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HEADER HYDROLASE 12-JUL-07 2QKY
TITLE COMPLEX STRUCTURE OF DIPEPTIDYL PEPTIDASE IV AND A
TITLE 2 OXADIAZOLYL KETONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 (EC 3.4.14.5) (DIPEPTIDYL
COMPND 3 PEPTIDASE IV) (DPP IV) (T-CELL ACTIVATION ANTIGEN CD26)
COMPND 4 (TP103) (ADENOSINE DEAMINASE COMPLEXING PROTEIN 2) (ADABP)
COMPND 5 (DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM) (DIPEPTIDYL
COMPND 6 PEPTIDASE IV SOLUBLE FORM);
COMPND 7 CHAIN: A, B, C, D;
COMPND 8 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 9 EC: 3.4.14.5;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DPP4, ADCP2, CD26;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: HI5
KEYWDS BETA-PROPELLER, DIMER, AMINOPEPTIDASE, GLYCOPROTEIN,
KEYWDS 2 HYDROLASE, MEMBRANE, PROTEASE, SECRETED, SERINE PROTEASE,
KEYWDS 3 SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.-H.KIM,S.Y.HONG,K.D.KOO,C.-S.LEE,G.T.KIM,H.O.HAN
REVDAT 1 15-JUL-08 2QKY 0
JRNL AUTH K.D.KOO,M.J.KIM,S.KIM,K.H.KIM,S.Y.HONG,G.C.HUR,
JRNL AUTH 2 H.J.YIM,G.T.KIM,H.O.HAN,O.H.KWON,T.S.KWON,J.S.KOH,
JRNL AUTH 3 C.S.LEE
JRNL TITL SYNTHESIS, SAR, AND X-RAY STRUCTURE OF NOVEL
JRNL TITL 2 POTENT DPPIV INHIBITORS: OXADIAZOLYL KETONES.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 4167 2007
JRNL REFN ASTM BMCLE8 UK ISSN 0960-894X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.7
REMARK 3 NUMBER OF REFLECTIONS : 59024
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4822
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23860
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 104
REMARK 3 SOLVENT ATOMS : 311
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.77600
REMARK 3 B22 (A**2) : 3.70200
REMARK 3 B33 (A**2) : 1.07400
REMARK 3 B12 (A**2) : 2.63300
REMARK 3 B13 (A**2) : -2.84300
REMARK 3 B23 (A**2) : -1.31300
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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 10.00
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 : 13Z.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QKY COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB043728.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-2004
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : MACSCIENCE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAC SCIENCE DIP-2030
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64035
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 1.890
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.110
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1N1M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG MME 2K, 0.1M BICINE, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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
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: 4320 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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: 4300 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 OD1 ASP A 65 N GLU A 464 2.04
REMARK 500 OG SER A 630 O2 13Z A 767 2.12
REMARK 500 OG SER C 630 O2 13Z C 767 2.15
REMARK 500 OE2 GLU B 660 NH2 ARG B 684 2.18
REMARK 500 O ASP D 110 N GLN D 112 2.19
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS D 394 CA - CB - SG ANGL. DEV. = 7.9 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 TYR A 48 -68.05 -92.98
REMARK 500 ASN A 51 29.96 87.17
REMARK 500 LEU A 57 -167.15 -113.56
REMARK 500 TYR A 58 82.90 -161.00
REMARK 500 SER A 64 -162.96 -125.57
REMARK 500 HIS A 66 16.35 -155.55
REMARK 500 ASN A 74 -7.36 57.75
REMARK 500 PHE A 95 45.58 -96.38
REMARK 500 ASP A 96 -9.24 -59.77
REMARK 500 GLU A 97 50.04 -152.89
REMARK 500 GLN A 123 -100.20 -116.31
REMARK 500 TRP A 124 -130.42 -90.79
REMARK 500 TYR A 128 161.39 176.53
REMARK 500 LEU A 137 1.34 -64.26
REMARK 500 ASN A 138 -86.10 -98.56
REMARK 500 LYS A 139 14.60 -61.29
REMARK 500 ARG A 140 50.97 36.79
REMARK 500 ILE A 143 143.54 -28.64
REMARK 500 GLU A 146 96.70 69.29
REMARK 500 PRO A 149 157.74 -38.46
REMARK 500 ASN A 151 39.32 75.62
