 1 1555 1555 1.45
LINK ND2 ASN D 229 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN D 279 C1 NAG D 773A 1555 1555 1.45
LINK ND2 ASN D 321 C1 NAG L 1 1555 1555 1.45
LINK ND2 ASN D 685 C1 NAG M 1 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.39
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.39
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.38
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.39
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.39
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.39
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.39
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.39
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.40
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.39
CISPEP 1 GLY A 474 PRO A 475 0 0.79
CISPEP 2 GLY B 474 PRO B 475 0 0.49
CISPEP 3 GLY C 474 PRO C 475 0 0.08
CISPEP 4 GLY D 474 PRO D 475 0 0.28
CRYST1 63.110 118.960 133.760 112.79 95.74 90.63 P 1 4
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 0.015845 0.000174 0.001804 0.00000
SCALE2 0.000000 0.008407 0.003565 0.00000
SCALE3 0.000000 0.000000 0.008162 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
