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HEADER HYDROLASE 16-MAR-03 1ORV
TITLE CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE IV (CD26)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 EC: 3.4.14.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 OTHER_DETAILS: KIDNEY
KEYWDS SERINE PROTEASE, MECHANISM, OXYANION HOLE, SUBSTRATE
KEYWDS 2 CHANNELING, DRUG DESIGN, DIABETES MELLITUS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ENGEL,T.HOFFMANN,L.WAGNER,M.WERMANN,U.HEISER,
AUTHOR 2 R.KIEFERSAUER,R.HUBER,W.BODE,H.U.DEMUTH,H.BRANDSTETTER
REVDAT 1 06-MAY-03 1ORV 0
JRNL AUTH M.ENGEL,T.HOFFMANN,L.WAGNER,M.WERMANN,U.HEISER,
JRNL AUTH 2 R.KIEFERSAUER,R.HUBER,W.BODE,H.U.DEMUTH,
JRNL AUTH 3 H.BRANDSTETTER
JRNL TITL THE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV
JRNL TITL 2 (CD26) REVEALS ITS FUNCTIONAL REGULATION AND
JRNL TITL 3 ENZYMATIC MECHANISM
JRNL REF PROC.NAT.ACAD.SCI.USA V. 100 5063 2003
JRNL REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 309996
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) : 0.217
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 15446
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 48262
REMARK 3 BIN R VALUE (WORKING SET) : 0.3360
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2605
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 : 504
REMARK 3 SOLVENT ATOMS : 1468
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.97000
REMARK 3 B22 (A**2) : -5.66000
REMARK 3 B33 (A**2) : -0.31000
REMARK 3 B12 (A**2) : 1.26000
REMARK 3 B13 (A**2) : -0.75000
REMARK 3 B23 (A**2) : 0.24000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.89
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) : 1.310 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.960 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.020 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.900 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 54.89
REMARK 3
REMARK 3 NCS MODEL : NULL
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_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : SUL.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : SUL.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ORV COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-2003.
REMARK 100 THE RCSB ID CODE IS RCSB018605.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-2000; 07-SEP-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0; 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG ; EMBL/
REMARK 200 DESY, HAMBURG
REMARK 200 BEAMLINE : BW6; BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05030; 1.00500, 1.00920,
REMARK 200 0.95000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : UNDULATOR; UNDULATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 320230
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 19.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MAIN
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.1
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 2000, 0.1 M AMMONIUM
REMARK 280 SULFATE, 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
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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, B, C, D, E, F, G, H, I,
REMARK 350 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 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 (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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 255 CB PRO A 255 CG 0.058
REMARK 500 PRO A 257 CB PRO A 257 CG 0.058
REMARK 500 PRO A 257 CG PRO A 257 CD 0.067