REMARK 500 TRP A 154 140.08 -178.42
REMARK 500 HIS A 162 24.73 -147.39
REMARK 500 ASN A 169 30.96 72.24
REMARK 500 PRO A 181 -177.41 -50.74
REMARK 500 LYS A 190 96.15 -168.24
REMARK 500 GLU A 191 125.37 -24.44
REMARK 500 ILE A 193 -57.66 -135.08
REMARK 500 ASP A 200 -166.02 -108.91
REMARK 500 VAL A 207 -49.04 -130.89
REMARK 500 SER A 209 43.86 28.76
REMARK 500 ALA A 210 147.48 -173.86
REMARK 500 ALA A 213 58.59 -164.33
REMARK 500 TRP A 216 172.14 -59.62
REMARK 500 THR A 231 -62.61 -20.33
REMARK 500 SER A 242 -154.26 42.24
REMARK 500 ASP A 243 -157.57 -54.11
REMARK 500 LEU A 246 99.08 -63.17
REMARK 500 ALA A 261 -155.77 -62.73
REMARK 500 SER A 275 73.01 -104.61
REMARK 500 ALA A 282 158.77 -45.97
REMARK 500 ASP A 302 131.70 -173.56
REMARK 500 ALA A 306 -61.90 -96.14
REMARK 500 GLN A 320 33.36 -52.70
REMARK 500 SER A 333 -80.69 -63.75
REMARK 500 SER A 334 -14.54 -48.78
REMARK 500 ARG A 358 149.48 -173.22
REMARK 500 SER A 370 143.15 -171.57
REMARK 500 ASN A 377 -167.15 -70.01
REMARK 500 ILE A 389 -18.59 -40.05
REMARK 500 THR A 401 55.14 -99.82
REMARK 500 LYS A 423 15.83 53.51
REMARK 500 ASP A 438 77.06 -152.70
REMARK 500 TYR A 439 8.48 -41.66
REMARK 500 LYS A 441 56.47 -100.66
REMARK 500 CYS A 447 -73.29 -32.65
REMARK 500 ASN A 450 82.32 -174.65
REMARK 500 GLN A 455 -9.18 -149.38
REMARK 500 SER A 462 -176.36 -69.38
REMARK 500 LEU A 491 -71.18 -25.25
REMARK 500 ALA A 499 -71.65 -48.98
REMARK 500 ASP A 501 -65.84 -29.88
REMARK 500 HIS A 533 19.00 48.03
REMARK 500 ALA A 548 29.03 42.67
REMARK 500 GLN A 553 107.99 -161.57
REMARK 500 ALA A 576 -153.33 -105.68
REMARK 500 SER A 577 148.11 167.11
REMARK 500 ARG A 581 125.07 -35.83
REMARK 500 GLN A 586 18.68 -142.32
REMARK 500 ARG A 596 -10.17 70.21
REMARK 500 THR A 600 -110.05 -124.38
REMARK 500 ALA A 610 -73.14 -55.83
REMARK 500 SER A 614 -26.03 -36.63
REMARK 500 ASN A 621 1.60 -53.06
REMARK 500 SER A 630 -118.07 54.03
REMARK 500 ASP A 678 -81.84 -125.70
REMARK 500 ASN A 679 50.25 -148.51
REMARK 500 SER A 690 2.11 -62.56
REMARK 500 MET A 733 129.66 -170.65
REMARK 500 ASP A 737 12.77 57.29
REMARK 500 ASP A 739 -157.14 -104.01
REMARK 500 TYR B 58 85.89 -152.68
REMARK 500 SER B 64 -157.75 -172.74
REMARK 500 HIS B 66 -0.55 -142.54
REMARK 500 GLN B 72 79.60 -158.22
REMARK 500 GLU B 73 57.38 83.24
REMARK 500 ASN B 85 170.89 -56.31
REMARK 500 SER B 86 145.76 -170.03
REMARK 500 SER B 93 32.66 -76.12
REMARK 500 PHE B 95 40.87 -91.25
REMARK 500 PRO B 109 -36.01 -32.04
REMARK 500 GLN B 123 -110.06 -144.24
REMARK 500 ARG B 125 -51.92 -28.53
REMARK 500 TYR B 128 159.05 177.17
REMARK 500 ASP B 136 70.07 -65.49
REMARK 500 LEU B 137 -41.39 -22.54
REMARK 500 ARG B 140 47.05 34.72
REMARK 500 ILE B 143 114.55 -34.15
REMARK 500 GLU B 146 79.54 17.70
REMARK 500 ASN B 151 19.01 81.66
REMARK 500 THR B 156 123.46 -179.51
REMARK 500 HIS B 162 35.47 -150.67
REMARK 500 ASN B 169 41.97 76.07
REMARK 500 ILE B 193 -67.14 -127.25
REMARK 500 ASP B 200 -154.35 -84.35
REMARK 500 VAL B 207 -74.34 -129.76
REMARK 500 PRO B 218 -35.69 -35.57
REMARK 500 TYR B 225 140.15 -174.49
REMARK 500 ASP B 230 31.41 -90.08
REMARK 500 SER B 242 -141.62 71.06
REMARK 500 ALA B 259 123.38 -38.86
REMARK 500 ALA B 261 -176.88 -58.04
REMARK 500 THR B 280 -121.75 -78.47
REMARK 500 GLU B 309 26.45 -143.84
REMARK 500 GLN B 320 39.76 -50.34
REMARK 500 ASP B 367 13.76 -69.66
REMARK 500 ASN B 377 -168.78 -61.73
REMARK 500 THR B 401 62.38 -111.89
REMARK 500 TYR B 422 119.56 -35.41
REMARK 500 SER B 446 -35.78 -131.06
REMARK 500 ALA B 465 27.68 83.63
REMARK 500 ASN B 497 23.12 45.41
REMARK 500 ASN B 506 50.69 -99.62
REMARK 500 VAL B 507 139.17 -172.64
REMARK 500 ASP B 515 -158.22 -111.17
REMARK 500 ASN B 520 43.31 24.58
REMARK 500 GLU B 521 -14.73 78.55
REMARK 500 LYS B 536 -0.17 -48.22
REMARK 500 TYR B 547 -53.33 -133.46
REMARK 500 ALA B 548 -3.68 56.94
REMARK 500 SER B 583 170.47 -57.89
REMARK 500 GLN B 586 12.06 -142.23
REMARK 500 HIS B 592 6.90 -69.16
REMARK 500 ARG B 596 -4.57 70.00
REMARK 500 THR B 600 -102.19 -130.19
REMARK 500 MET B 616 -31.27 -35.46
REMARK 500 ASP B 620 88.38 -68.31
REMARK 500 ASN B 621 -36.53 -35.94
