content |
HEADER HYDROLASE 30-AUG-06 2I78
TITLE CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP IV)
TITLE 2 COMPLEXED WITH ABT-341, A CYCLOHEXENE-CONSTRAINED
TITLE 3 PHENETHYLAMINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE 4, DPP IV, T-CELL ACTIVATION
COMPND 5 ANTIGEN CD26, TP103, ADENOSINE DEAMINASE COMPLEXING
COMPND 6 PROTEIN 2, ADABP;
COMPND 7 EC: 3.4.14.5;
COMPND 8 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_COMMON: FALL ARMYWORM
KEYWDS SERINE PEPTIDASE,, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.LONGENECKER,Z.PEI,X.LI
REVDAT 1 09-OCT-07 2I78 0
JRNL AUTH Z.PEI,X.LI,T.W.VONGELDERN,D.J.MADAR,
JRNL AUTH 2 K.L LONGENECKER,H.YONG,T.H.LUBBEN,K.D.STEWART,
JRNL AUTH 3 B.A.ZINKER,B.J.BACKES,A.S.JUDD,M.MULHERN,
JRNL AUTH 4 S.J.BALLARON,M.A.STASHKO,A.K.MIKA,D.W.A.BENO,
JRNL AUTH 5 G.A.REINHART,R.M.FRYER,L.C.PREUSSER,
JRNL AUTH 6 A.J.KEMPF-GROTE,H.L.SHAM,J.M.TREVILLYAN
JRNL TITL DISCOVERY OF CYCLOHEXENE-CONSTRAINED
JRNL TITL 2 PHENETHYLAMINE ABT-341, A HIGHLY POTENT,
JRNL TITL 3 SELECTIVE, ORALLY BIOAVAILABLE, SAFE AND POTENTIAL
JRNL TITL 4 NEXT-GENERATION DIPEPTIDYL PEPTIDASE IV INHIBITOR
JRNL TITL 5 FOR THE TREATMENT OF TYPE 2 DIABETES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 129.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 126792
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6375
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7246
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 345
REMARK 3 BIN FREE R VALUE : 0.3890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 24449
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.27000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : 1.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.26000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.575
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.317
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.232
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.455
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.876
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24534 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 33384 ; 1.341 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2900 ; 6.844 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1232 ;34.886 ;23.961
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3980 ;18.838 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;18.036 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3507 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19010 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 11247 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 16549 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1213 ; 0.172 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 70 ; 0.225 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.306 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 14809 ; 0.541 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23471 ; 0.960 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11465 ; 1.118 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 9913 ; 1.782 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 39 A 764 4
REMARK 3 1 B 39 B 764 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 5949 ; 0.310 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 5949 ; 0.750 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 39 C 764 4
REMARK 3 1 D 39 D 764 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 C (A): 5949 ; 0.280 ; 0.500
REMARK 3 MEDIUM THERMAL 2 C (A**2): 5949 ; 0.540 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2I78 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB039224.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126817
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.38900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,1/2+Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 63.20950
REMARK 290 SMTRY3 2 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 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 300
REMARK 300 REMARK: A DIMER OF DPP4 MOLECULES IS THOUGHT TO BE
REMARK 300 BIOLOGICALLY RELEVANT, AND THE ASYMMETRIC UNIT IS COMPRISED
REMARK 300 OF TWO DIMERS.