REMARK 500 PRO A 264 CB PRO A 264 CG 0.075
REMARK 500 PRO A 655 CB PRO A 655 CG 0.058
REMARK 500 VAL A 711 CB VAL A 711 CG1 0.056
REMARK 500 MET A 733 SD MET A 733 CE -0.074
REMARK 500 PRO B 257 CG PRO B 257 CD 0.061
REMARK 500 ARG B 336 CB ARG B 336 CG -0.057
REMARK 500 MET B 733 SD MET B 733 CE -0.069
REMARK 500 MET B 746 CG MET B 746 SD 0.061
REMARK 500 MET B 746 SD MET B 746 CE 0.065
REMARK 500 PRO C 257 CG PRO C 257 CD 0.056
REMARK 500 PRO C 264 CB PRO C 264 CG 0.058
REMARK 500 PRO C 362 CB PRO C 362 CG 0.066
REMARK 500 PRO D 234 CB PRO D 234 CG 0.057
REMARK 500 PRO D 257 CG PRO D 257 CD 0.058
REMARK 500 MET D 638 SD MET D 638 CE 0.058
REMARK 500 MET D 671 SD MET D 671 CE -0.068
REMARK 500 MET D 689 SD MET D 689 CE -0.066
REMARK 500 LEU D 719 CG LEU D 719 CD1 0.061
REMARK 500 MET D 733 SD MET D 733 CE -0.098
REMARK 500 MET D 746 SD MET D 746 CE -0.112
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 ASN A 92 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ILE A 143 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 GLU A 206 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU A 214 CA - CB - CG ANGL. DEV. = 11.0 DEGREES
REMARK 500 ILE A 236 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 PHE A 240 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 PRO A 255 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 LEU A 300 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 GLN A 388 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 GLU A 448 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 SER A 458 N - CA - C ANGL. DEV. =-12.9 DEGREES
REMARK 500 ILE A 529 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 LEU A 542 CA - CB - CG ANGL. DEV. = 9.8 DEGREES
REMARK 500 TYR A 547 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 LEU A 561 N - CA - C ANGL. DEV. =-13.4 DEGREES
REMARK 500 VAL A 656 N - CA - C ANGL. DEV. =-13.5 DEGREES
REMARK 500 GLU A 699 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 VAL A 711 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 ALA A 743 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 SER B 158 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLU B 206 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU B 214 CA - CB - CG ANGL. DEV. = 10.7 DEGREES
REMARK 500 ILE B 236 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 PRO B 255 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 LEU B 300 N - CA - C ANGL. DEV. =-13.2 DEGREES
REMARK 500 GLN B 388 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 SER B 458 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 ILE B 529 N - CA - C ANGL. DEV. =-11.8 DEGREES
REMARK 500 TYR B 547 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 ALA B 548 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 LEU B 561 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 VAL B 656 N - CA - C ANGL. DEV. =-12.8 DEGREES
REMARK 500 VAL B 711 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ALA B 743 N - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG C 40 N - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 THR C 102 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 ASN C 103 N - CA - C ANGL. DEV. = 18.7 DEGREES
REMARK 500 ASP C 104 N - CA - C ANGL. DEV. =-18.4 DEGREES
REMARK 500 ASP C 104 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 GLU C 206 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 ILE C 236 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 PHE C 240 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 PRO C 255 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 LEU C 300 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 GLN C 388 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 SER C 458 N - CA - C ANGL. DEV. =-12.2 DEGREES