REMARK 500 SER B 630 -129.86 70.51
REMARK 500 LYS B 648 -61.20 -91.40
REMARK 500 PRO B 674 33.85 -61.10
REMARK 500 ASP B 678 -110.10 -103.55
REMARK 500 SER B 686 40.62 -147.23
REMARK 500 ASN B 710 -77.61 -76.95
REMARK 500 HIS B 712 157.67 -34.53
REMARK 500 GLN B 714 -33.10 -36.93
REMARK 500 MET B 733 110.55 -171.41
REMARK 500 THR B 736 116.09 -38.76
REMARK 500 ASP B 739 -153.85 -91.30
REMARK 500 ILE B 742 60.43 25.53
REMARK 500 SER B 764 45.50 25.04
REMARK 500 ASN C 51 49.83 28.98
REMARK 500 TYR C 58 49.62 -143.29
REMARK 500 ASN C 74 13.08 39.31
REMARK 500 ASN C 92 -39.76 -35.21
REMARK 500 PHE C 95 38.84 -93.65
REMARK 500 TYR C 105 -156.99 -129.21
REMARK 500 SER C 106 91.87 167.68
REMARK 500 PRO C 109 -37.08 -38.91
REMARK 500 GLN C 123 -100.86 -129.36
REMARK 500 TRP C 124 -146.43 -88.81
REMARK 500 TYR C 128 168.21 172.90
REMARK 500 ARG C 140 56.28 28.83
REMARK 500 ILE C 143 102.38 -33.15
REMARK 500 GLU C 146 70.87 52.02
REMARK 500 PRO C 149 -175.66 -63.39
REMARK 500 TRP C 154 135.45 -170.53
REMARK 500 HIS C 162 35.80 -151.66
REMARK 500 PRO C 178 -10.90 -48.28
REMARK 500 ILE C 193 -55.55 -125.89
REMARK 500 ASP C 200 -156.21 -79.61
REMARK 500 ALA C 210 151.04 178.86
REMARK 500 PRO C 218 -33.70 -32.14
REMARK 500 SER C 242 -138.69 55.95
REMARK 500 ALA C 259 105.94 -32.92
REMARK 500 ALA C 261 175.83 -58.94
REMARK 500 SER C 275 64.31 -114.41
REMARK 500 GLN C 320 49.45 -67.14
REMARK 500 LEU C 366 -58.55 -22.02
REMARK 500 ASN C 377 -159.50 -72.27
REMARK 500 THR C 401 59.65 -96.06
REMARK 500 LYS C 423 14.90 48.54
REMARK 500 TYR C 439 3.90 -61.26
REMARK 500 ASN C 450 66.89 -179.57
REMARK 500 GLN C 455 -12.41 -143.71
REMARK 500 ARG C 492 -173.15 178.33
REMARK 500 LYS C 536 13.84 -64.46
REMARK 500 PRO C 541 -178.46 -57.50
REMARK 500 ALA C 548 17.78 36.83
REMARK 500 GLN C 553 101.12 -172.30
REMARK 500 SER C 583 175.94 -51.21
REMARK 500 GLN C 586 21.49 -147.05
REMARK 500 ARG C 596 6.51 59.56
REMARK 500 THR C 600 -85.80 -128.67
REMARK 500 PHE C 618 30.98 -99.93
REMARK 500 LYS C 622 21.94 -77.64
REMARK 500 ARG C 623 65.65 -161.93
REMARK 500 SER C 630 -117.12 54.57
REMARK 500 ALA C 654 54.88 29.16
REMARK 500 SER C 664 -74.03 -53.36
REMARK 500 THR C 667 -73.31 -45.87
REMARK 500 GLU C 668 -17.22 -44.94
REMARK 500 PRO C 674 32.71 -66.44
REMARK 500 ASP C 678 -98.27 -146.55
REMARK 500 PHE C 695 -16.59 -46.06
REMARK 500 ASN C 710 -75.00 -89.55
REMARK 500 VAL C 711 68.03 -100.98
REMARK 500 HIS C 712 138.14 -22.74
REMARK 500 GLN C 715 -75.06 -55.89
REMARK 500 MET C 733 96.47 -172.81
REMARK 500 ASP C 737 1.55 54.98
REMARK 500 ASP C 739 -157.95 -119.93
REMARK 500 ARG D 54 172.87 -55.73
REMARK 500 GLN D 72 133.92 178.59
REMARK 500 GLU D 73 33.34 38.15
REMARK 500 GLU D 82 -73.23 -62.18
REMARK 500 SER D 87 94.47 -160.81
REMARK 500 VAL D 88 101.97 -18.14
REMARK 500 LEU D 90 106.74 -165.90
REMARK 500 PHE D 95 40.99 -101.42
REMARK 500 GLU D 97 37.49 -71.84
REMARK 500 HIS D 100 136.97 -179.17
REMARK 500 PRO D 109 -34.72 -37.10
REMARK 500 LYS D 122 130.38 -36.41
REMARK 500 GLN D 123 -82.79 -103.01
REMARK 500 TRP D 124 -119.09 -99.07
REMARK 500 ALA D 130 147.14 172.15
REMARK 500 ASN D 138 -82.28 -40.73
REMARK 500 ILE D 143 102.37 -54.10
REMARK 500 PRO D 149 150.93 -30.98
REMARK 500 HIS D 162 14.43 -151.75
REMARK 500 PRO D 178 5.37 -52.43
REMARK 500 PRO D 181 -178.36 -57.30
REMARK 500 THR D 188 1.50 -59.26
REMARK 500 GLU D 191 106.26 -55.74
REMARK 500 ILE D 193 -65.77 -126.36
REMARK 500 ASP D 200 -155.95 -88.51
REMARK 500 VAL D 207 -77.08 -80.08
REMARK 500 SER D 242 179.70 80.36
REMARK 500 SER D 245 -3.29 -58.82
REMARK 500 ALA D 259 111.97 -27.16
REMARK 500 THR D 280 -97.48 -82.32
REMARK 500 GLN D 320 57.62 -39.44
REMARK 500 PHE D 357 -25.75 -143.90
REMARK 500 PRO D 359 136.64 -39.76
REMARK 500 LEU D 366 -63.33 -18.63
REMARK 500 ILE D 389 -18.98 -47.11
REMARK 500 LYS D 423 13.49 47.06
REMARK 500 ASP D 438 103.95 -175.91
REMARK 500 TYR D 439 3.24 -69.55
REMARK 500 ASN D 450 87.19 -161.89
REMARK 500 GLU D 495 116.17 -178.97
REMARK 500 GLU D 521 -0.00 53.61
REMARK 500 HIS D 533 43.31 38.24
REMARK 500 ALA D 548 -9.36 71.02