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: DIMER
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: DIMER
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 O HOH A 765 O HOH A 952 2.08
REMARK 500 NZ LYS D 539 O GLY D 617 2.13
REMARK 500 ND2 ASN B 219 O HOH B 1092 2.16
REMARK 500 O HOH C 863 O HOH C 864 2.17
REMARK 500 NE ARG A 691 O HOH A 949 2.18
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 LEU A 90 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 LEU A 415 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 LEU B 276 CA - CB - CG ANGL. DEV. = 14.9 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 ARG A 40 156.13 46.62
REMARK 500 LYS A 71 89.28 -68.75
REMARK 500 ASN A 74 -89.71 -76.08
REMARK 500 GLN A 123 -109.13 -106.24
REMARK 500 TRP A 124 -145.63 -86.39
REMARK 500 HIS A 162 26.10 -151.76
REMARK 500 PRO A 181 147.79 -39.82
REMARK 500 ASP A 192 -0.25 71.16
REMARK 500 ILE A 193 -66.38 -122.00
REMARK 500 SER A 242 -163.69 67.06
REMARK 500 GLU A 244 -45.62 -27.69
REMARK 500 SER A 278 -15.27 56.49
REMARK 500 ALA A 289 -147.86 70.85
REMARK 500 ILE A 295 3.37 -66.89
REMARK 500 GLN A 320 31.80 -78.65
REMARK 500 ALA A 342 -34.98 129.79
REMARK 500 ASN A 377 -179.50 -53.52
REMARK 500 LYS A 423 17.34 57.54
REMARK 500 ASN A 450 76.75 -172.01
REMARK 500 GLN A 508 90.03 -60.72
REMARK 500 ASN A 520 85.15 1.80
REMARK 500 GLU A 521 -55.40 97.00
REMARK 500 TYR A 547 -73.92 -118.86
REMARK 500 ASN A 562 -159.96 -139.29
REMARK 500 ARG A 597 44.20 -141.80
REMARK 500 THR A 600 -95.17 -127.58
REMARK 500 SER A 630 -125.40 75.00
REMARK 500 ASP A 678 -95.45 -120.04
REMARK 500 ASN A 710 -70.70 -91.40
REMARK 500 ASP A 739 -160.50 -107.30
REMARK 500 ILE A 742 54.95 29.77
REMARK 500 ARG B 40 -149.38 41.79
REMARK 500 GLN B 72 -144.00 -148.05
REMARK 500 ASN B 74 -80.14 -122.52
REMARK 500 GLN B 123 -103.90 -112.11
REMARK 500 TRP B 124 -151.06 -89.29
REMARK 500 ARG B 140 28.97 44.00
REMARK 500 HIS B 162 24.81 -149.81
REMARK 500 GLU B 191 123.74 -38.40
REMARK 500 ILE B 193 -63.54 -120.74
REMARK 500 SER B 242 -166.54 65.42
REMARK 500 GLU B 244 -37.99 -36.15
REMARK 500 SER B 277 -118.32 -65.44
REMARK 500 SER B 278 32.08 166.13
REMARK 500 ASN B 281 107.97 -48.13
REMARK 500 ALA B 289 -148.52 74.72
REMARK 500 GLN B 320 49.41 -78.33
REMARK 500 SER B 334 -17.14 -175.55
REMARK 500 ALA B 342 -43.44 117.42
REMARK 500 ASP B 438 103.28 -161.09
REMARK 500 ASN B 450 74.66 -169.59
REMARK 500 ASN B 520 71.21 7.28
REMARK 500 GLU B 521 -57.33 92.64
REMARK 500 TYR B 547 -70.19 -133.78
REMARK 500 ARG B 597 49.03 -141.48
REMARK 500 THR B 600 -94.04 -106.09
REMARK 500 SER B 630 -128.29 65.38
REMARK 500 ALA B 654 58.92 39.96
REMARK 500 PRO B 674 43.45 -83.02
REMARK 500 ASP B 678 -101.20 -90.04
REMARK 500 ASP B 708 97.94 -66.92
REMARK 500 ASN B 710 -72.14 -101.10
REMARK 500 ASP B 739 -160.54 -101.30
REMARK 500 ARG C 40 -142.26 -69.75
REMARK 500 ASN C 51 38.50 72.57
REMARK 500 LYS C 71 107.08 -45.20
REMARK 500 ASN C 74 -61.16 -104.44
REMARK 500 GLN C 123 -106.01 -116.79
REMARK 500 TRP C 124 -143.78 -87.63
REMARK 500 LYS C 139 13.93 -144.43
REMARK 500 PRO C 178 -3.99 -43.95
REMARK 500 GLU C 191 124.01 -25.59
REMARK 500 ASP C 192 12.44 59.71
REMARK 500 ILE C 193 -59.95 -129.44
REMARK 500 ALA C 213 38.04 -145.26
REMARK 500 SER C 242 -166.22 62.62
REMARK 500 SER C 277 -17.36 -152.12
REMARK 500 SER C 278 -35.73 78.04
REMARK 500 ALA C 282 133.40 -37.81
REMARK 500 THR C 288 -122.96 -85.35
REMARK 500 ALA C 289 167.81 64.08
REMARK 500 GLN C 308 -19.51 -46.48
REMARK 500 GLN C 320 30.59 -79.62
REMARK 500 SER C 334 -62.90 -175.90
REMARK 500 ALA C 342 -6.99 73.73
REMARK 500 LYS C 423 9.14 58.96
REMARK 500 TYR C 439 21.65 -66.65
REMARK 500 ASN C 450 79.57 -156.21
REMARK 500 ASN C 520 83.26 6.20
REMARK 500 GLU C 521 -38.35 85.32
REMARK 500 TYR C 547 -65.43 -127.33
REMARK 500 THR C 600 -96.08 -107.12
REMARK 500 SER C 630 -127.49 64.04
REMARK 500 ASP C 678 -95.55 -114.91
REMARK 500 ASN C 679 31.42 -140.01
REMARK 500 ASN C 710 -74.92 -86.81
REMARK 500 ASP C 739 -159.67 -106.07
REMARK 500 ILE C 742 53.09 36.37
REMARK 500 ARG D 40 -76.89 -23.81
REMARK 500 ASN D 74 -80.97 -78.91
REMARK 500 PRO D 109 38.40 -69.04
REMARK 500 GLN D 123 -103.41 -106.08
REMARK 500 TRP D 124 -143.45 -91.43
REMARK 500 LYS D 139 26.64 -151.53
REMARK 500 HIS D 162 16.33 -140.94
REMARK 500 ASP D 192 -3.31 69.60
REMARK 500 ILE D 193 -56.70 -120.29
REMARK 500 SER D 242 -166.79 57.66
REMARK 500 SER D 278 -3.56 71.15
REMARK 500 THR D 288 -166.50 -108.82
REMARK 500 ALA D 289 -159.93 65.47
REMARK 500 ALA D 306 -64.60 -94.95
REMARK 500 THR D 307 -156.47 -120.82
REMARK 500 GLN D 320 39.84 -90.07
REMARK 500 SER D 334 -47.36 -174.58
REMARK 500 ASN D 450 71.91 -166.48
REMARK 500 ASN D 487 16.34 -142.95
REMARK 500 ARG D 492 159.25 179.64
REMARK 500 GLN D 508 81.60 -64.44
REMARK 500 ASN D 520 52.91 38.49
REMARK 500 TYR D 547 -71.22 -109.07
REMARK 500 SER D 583 152.56 -49.67
REMARK 500 ARG D 597 38.46 -146.99
REMARK 500 THR D 600 -91.33 -111.66
REMARK 500 SER D 630 -125.38 65.41
REMARK 500 ASP D 678 -75.24 -107.42
REMARK 500 ASN D 679 18.84 -152.34
REMARK 500 ASN D 710 -77.34 -95.31
REMARK 500 ASP D 739 -156.35 -102.19
REMARK 500 ILE D 742 57.44 31.21
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2I78 A 39 764 UNP P27487 DPP4_HUMAN 39 764
DBREF 2I78 B 39 764 UNP P27487 DPP4_HUMAN 39 764
DBREF 2I78 C 39 764 UNP P27487 DPP4_HUMAN 39 764
DBREF 2I78 D 39 764 UNP P27487 DPP4_HUMAN 39 764