REMARK 500 LEU C 542 CA - CB - CG ANGL. DEV. = 10.7 DEGREES
REMARK 500 TYR C 547 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 LEU C 561 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 VAL C 656 N - CA - C ANGL. DEV. =-13.2 DEGREES
REMARK 500 VAL C 711 N - CA - C ANGL. DEV. =-12.0 DEGREES
REMARK 500 ALA C 743 N - CA - C ANGL. DEV. = 10.9 DEGREES
REMARK 500 SER D 158 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 GLU D 206 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 ILE D 236 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 PHE D 240 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 PRO D 255 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 LEU D 300 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 ALA D 319 N - CA - C ANGL. DEV. =-15.2 DEGREES
REMARK 500 TRP D 337 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLN D 388 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 SER D 458 N - CA - C ANGL. DEV. =-13.0 DEGREES
REMARK 500 ASN D 463 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 ILE D 529 N - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 PRO D 541 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 TYR D 547 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 LEU D 561 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 VAL D 656 N - CA - C ANGL. DEV. =-12.8 DEGREES
REMARK 500 VAL D 711 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 ALA D 743 N - CA - C ANGL. DEV. = 10.8 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 93 -30.54 64.27
REMARK 500 LEU A 491 -70.46 52.66
REMARK 500 SER A 630 -116.22 62.48
REMARK 500 ARG B 40 124.09 59.98
REMARK 500 LEU B 491 -66.22 42.81
REMARK 500 SER B 630 -116.44 60.30
REMARK 500 GLU C 73 -73.24 65.70
REMARK 500 ASN C 103 162.99 21.25
REMARK 500 GLU D 82 -58.30 72.89
REMARK 500 SER D 630 -116.78 62.10
DBREF 1ORV A 39 766 GB 28566188 AAO43404 39 766
DBREF 1ORV B 39 766 GB 28566188 AAO43404 39 766
DBREF 1ORV C 39 766 GB 28566188 AAO43404 39 766
DBREF 1ORV D 39 766 GB 28566188 AAO43404 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 1ORV ASN A 85 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN A 92 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN A 229 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN A 279 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN A 321 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN A 685 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN B 85 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN B 92 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN B 229 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN B 279 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN B 321 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN B 685 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN C 85 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN C 92 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN C 229 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN C 279 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN C 321 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN C 685 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN D 85 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN D 92 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN D 229 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN D 279 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN D 321 ASN GLYCOSYLATION SITE