REMARK 500 ASN D 572 69.38 31.64
REMARK 500 GLN D 586 33.92 -151.71
REMARK 500 THR D 600 -78.80 -130.04
REMARK 500 SER D 630 -105.32 66.09
REMARK 500 THR D 667 -70.67 -51.41
REMARK 500 ASP D 678 -111.98 -129.67
REMARK 500 TYR D 683 -75.97 -52.92
REMARK 500 SER D 690 3.52 -67.08
REMARK 500 ASN D 710 -85.22 -67.84
REMARK 500 HIS D 712 150.65 -36.26
REMARK 500 GLN D 714 -35.52 -34.70
REMARK 500 MET D 733 113.72 -179.43
REMARK 500 THR D 736 118.37 -37.06
REMARK 500 ASP D 739 -153.47 -90.46
REMARK 500 ILE D 742 64.73 33.61
REMARK 500 SER D 764 77.93 20.83
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 A 183 0.07 SIDE_CHAIN
REMARK 500 TYR A 700 0.07 SIDE_CHAIN
REMARK 500 TYR B 128 0.07 SIDE_CHAIN
REMARK 500 TYR C 83 0.07 SIDE_CHAIN
REMARK 500 TYR D 752 0.07 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 776 DISTANCE = 5.08 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: 13Z BINDING SITE FOR RESIDUE A 767
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: 13Z BINDING SITE FOR RESIDUE B 767
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: 13Z BINDING SITE FOR RESIDUE C 767
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: 13Z BINDING SITE FOR RESIDUE D 767
DBREF 2QKY A 40 766 UNP P27487 DPP4_HUMAN 40 766
DBREF 2QKY B 40 766 UNP P27487 DPP4_HUMAN 40 766
DBREF 2QKY C 40 766 UNP P27487 DPP4_HUMAN 40 766
DBREF 2QKY D 40 766 UNP P27487 DPP4_HUMAN 40 766
SEQADV 2QKY THR A 39 UNP P27487 EXPRESSION TAG
SEQADV 2QKY THR B 39 UNP P27487 EXPRESSION TAG
SEQADV 2QKY THR C 39 UNP P27487 EXPRESSION TAG
SEQADV 2QKY THR D 39 UNP P27487 EXPRESSION TAG
SEQRES 1 A 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 B 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 C 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 C 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 C 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 C 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 C 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
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 VAL
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 ILE GLU PRO ASN LEU PRO
SEQRES 12 C 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 C 728 TYR ASN GLY ILE 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 VAL PRO TYR PRO LYS ALA
SEQRES 18 C 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 C 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 C 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 C 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 C 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 C 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 C 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 C 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 C 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 C 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 C 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR 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 TYR LYS GLY MET PRO GLY GLY
SEQRES 31 C 728 ARG ASN LEU TYR LYS ILE GLN LEU SER 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 VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 C 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 C 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 C 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 C 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 C 728 ASN GLU 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 LEU ASP
SEQRES 40 C 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 C 728 PHE ARG LEU ASN 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 ALA
SEQRES 45 C 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN 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 SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 C 728 GLY ILE ALA VAL ALA PRO VAL SER ARG 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 HIS 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 ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 C 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 C 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 C 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 728 THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 D 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 D 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 D 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 D 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 D 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