SEQRES 1 A 726 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 726 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 726 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 726 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 726 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 726 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 726 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 726 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 726 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 726 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 726 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 726 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 726 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 726 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 726 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 726 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 726 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 726 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 726 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 726 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 726 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 726 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 726 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 726 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 726 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 726 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 726 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 726 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 726 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 726 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 726 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 726 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 726 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 726 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 726 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 726 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 726 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 726 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 726 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 726 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 726 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 726 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 726 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 726 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 726 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 726 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 726 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 726 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 726 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 726 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 726 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 726 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 726 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 726 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 726 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 726 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
SEQRES 1 B 726 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 726 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 726 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 726 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 726 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 726 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 726 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 726 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 726 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 726 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 726 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 726 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 726 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 726 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 726 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 726 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 726 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 726 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 726 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 726 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 726 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 726 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 726 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 726 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 726 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 726 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 726 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 726 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 726 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 726 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 726 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 B 726 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 726 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 726 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 726 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 726 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 726 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 726 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 726 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 726 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 726 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 726 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 726 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 726 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 726 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 726 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 726 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 726 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 726 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 726 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 726 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 726 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 726 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 726 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 726 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 726 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
SEQRES 1 C 726 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 C 726 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 C 726 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 C 726 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 C 726 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 C 726 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 C 726 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 C 726 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 C 726 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 C 726 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 C 726 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 C 726 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 C 726 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 C 726 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 C 726 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 C 726 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 C 726 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 C 726 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 C 726 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 C 726 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 C 726 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 C 726 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 C 726 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 C 726 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 C 726 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 C 726 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 C 726 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 C 726 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 C 726 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 C 726 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 C 726 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 C 726 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 C 726 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 C 726 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 C 726 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 C 726 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 C 726 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 C 726 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 C 726 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 C 726 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 C 726 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 C 726 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 C 726 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 C 726 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 C 726 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 C 726 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 C 726 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 C 726 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 C 726 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 C 726 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 C 726 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 C 726 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 C 726 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 C 726 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 C 726 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 C 726 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
SEQRES 1 D 726 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 D 726 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 D 726 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 D 726 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 D 726 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 D 726 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 D 726 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 D 726 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 D 726 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 D 726 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 D 726 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 D 726 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 D 726 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 D 726 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 D 726 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 D 726 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 D 726 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 D 726 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 D 726 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 D 726 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 D 726 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 D 726 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 D 726 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 D 726 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 D 726 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 D 726 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 D 726 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 D 726 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 D 726 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 D 726 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 D 726 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 D 726 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 D 726 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 D 726 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 D 726 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 D 726 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 D 726 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 D 726 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 D 726 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 D 726 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 D 726 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 D 726 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 D 726 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 D 726 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 D 726 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 D 726 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 D 726 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 D 726 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 D 726 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 D 726 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 D 726 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 D 726 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 D 726 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 D 726 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 D 726 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 D 726 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER
HET KIQ B 901 31
HETNAM KIQ (1S,6R)-3-{[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,
HETNAM 2 KIQ 4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]CARBONYL}-6-(2,4,5-
HETNAM 3 KIQ TRIFLUOROPHENYL)CYCLOHEX-3-EN-1-AMINE
FORMUL 5 KIQ C19 H17 F6 N5 O
FORMUL 6 HOH *622(H2 O)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 PRO A 290 ILE A 295 1 6
HELIX 4 4 GLU A 421 MET A 425 5 5
HELIX 5 5 ASN A 497 GLN A 505 1 9
HELIX 6 6 ASN A 562 THR A 570 1 9
HELIX 7 7 GLY A 587 HIS A 592 1 6
HELIX 8 8 ALA A 593 ASN A 595 5 3
HELIX 9 9 THR A 600 LYS A 615 1 16
HELIX 10 10 SER A 630 GLY A 641 1 12
HELIX 11 11 ARG A 658 TYR A 662 5 5
HELIX 12 12 ASP A 663 GLY A 672 1 10
HELIX 13 13 ASN A 679 SER A 686 1 8
HELIX 14 14 VAL A 688 VAL A 698 5 11
HELIX 15 15 HIS A 712 VAL A 726 1 15
HELIX 16 16 SER A 744 SER A 764 1 21
HELIX 17 17 THR B 44 ASN B 51 1 8
HELIX 18 18 PHE B 95 GLY B 99 5 5
HELIX 19 19 ASP B 200 VAL B 207 1 8
HELIX 20 20 PRO B 290 ILE B 295 1 6
HELIX 21 21 GLU B 421 MET B 425 5 5
HELIX 22 22 ASN B 497 GLN B 505 1 9
HELIX 23 23 ASN B 562 ASN B 572 1 11
HELIX 24 24 GLY B 587 HIS B 592 1 6
HELIX 25 25 THR B 600 LYS B 615 1 16
HELIX 26 26 SER B 630 LEU B 640 1 11
HELIX 27 27 ARG B 658 TYR B 662 5 5
HELIX 28 28 ASP B 663 GLY B 672 1 10
HELIX 29 29 ASN B 679 SER B 686 1 8
HELIX 30 30 VAL B 688 VAL B 698 5 11
HELIX 31 31 PHE B 713 ASP B 725 1 13
HELIX 32 32 SER B 744 SER B 764 1 21
HELIX 33 33 THR C 44 ASN C 51 1 8
HELIX 34 34 GLU C 91 ASP C 96 5 6
HELIX 35 35 ASP C 200 VAL C 207 1 8
HELIX 36 36 PRO C 290 ILE C 295 1 6
HELIX 37 37 GLU C 421 MET C 425 5 5
HELIX 38 38 ASN C 497 GLN C 505 1 9
HELIX 39 39 ASN C 562 THR C 570 1 9
HELIX 40 40 GLY C 587 HIS C 592 1 6
HELIX 41 41 ALA C 593 ASN C 595 5 3
HELIX 42 42 THR C 600 MET C 616 1 17
HELIX 43 43 SER C 630 GLY C 641 1 12
HELIX 44 44 ARG C 658 TYR C 662 5 5
HELIX 45 45 ASP C 663 GLY C 672 1 10
HELIX 46 46 ASN C 679 SER C 686 1 8
HELIX 47 47 VAL C 688 VAL C 698 5 11
HELIX 48 48 PHE C 713 VAL C 726 1 14
HELIX 49 49 SER C 744 SER C 764 1 21
HELIX 50 50 THR D 44 LYS D 50 1 7
HELIX 51 51 ASP D 200 VAL D 207 1 8
HELIX 52 52 PRO D 290 ILE D 295 1 6
HELIX 53 53 GLU D 421 MET D 425 5 5
HELIX 54 54 ASN D 497 GLN D 505 1 9
HELIX 55 55 ASN D 562 THR D 570 1 9
HELIX 56 56 GLY D 587 HIS D 592 1 6
HELIX 57 57 ALA D 593 ASN D 595 5 3
HELIX 58 58 THR D 600 LYS D 615 1 16
HELIX 59 59 SER D 630 GLY D 641 1 12
HELIX 60 60 ARG D 658 TYR D 662 5 5
HELIX 61 61 ASP D 663 GLY D 672 1 10
HELIX 62 62 ASN D 679 SER D 686 1 8
HELIX 63 63 VAL D 688 VAL D 698 5 11
HELIX 64 64 HIS D 712 VAL D 726 1 15
HELIX 65 65 SER D 744 SER D 764 1 21
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 LEU A 60 TRP A 62 0
SHEET 2 B 4 GLU A 67 LYS A 71 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ILE A 76 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 B 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 C 4 ASP A 104 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O GLU A 117 N ASP A 104
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 THR A 152 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N GLN A 153
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O VAL A 271 N LEU A 223
SHEET 4 F 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 H 4 HIS A 298 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 H 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 ARG A 336 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 TRP A 305 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 I 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 I 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 L 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 L 4 LYS A 489 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 ASP A 545 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 ARG B 61 TRP B 62 0
SHEET 2 O 4 GLU B 67 TYR B 70 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 O 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 P 4 ILE B 102 ILE B 107 0
SHEET 2 P 4 PHE B 113 LYS B 122 -1 O GLU B 117 N ASN B 103
SHEET 3 P 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 P 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 Q 4 THR B 152 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O VAL B 167 N GLN B 153
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 Q 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O VAL B 271 N LEU B 223
SHEET 4 S 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 U 4 HIS B 298 TRP B 305 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 U 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 U 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 V 4 HIS B 298 TRP B 305 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 V 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 V 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 W 4 HIS B 363 PHE B 364 0
SHEET 2 W 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 W 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 W 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 X 4 VAL B 404 LEU B 410 0