MODRES 1ORV ASN D 685 ASN GLYCOSYLATION SITE
HET NAG A 85A 14
HET NAG A 92A 14
HET NAG E 229A 14
HET NAG E 229B 14
HET NAG A 279A 14
HET NAG A 321A 14
HET NAG F 685A 14
HET NAG F 685B 14
HET NAG B 85A 14
HET NAG G 92A 14
HET NAG G 92B 14
HET MAN G 92C 11
HET NAG B 229A 14
HET NAG B 279A 14
HET NAG B 321A 14
HET NAG H 685A 14
HET NAG H 685B 14
HET NAG C 85A 14
HET NAG C 92A 14
HET NAG C 229A 14
HET NAG C 279A 14
HET NAG C 321A 14
HET NAG I 685A 14
HET NAG I 685B 14
HET NAG D 85A 14
HET NAG J 92A 14
HET NAG J 92B 14
HET MAN J 92C 11
HET NAG K 229A 14
HET NAG K 229B 14
HET NAG D 279A 14
HET NAG L 321A 14
HET NAG L 321B 14
HET NAG M 685A 14
HET NAG M 685B 14
HET SUL 1500 5
HET SUL 1501 5
HET SUL 1502 5
HET SUL 1503 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM SUL SULFATE ANION
HETSYN NAG NAG
FORMUL 5 NAG 33(C8 H15 N1 O6)
FORMUL 12 MAN 2(C6 H12 O6)
FORMUL 29 SUL 4(O4 S1 2-)
FORMUL 33 HOH *1468(H2 O1)
HELIX 1 1 THR A 44 SER A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 ARG A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 SER A 340 ALA A 342 5 3
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 LYS A 615 1 16
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 SER B 51 1 8
HELIX 21 21 ASN B 92 GLY B 99 1 8
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 ASP C 200 VAL C 207 1 8
HELIX 43 43 ARG C 274 LEU C 276 5 3
HELIX 44 44 PRO C 290 ILE C 295 1 6
HELIX 45 45 SER C 340 ALA C 342 5 3
HELIX 46 46 GLU C 421 MET C 425 5 5
HELIX 47 47 ASN C 463 ALA C 465 5 3
HELIX 48 48 ASN C 497 ASP C 506 1 10
HELIX 49 49 SER C 562 THR C 570 1 9
HELIX 50 50 GLY C 587 HIS C 592 1 6
HELIX 51 51 ALA C 593 ASN C 595 5 3
HELIX 52 52 THR C 600 MET C 616 1 17
HELIX 53 53 SER C 630 GLY C 641 1 12
HELIX 54 54 LYS C 658 TYR C 662 5 5
HELIX 55 55 ASP C 663 GLY C 672 1 10
HELIX 56 56 ASN C 679 ASN C 685 1 7
HELIX 57 57 SER C 686 THR C 687 5 2
HELIX 58 58 VAL C 688 VAL C 698 5 11
HELIX 59 59 HIS C 712 ALA C 726 1 15
HELIX 60 60 SER C 744 PHE C 763 1 20
HELIX 61 61 THR D 44 LYS D 50 1 7
HELIX 62 62 ASN D 92 GLU D 97 1 6
HELIX 63 63 ASP D 200 VAL D 207 1 8
HELIX 64 64 ARG D 274 LEU D 276 5 3
HELIX 65 65 PRO D 290 ILE D 295 1 6
HELIX 66 66 SER D 340 ALA D 342 5 3
HELIX 67 67 GLU D 421 MET D 425 5 5
HELIX 68 68 ASN D 497 GLN D 505 1 9
HELIX 69 69 SER D 562 THR D 570 1 9
HELIX 70 70 GLY D 587 HIS D 592 1 6
HELIX 71 71 ALA D 593 ASN D 595 5 3
HELIX 72 72 THR D 600 LYS D 615 1 16
HELIX 73 73 SER D 630 GLY D 641 1 12
HELIX 74 74 LYS D 658 TYR D 662 5 5
HELIX 75 75 ASP D 663 GLY D 672 1 10
HELIX 76 76 ASN D 679 ASN D 685 1 7
HELIX 77 77 SER D 686 THR D 687 5 2
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 4 LEU A 60 TRP A 62 0
SHEET 2 A 4 GLU A 67 GLN A 72 -1 O LEU A 69 N GLN A 61
SHEET 3 A 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 A 4 SER A 87 LEU A 90 -1 O SER A 87 N LEU A 78
SHEET 1 B 4 ASP A 104 VAL A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 B 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 TRP A 154 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 C 4 GLN A 183 ARG A 184 -1 O GLN A 183 N VAL A 174
SHEET 1 D 4 THR A 283 ILE A 287 0
SHEET 2 D 4 THR A 265 ASP A 272 -1 N ASP A 272 O THR A 283
SHEET 3 D 4 PHE A 222 ASN A 229 -1 N ASN A 229 O THR A 265
SHEET 4 D 4 ILE A 194 ASN A 196 -1 N TYR A 195 O PHE A 228
SHEET 1 E 4 THR A 283 ILE A 287 0
SHEET 2 E 4 THR A 265 ASP A 272 -1 N ASP A 272 O THR A 283
SHEET 3 E 4 PHE A 222 ASN A 229 -1 N ASN A 229 O THR A 265