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 VAL
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 ILE GLU PRO ASN LEU PRO
SEQRES 12 D 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 D 728 TYR ASN GLY ILE 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 VAL PRO TYR PRO LYS ALA
SEQRES 18 D 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 D 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 D 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 D 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 D 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 D 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 D 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 D 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 D 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 D 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 D 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR 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 TYR LYS GLY MET PRO GLY GLY
SEQRES 31 D 728 ARG ASN LEU TYR LYS ILE GLN LEU SER 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 VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 D 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 D 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 D 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 D 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 D 728 ASN GLU 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 LEU ASP
SEQRES 40 D 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 D 728 PHE ARG LEU ASN 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 ALA
SEQRES 45 D 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN 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 SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 D 728 GLY ILE ALA VAL ALA PRO VAL SER ARG 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 HIS 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 ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 D 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 D 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 D 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET 13Z A 767 26
HET 13Z B 767 26
HET 13Z C 767 26
HET 13Z D 767 26
HETNAM 13Z 2-[(2-{(2S,4S)-2-[(R)-(5-TERT-BUTYL-1,3,4-OXADIAZOL-2-
HETNAM 2 13Z YL)(HYDROXY)METHYL]-4-FLUOROPYRROLIDIN-1-YL}-2-
HETNAM 3 13Z OXOETHYL)AMINO]-2-METHYLPROPAN-1-OL
FORMUL 5 13Z 4(C17 H29 F N4 O4)
FORMUL 9 HOH *311(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 LEU A 340 GLN A 344 5 5
HELIX 4 4 GLU A 421 MET A 425 5 5
HELIX 5 5 SER A 446 ASN A 450 5 5
HELIX 6 6 ASN A 497 GLN A 505 1 9
HELIX 7 7 ASN A 562 ASN A 572 1 11
HELIX 8 8 GLY A 587 HIS A 592 1 6
HELIX 9 9 ALA A 593 ASN A 595 5 3
HELIX 10 10 THR A 600 MET A 616 1 17
HELIX 11 11 SER A 630 GLY A 641 1 12
HELIX 12 12 ARG A 658 TYR A 662 5 5
HELIX 13 13 ASP A 663 GLY A 672 1 10
HELIX 14 14 ASN A 679 SER A 686 1 8
HELIX 15 15 VAL A 688 VAL A 698 5 11
HELIX 16 16 PHE A 713 VAL A 726 1 14
HELIX 17 17 SER A 744 SER A 764 1 21
HELIX 18 18 THR B 44 LYS B 50 1 7
HELIX 19 19 GLU B 91 PHE B 95 5 5
HELIX 20 20 ASP B 200 GLU B 206 1 7
HELIX 21 21 PRO B 290 ILE B 295 1 6
HELIX 22 22 LEU B 340 ALA B 342 5 3
HELIX 23 23 GLU B 421 MET B 425 5 5
HELIX 24 24 ASN B 497 LEU B 504 1 8
HELIX 25 25 GLN B 505 VAL B 507 5 3
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 MET B 616 1 17
HELIX 30 30 SER B 630 SER B 642 1 13
HELIX 31 31 ARG B 658 TYR B 662 5 5
HELIX 32 32 ASP B 663 GLY B 672 1 10
HELIX 33 33 ASN B 679 ASN B 685 1 7
HELIX 34 34 SER B 686 THR B 687 5 2
HELIX 35 35 VAL B 688 VAL B 698 5 11
HELIX 36 36 PHE B 713 ASP B 725 1 13
HELIX 37 37 SER B 744 PHE B 763 1 20
HELIX 38 38 THR C 44 LYS C 50 1 7
HELIX 39 39 ASP C 200 VAL C 207 1 8
HELIX 40 40 PRO C 290 ILE C 295 1 6
HELIX 41 41 VAL C 341 GLN C 344 5 4
HELIX 42 42 GLU C 421 MET C 425 5 5
HELIX 43 43 ASN C 497 GLN C 505 1 9
HELIX 44 44 ASN C 562 ASN C 572 1 11
HELIX 45 45 GLY C 587 HIS C 592 1 6
HELIX 46 46 ALA C 593 ASN C 595 5 3
HELIX 47 47 THR C 600 LYS C 615 1 16
HELIX 48 48 SER C 630 GLY C 641 1 12
HELIX 49 49 ASP C 663 GLY C 672 1 10
HELIX 50 50 ASN C 679 ARG C 684 1 6
HELIX 51 51 VAL C 688 VAL C 698 5 11
HELIX 52 52 PHE C 713 VAL C 726 1 14
HELIX 53 53 SER C 744 PHE C 763 1 20
HELIX 54 54 THR D 44 LYS D 50 1 7
HELIX 55 55 PHE D 95 GLY D 99 5 5
HELIX 56 56 ASP D 200 GLU D 206 1 7
HELIX 57 57 ASP D 274 LEU D 276 5 3
HELIX 58 58 PRO D 290 ILE D 295 1 6
HELIX 59 59 VAL D 341 GLN D 344 5 4
HELIX 60 60 GLU D 421 MET D 425 5 5
HELIX 61 61 ASN D 497 GLN D 505 1 9
HELIX 62 62 ASN D 562 ASN D 572 1 11
HELIX 63 63 GLN D 586 HIS D 592 1 7
HELIX 64 64 ALA D 593 ASN D 595 5 3
HELIX 65 65 THR D 600 MET D 616 1 17
HELIX 66 66 TYR D 631 GLY D 641 1 11
HELIX 67 67 ARG D 658 TYR D 662 5 5
HELIX 68 68 ASP D 663 GLY D 672 1 10
HELIX 69 69 ASN D 679 ASN D 685 1 7
HELIX 70 70 VAL D 688 VAL D 698 5 11
HELIX 71 71 PHE D 713 VAL D 726 1 14
HELIX 72 72 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 ARG 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 86 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 B 4 ASP A 104 ILE 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 ALA A 165 N THR A 156
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 C 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 D 3 ILE A 194 ASN A 196 0
SHEET 2 D 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 D 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 E 4 ILE A 194 ASN A 196 0
SHEET 2 E 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 E 4 ILE A 285 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
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 ASN A 338 -1 O ASN 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 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 I 4 PRO A 362 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 ARG 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 TYR 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 GLU A 408
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O ASN A 430 N SER A 419
SHEET 4 J 4 THR A 443 CYS A 444 -1 O THR A 443 N LYS 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 ARG A 471 N SER A 458
SHEET 3 K 4 LEU A 479 SER A 484 -1 O HIS A 483 N TYR A 468
SHEET 4 K 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 L 2 SER A 511 LEU A 519 0
SHEET 2 L 2 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 1 M 6 ILE A 574 ALA A 576 0
SHEET 2 M 6 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 3 M 6 VAL A 619 TRP A 629 1 O ARG A 623 N LEU A 542
SHEET 4 M 6 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 5 M 6 GLU A 699 HIS A 704 1 O LEU A 701 N ALA A 652
SHEET 6 M 6 GLN A 731 TRP A 734 1 O GLN A 731 N TYR A 700
SHEET 1 N 4 ARG B 61 TRP B 62 0
SHEET 2 N 4 GLU B 67 TYR B 70 -1 O LEU B 69 N ARG B 61
SHEET 3 N 4 LEU B 77 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 N 4 SER B 86 VAL B 88 -1 O SER B 87 N VAL B 78
SHEET 1 O 3 ILE B 102 ILE B 107 0
SHEET 2 O 3 ILE B 114 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 O 3 TYR B 128 ILE B 134 -1 O ASP B 133 N LEU B 116
SHEET 1 P 3 LEU B 164 VAL B 167 0
SHEET 2 P 3 ILE B 172 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 3 P 3 TYR B 183 ARG B 184 -1 O TYR 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 ASN B 272 -1 O VAL B 271 N LEU B 223
SHEET 4 R 4 ILE B 285 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 TRP B 305 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 CYS B 328 N ILE B 311
SHEET 4 T 4 TRP B 337 ASN B 338 -1 O ASN B 338 N ASP B 329
SHEET 1 U 4 HIS B 298 TRP B 305 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