SHEET 4 E 4 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 G 4 HIS A 298 THR A 307 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 G 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 G 4 TRP A 337 ILE A 338 -1 O ILE A 338 N ASP A 329
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O 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 GLN A 344 ILE A 348 -1 O GLU A 347 N SER A 323
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 CYS A 394 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 TYR A 416 N ALA A 409
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 LYS A 489 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 VAL A 546 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 LEU A 702
SHEET 1 M 4 LEU B 60 TRP B 62 0
SHEET 2 M 4 GLU B 67 GLN B 72 -1 O LEU B 69 N GLN B 61
SHEET 3 M 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 M 4 SER B 86 LEU B 90 -1 O SER B 87 N LEU B 78
SHEET 1 N 4 ASP B 104 VAL B 107 0
SHEET 2 N 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 N 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 N 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 O 4 TRP B 154 TRP B 157 0
SHEET 2 O 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 O 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 O 4 GLN B 183 ARG B 184 -1 O GLN B 183 N VAL B 174
SHEET 1 P 4 SER B 284 ILE B 287 0
SHEET 2 P 4 THR B 265 ASP B 272 -1 N VAL B 270 O TYR B 285
SHEET 3 P 4 PHE B 222 ASN B 229 -1 N GLN B 227 O LYS B 267
SHEET 4 P 4 ILE B 194 ASN B 196 -1 N TYR B 195 O PHE B 228
SHEET 1 Q 4 SER B 284 ILE B 287 0
SHEET 2 Q 4 THR B 265 ASP B 272 -1 N VAL B 270 O TYR B 285
SHEET 3 Q 4 PHE B 222 ASN B 229 -1 N GLN B 227 O LYS B 267
SHEET 4 Q 4 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 R 2 LEU B 235 PHE B 240 0
SHEET 2 R 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 S 4 HIS B 298 THR B 307 0
SHEET 2 S 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 S 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 S 4 TRP B 337 ILE B 338 -1 O ILE B 338 N ASP B 329
SHEET 1 T 4 HIS B 298 THR B 307 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 T 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 T 4 GLN B 344 ILE B 348 -1 O GLU B 347 N SER B 323
SHEET 1 U 4 HIS B 363 PHE B 364 0
SHEET 2 U 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 U 4 LYS B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 U 4 CYS B 394 PHE B 396 -1 O THR B 395 N HIS B 386
SHEET 1 V 4 VAL B 404 LEU B 410 0
SHEET 2 V 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 V 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 V 4 VAL B 442 CYS B 444 -1 O THR B 443 N ARG B 433
SHEET 1 W 4 TYR B 457 PHE B 461 0
SHEET 2 W 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 W 4 LEU B 479 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 W 4 VAL B 493 GLU B 495 -1 O LEU B 494 N TYR B 480
SHEET 1 X 8 SER B 511 LEU B 519 0
SHEET 2 X 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 X 8 ILE B 574 ASP B 579 -1 O VAL B 575 N ILE B 529
SHEET 4 X 8 TYR B 540 GLU B 545 1 N LEU B 543 O ILE B 574
SHEET 5 X 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 X 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 X 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 X 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
SHEET 1 Y 2 ARG C 41 THR C 42 0
SHEET 2 Y 2 VAL C 507 GLN C 508 1 O GLN C 508 N ARG C 41
SHEET 1 Z 4 LEU C 60 TRP C 62 0
SHEET 2 Z 4 GLU C 67 GLN C 72 -1 O LEU C 69 N GLN C 61
SHEET 3 Z 4 ASN C 75 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 4 Z 4 SER C 86 LEU C 90 -1 O SER C 87 N LEU C 78