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 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 V 4 PRO B 362 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 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 V 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR 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 TYR B 416 N GLU B 408
SHEET 3 W 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 W 4 VAL B 442 THR B 443 -1 O THR B 443 N LYS B 433
SHEET 1 X 4 VAL B 459 PHE B 461 0
SHEET 2 X 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 X 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 X 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Y 3 SER B 511 LYS B 513 0
SHEET 2 Y 3 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Y 3 PHE B 516 LEU B 519 -1 N LEU B 519 O THR B 522
SHEET 1 Z 8 SER B 511 LYS B 513 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Z 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Z 8 TYR B 540 ASP B 545 1 N ASP B 545 O ALA B 576
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O ASP B 620 N TYR B 540
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O ILE B 651 N GLY B 628
SHEET 7 Z 8 LEU B 701 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
SHEET 1 AA 4 ARG C 61 TRP C 62 0
SHEET 2 AA 4 GLU C 67 GLN C 72 -1 O LEU C 69 N ARG C 61
SHEET 3 AA 4 ASN C 75 ASN C 80 -1 O ASN C 75 N GLN C 72
SHEET 4 AA 4 SER C 86 LEU C 90 -1 O PHE C 89 N ILE C 76
SHEET 1 AB 3 PHE C 113 LYS C 122 0
SHEET 2 AB 3 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 3 AB 3 GLN C 141 ILE C 143 -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 VAL C 167 -1 O ALA C 165 N THR C 156
SHEET 3 AC 4 ILE C 172 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AC 4 TYR C 183 ARG C 184 -1 O TYR 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 ASN C 272 -1 O VAL C 271 N LEU C 223
SHEET 4 AE 4 ILE C 285 GLN C 286 -1 O ILE C 285 N VAL C 270
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 ARG C 310 N ALA C 306
SHEET 3 AG 4 TYR C 322 TYR C 330 -1 O VAL C 324 N TRP C 315
SHEET 4 AG 4 TRP C 337 CYS C 339 -1 O ASN 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 ARG C 310 N ALA C 306
SHEET 3 AH 4 TYR C 322 TYR C 330 -1 O VAL C 324 N TRP C 315
SHEET 4 AH 4 HIS C 345 MET 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 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AI 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR 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 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AK 2 CYS C 454 TYR C 456 0
SHEET 2 AK 2 GLY C 474 PRO C 475 -1 O GLY C 474 N GLN C 455
SHEET 1 AL 4 VAL C 459 PHE C 461 0
SHEET 2 AL 4 TYR C 467 CYS C 472 -1 O GLN C 469 N SER C 460
SHEET 3 AL 4 LEU C 479 SER C 484 -1 O THR C 481 N LEU C 470
SHEET 4 AL 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AM 8 LEU C 514 LEU C 519 0
SHEET 2 AM 8 THR C 522 ILE C 529 -1 O THR C 522 N LEU C 519
SHEET 3 AM 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AM 8 TYR C 540 ASP C 545 1 N LEU C 543 O ILE C 574
SHEET 5 AM 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 542
SHEET 6 AM 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AM 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 652
SHEET 8 AM 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AN 2 LYS D 41 THR D 42 0
SHEET 2 AN 2 VAL D 507 GLN D 508 1 O GLN D 508 N LYS D 41
SHEET 1 AO 4 ARG D 61 TRP D 62 0
SHEET 2 AO 4 GLU D 67 TYR D 70 -1 O LEU D 69 N ARG D 61
SHEET 3 AO 4 ILE D 76 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 4 AO 4 SER D 86 LEU D 90 -1 O PHE D 89 N ILE D 76
SHEET 1 AP 4 ASP D 104 ILE D 107 0
SHEET 2 AP 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AP 4 TYR D 128 ASP D 136 -1 O ASP D 133 N LEU D 116
SHEET 4 AP 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AQ 4 THR D 152 TRP D 157 0
SHEET 2 AQ 4 LEU D 164 TRP D 168 -1 O VAL D 167 N TRP D 154
SHEET 3 AQ 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AQ 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AR 3 ILE D 194 ASN D 196 0