SHEET 1 AA 4 TYR C 105 VAL C 107 0
SHEET 2 AA 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AA 4 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 4 AA 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AB 4 TRP C 154 TRP C 157 0
SHEET 2 AB 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AB 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AB 4 GLN C 183 ARG C 184 -1 O GLN C 183 N VAL C 174
SHEET 1 AC 4 SER C 284 ILE C 287 0
SHEET 2 AC 4 THR C 265 ASP C 272 -1 N VAL C 270 O TYR C 285
SHEET 3 AC 4 PHE C 222 ASN C 229 -1 N TYR C 225 O PHE C 269
SHEET 4 AC 4 ILE C 194 ASN C 196 -1 N TYR C 195 O PHE C 228
SHEET 1 AD 4 SER C 284 ILE C 287 0
SHEET 2 AD 4 THR C 265 ASP C 272 -1 N VAL C 270 O TYR C 285
SHEET 3 AD 4 PHE C 222 ASN C 229 -1 N TYR C 225 O PHE C 269
SHEET 4 AD 4 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AE 2 LEU C 235 PHE C 240 0
SHEET 2 AE 2 LYS C 250 PRO C 255 -1 O VAL C 252 N TYR C 238
SHEET 1 AF 4 HIS C 298 THR C 307 0
SHEET 2 AF 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AF 4 TYR C 322 TYR C 330 -1 O ILE C 324 N TRP C 315
SHEET 4 AF 4 TRP C 337 ILE C 338 -1 O ILE C 338 N ASP C 329
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 ILE C 324 N TRP C 315
SHEET 4 AG 4 GLN C 344 ILE C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AH 4 HIS C 363 PHE C 364 0
SHEET 2 AH 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AH 4 LYS C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AH 4 CYS C 394 PHE C 396 -1 O THR C 395 N HIS C 386
SHEET 1 AI 4 VAL C 404 LEU C 410 0
SHEET 2 AI 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AI 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AI 4 ASP C 438 CYS C 444 -1 O THR C 443 N ARG C 433
SHEET 1 AJ 4 TYR C 457 PHE C 461 0
SHEET 2 AJ 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AJ 4 LEU C 479 SER C 484 -1 O THR C 481 N LEU C 470
SHEET 4 AJ 4 GLU C 490 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AK 8 SER C 511 LEU C 519 0
SHEET 2 AK 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AK 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AK 8 TYR C 540 GLU C 545 1 N LEU C 543 O ILE C 574
SHEET 5 AK 8 VAL C 619 TRP C 629 1 O ASP C 620 N TYR C 540
SHEET 6 AK 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AK 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 652
SHEET 8 AK 8 GLN C 731 TYR C 735 1 O GLN C 731 N LEU C 702
SHEET 1 AL 2 ARG D 41 THR D 42 0
SHEET 2 AL 2 VAL D 507 GLN D 508 1 O GLN D 508 N ARG D 41
SHEET 1 AM 4 LEU D 60 TRP D 62 0
SHEET 2 AM 4 GLU D 67 GLN D 72 -1 O LEU D 69 N GLN D 61
SHEET 3 AM 4 ASN D 75 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 4 AM 4 SER D 86 LEU D 90 -1 O SER D 87 N LEU D 78
SHEET 1 AN 4 THR D 102 VAL D 107 0
SHEET 2 AN 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AN 4 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 4 AN 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AO 4 TRP D 154 TRP D 157 0
SHEET 2 AO 4 LEU D 164 TRP D 168 -1 O VAL D 167 N TRP D 154
SHEET 3 AO 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AO 4 GLN D 183 ARG D 184 -1 O GLN D 183 N VAL D 174
SHEET 1 AP 4 SER D 284 ILE D 287 0
SHEET 2 AP 4 THR D 265 ASP D 272 -1 N PHE D 268 O ILE D 287
SHEET 3 AP 4 PHE D 222 ASN D 229 -1 N GLN D 227 O LYS D 267
SHEET 4 AP 4 ILE D 194 ASN D 196 -1 N TYR D 195 O PHE D 228
SHEET 1 AQ 4 SER D 284 ILE D 287 0
SHEET 2 AQ 4 THR D 265 ASP D 272 -1 N PHE D 268 O ILE D 287
SHEET 3 AQ 4 PHE D 222 ASN D 229 -1 N GLN D 227 O LYS D 267
SHEET 4 AQ 4 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AR 2 LEU D 235 PHE D 240 0
SHEET 2 AR 2 LYS D 250 PRO D 255 -1 O VAL D 252 N TYR D 238
SHEET 1 AS 4 HIS D 298 THR D 307 0
SHEET 2 AS 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AS 4 TYR D 322 TYR D 330 -1 O ILE D 324 N TRP D 315
SHEET 4 AS 4 TRP D 337 ILE D 338 -1 O ILE D 338 N ASP D 329
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 GLN D 344 ILE D 348 -1 O GLU D 347 N SER D 323
SHEET 1 AU 4 HIS D 363 PHE D 364 0
SHEET 2 AU 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AU 4 LYS D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AU 4 CYS D 394 PHE D 396 -1 O THR D 395 N HIS D 386
SHEET 1 AV 4 VAL D 404 LEU D 410 0
SHEET 2 AV 4 TYR D 414 SER D 419 -1 O TYR D 416 N ALA D 409
SHEET 3 AV 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AV 4 ASP D 438 CYS D 444 -1 O THR D 443 N ARG D 433
SHEET 1 AW 4 TYR D 457 PHE D 461 0
SHEET 2 AW 4 TYR D 467 CYS D 472 -1 O ARG D 471 N SER D 458
SHEET 3 AW 4 LEU D 479 SER D 484 -1 O LEU D 479 N CYS D 472
SHEET 4 AW 4 GLU D 490 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AX 8 SER D 511 LEU D 519 0
SHEET 2 AX 8 THR D 522 LEU D 530 -1 O LEU D 530 N SER D 511
SHEET 3 AX 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AX 8 TYR D 540 GLU D 545 1 N LEU D 543 O ILE D 574
SHEET 5 AX 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 542
SHEET 6 AX 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AX 8 GLU D 699 GLY D 705 1 O ILE D 703 N ALA D 652
SHEET 8 AX 8 GLN D 731 TYR D 735 1 O GLN D 731 N LEU D 702
SSBOND 1 CYS A 385 CYS A 394
SSBOND 2 CYS A 444 CYS A 447
SSBOND 3 CYS A 454 CYS A 472
SSBOND 4 CYS A 649 CYS A 762
SSBOND 5 CYS B 385 CYS B 394
SSBOND 6 CYS B 444 CYS B 447
SSBOND 7 CYS B 454 CYS B 472
SSBOND 8 CYS B 649 CYS B 762
SSBOND 9 CYS C 385 CYS C 394
SSBOND 10 CYS C 444 CYS C 447
SSBOND 11 CYS C 454 CYS C 472
SSBOND 12 CYS C 649 CYS C 762
SSBOND 13 CYS D 385 CYS D 394
SSBOND 14 CYS D 444 CYS D 447
SSBOND 15 CYS D 454 CYS D 472
SSBOND 16 CYS D 649 CYS D 762
LINK ND2 ASN A 85 C1 NAG A 85A
LINK ND2 ASN A 92 C1 NAG A 92A
LINK ND2 ASN A 229 C1 NAG E 229A
LINK ND2 ASN A 279 C1 NAG A 279A
LINK ND2 ASN A 321 C1 NAG A 321A
LINK ND2 ASN A 685 C1 NAG F 685A
LINK ND2 ASN B 85 C1 NAG B 85A
LINK ND2 ASN B 92 C1 NAG G 92A
LINK ND2 ASN B 229 C1 NAG B 229A
LINK ND2 ASN B 279 C1 NAG B 279A
LINK ND2 ASN B 321 C1 NAG B 321A
LINK ND2 ASN B 685 C1 NAG H 685A
LINK ND2 ASN C 85 C1 NAG C 85A
LINK ND2 ASN C 92 C1 NAG C 92A
LINK ND2 ASN C 229 C1 NAG C 229A
LINK ND2 ASN C 279 C1 NAG C 279A
LINK ND2 ASN C 321 C1 NAG C 321A
LINK ND2 ASN C 685 C1 NAG I 685A
LINK ND2 ASN D 85 C1 NAG D 85A
LINK ND2 ASN D 92 C1 NAG J 92A
LINK ND2 ASN D 229 C1 NAG K 229A
LINK ND2 ASN D 279 C1 NAG D 279A
LINK ND2 ASN D 321 C1 NAG L 321A
LINK ND2 ASN D 685 C1 NAG M 685A
LINK O4 NAG E 229A C1 NAG E 229B
LINK O4 NAG F 685A C1 NAG F 685B
LINK O4 NAG G 92A C1 NAG G 92B
LINK O4 NAG G 92B C1 MAN G 92C
LINK O4 NAG H 685A C1 NAG H 685B
LINK O4 NAG I 685A C1 NAG I 685B
LINK O4 NAG J 92A C1 NAG J 92B
LINK O4 NAG J 92B C1 MAN J 92C
LINK O4 NAG K 229A C1 NAG K 229B
LINK O4 NAG L 321A C1 NAG L 321B
LINK O4 NAG M 685A C1 NAG M 685B
CISPEP 1 GLY A 474 PRO A 475 0 0.24
CISPEP 2 GLY B 474 PRO B 475 0 0.37
CISPEP 3 GLY C 474 PRO C 475 0 0.23
CISPEP 4 GLY D 474 PRO D 475 0 0.65
CRYST1 62.000 118.180 133.590 112.76 94.93 91.14 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 0.016129 0.000321 0.001647 0.00000
SCALE2 0.000000 0.008463 0.003586 0.00000
SCALE3 0.000000 0.000000 0.008160 0.00000
TER 5967 PRO A 766
TER 11934 PRO B 766
TER 17901 PRO C 766
TER 23868 PRO D 766
MASTER 353 0 39 80 204 0 0 625836 4 560 224
END |