SHEET 2 AR 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AR 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AS 4 ILE D 194 ASN D 196 0
SHEET 2 AS 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AS 4 THR D 265 ASN D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AS 4 SER D 284 ILE D 287 -1 O ILE D 285 N VAL D 270
SHEET 1 AT 2 LEU D 235 PHE D 240 0
SHEET 2 AT 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AU 4 HIS D 298 TRP D 305 0
SHEET 2 AU 4 ARG D 310 ARG D 317 -1 O LEU D 316 N TYR D 299
SHEET 3 AU 4 TYR D 322 ASP D 331 -1 O VAL D 324 N TRP D 315
SHEET 4 AU 4 ARG D 336 CYS D 339 -1 O ASN D 338 N ASP D 329
SHEET 1 AV 4 HIS D 298 TRP D 305 0
SHEET 2 AV 4 ARG D 310 ARG D 317 -1 O LEU D 316 N TYR D 299
SHEET 3 AV 4 TYR D 322 ASP D 331 -1 O VAL D 324 N TRP D 315
SHEET 4 AV 4 HIS D 345 MET D 348 -1 O HIS D 345 N MET D 325
SHEET 1 AW 4 HIS D 363 PHE D 364 0
SHEET 2 AW 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AW 4 ARG D 382 GLN D 388 -1 O CYS D 385 N LYS D 373
SHEET 4 AW 4 LYS D 391 PHE D 396 -1 O LYS D 391 N GLN D 388
SHEET 1 AX 4 VAL D 404 LEU D 410 0
SHEET 2 AX 4 TYR D 414 SER D 419 -1 O ILE D 418 N ILE D 405
SHEET 3 AX 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AX 4 ASP D 438 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AY 4 VAL D 459 PHE D 461 0
SHEET 2 AY 4 TYR D 467 CYS D 472 -1 O GLN D 469 N SER D 460
SHEET 3 AY 4 LEU D 479 SER D 484 -1 O LEU D 479 N CYS D 472
SHEET 4 AY 4 LYS D 489 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AZ 8 SER D 511 LEU D 519 0
SHEET 2 AZ 8 THR D 522 LEU D 530 -1 O PHE D 524 N ILE D 517
SHEET 3 AZ 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AZ 8 TYR D 540 ASP D 545 1 N PRO D 541 O ILE D 574
SHEET 5 AZ 8 VAL D 619 TRP D 629 1 O ASP D 620 N TYR D 540
SHEET 6 AZ 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AZ 8 GLU D 699 GLY D 705 1 O LEU D 701 N ALA D 652
SHEET 8 AZ 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.03
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.04
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.03
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.04
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.03
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.02
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.04
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.05
SSBOND 13 CYS C 444 CYS C 447 1555 1555 2.03
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.04
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.03
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.05
SSBOND 17 CYS D 385 CYS D 394 1555 1555 2.04
SSBOND 18 CYS D 444 CYS D 447 1555 1555 2.03
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.02
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.04
LINK OG SER A 630 C7 13Z A 767 1555 1555 1.38
LINK OG SER B 630 C7 13Z B 767 1555 1555 1.39
LINK OG SER C 630 C7 13Z C 767 1555 1555 1.40
LINK OG SER D 630 C7 13Z D 767 1555 1555 1.37
CISPEP 1 GLY A 474 PRO A 475 0 -0.09
CISPEP 2 GLY B 474 PRO B 475 0 -0.13
CISPEP 3 LEU B 765 PRO B 766 0 0.34
CISPEP 4 GLY C 474 PRO C 475 0 -0.31
CISPEP 5 GLY D 474 PRO D 475 0 0.15
CISPEP 6 LEU D 765 PRO D 766 0 0.38
SITE 1 AC1 10 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC1 10 SER A 630 TYR A 631 TYR A 662 TYR A 666
SITE 3 AC1 10 ASN A 710 HIS A 740
SITE 1 AC2 11 ARG B 125 GLU B 205 GLU B 206 PHE B 357
SITE 2 AC2 11 TYR B 547 SER B 630 TYR B 631 TYR B 662
SITE 3 AC2 11 TYR B 666 ASN B 710 HIS B 740
SITE 1 AC3 9 ARG C 125 GLU C 205 GLU C 206 TYR C 547
SITE 2 AC3 9 SER C 630 TYR C 631 TYR C 662 TYR C 666
SITE 3 AC3 9 HIS C 740
SITE 1 AC4 10 ARG D 125 GLU D 205 GLU D 206 TYR D 547
SITE 2 AC4 10 SER D 630 TYR D 631 TYR D 662 TYR D 666
SITE 3 AC4 10 ASN D 710 HIS D 740
CRYST1 73.178 106.115 132.051 76.30 78.62 80.11 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 0.013665 -0.002383 -0.002301 0.00000
SCALE2 0.000000 0.009566 -0.002056 0.00000
SCALE3 0.000000 0.000000 0.007901 0.00000
TER 5966 PRO A 766
TER 11932 PRO B 766
TER 17898 PRO C 766
TER 23864 PRO D 766
MASTER 582 0 4 72 200 0 12 624275 4 148 224
END |