SHEET 2 X 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 X 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 X 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 Y 4 TYR B 457 PHE B 461 0
SHEET 2 Y 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 Y 4 LYS B 489 GLU B 495 -1 O LEU B 494 N TYR B 480
SHEET 1 Z 8 SER B 511 LEU B 519 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 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O TRP B 627 N VAL B 546
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Z 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AA 4 ARG C 61 TRP C 62 0
SHEET 2 AA 4 GLU C 67 LYS C 71 -1 O LEU C 69 N ARG C 61
SHEET 3 AA 4 ILE C 76 ASN C 80 -1 O PHE C 79 N TYR C 68
SHEET 4 AA 4 SER C 86 LEU C 90 -1 O SER C 87 N VAL C 78
SHEET 1 AB 4 ASP C 104 ILE C 107 0
SHEET 2 AB 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AB 4 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 4 AB 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AC 4 TRP C 154 TRP C 157 0
SHEET 2 AC 4 LEU C 164 TRP C 168 -1 O ALA C 165 N THR C 156
SHEET 3 AC 4 ASP C 171 LYS C 175 -1 O TYR C 173 N TYR C 166
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 LYS C 267 N GLN C 227
SHEET 4 AE 4 SER C 284 ILE C 287 -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 LYS C 250 N PHE C 240
SHEET 1 AG 4 HIS C 298 THR C 307 0
SHEET 2 AG 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AG 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AG 4 TRP C 337 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 SER C 312 N THR C 304
SHEET 3 AH 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AH 4 HIS C 345 MET C 348 -1 O HIS C 345 N MET C 325
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 ALA C 409
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 4 TYR C 457 PHE C 461 0
SHEET 2 AK 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AK 4 LEU C 479 SER C 484 -1 O THR C 481 N LEU C 470
SHEET 4 AK 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AL 8 SER C 511 LEU C 519 0
SHEET 2 AL 8 THR C 522 LEU C 530 -1 O TYR C 526 N ASP C 515
SHEET 3 AL 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AL 8 TYR C 540 VAL C 546 1 N ASP C 545 O ALA C 576
SHEET 5 AL 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 542
SHEET 6 AL 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AL 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AL 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AM 4 LEU D 60 TRP D 62 0
SHEET 2 AM 4 GLU D 67 LYS D 71 -1 O LEU D 69 N ARG D 61
SHEET 3 AM 4 ILE D 76 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 4 AM 4 SER D 86 LEU D 90 -1 O PHE D 89 N ILE D 76
SHEET 1 AN 4 ASP D 104 ILE 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 THR D 129 N VAL D 121
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 TYR D 173 N TYR D 166
SHEET 4 AO 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AP 3 ILE D 194 ASN D 196 0
SHEET 2 AP 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AP 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AQ 4 ILE D 194 ASN D 196 0
SHEET 2 AQ 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AQ 4 THR D 265 ASN D 272 -1 O LYS D 267 N GLN D 227
SHEET 4 AQ 4 ILE D 285 ILE D 287 -1 O ILE D 285 N VAL D 270
SHEET 1 AR 2 LEU D 235 PHE D 240 0
SHEET 2 AR 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AS 4 HIS D 298 TRP D 305 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 ASP D 326 N LEU D 313
SHEET 4 AS 4 TRP D 337 ASN D 338 -1 O ASN D 338 N ASP D 329
SHEET 1 AT 4 HIS D 298 TRP D 305 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 ASP D 326 N LEU D 313
SHEET 4 AT 4 HIS D 345 MET 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 ARG D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AU 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR 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 ILE D 418 N ILE D 405
SHEET 3 AV 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AV 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS 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 GLN D 469 N SER D 460
SHEET 3 AW 4 LEU D 479 SER D 484 -1 O LEU D 479 N CYS D 472
SHEET 4 AW 4 LYS D 489 GLU D 495 -1 O LEU D 491 N LEU D 482
SHEET 1 AX 8 SER D 511 LEU D 519 0
SHEET 2 AX 8 THR D 522 LEU D 530 -1 O THR D 522 N LEU D 519
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 ASP D 545 1 N LEU D 543 O ILE D 574
SHEET 5 AX 8 VAL D 619 TRP D 629 1 O ASP D 620 N TYR D 540
SHEET 6 AX 8 CYS D 649 VAL D 653 1 O ILE D 651 N ILE D 626
SHEET 7 AX 8 GLU D 699 GLY D 705 1 O LEU D 701 N ALA D 652
SHEET 8 AX 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 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.06
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.07
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.04
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.08
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
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 2.04
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.04
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.04
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.04
SSBOND 17 CYS D 385 CYS D 394 1555 1555 2.04
SSBOND 18 CYS D 444 CYS D 447 1555 1555 2.04
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.04
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.06
CISPEP 1 ALA A 289 PRO A 290 0 -4.66
CISPEP 2 GLY A 474 PRO A 475 0 9.83
CISPEP 3 ALA B 289 PRO B 290 0 -8.38
CISPEP 4 GLY B 474 PRO B 475 0 5.77
CISPEP 5 ALA C 289 PRO C 290 0 -21.05
CISPEP 6 GLY C 474 PRO C 475 0 5.03
CISPEP 7 ALA D 289 PRO D 290 0 -6.12
CISPEP 8 GLY D 474 PRO D 475 0 2.68
CRYST1 119.933 126.419 127.531 90.00 100.26 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008338 0.000000 0.001509 0.00000
SCALE2 0.000000 0.007910 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007969 0.00000
TER 5950 SER A 764
TER 11900 SER B 764
TER 17850 SER C 764
TER 23800 SER D 764
MASTER 430 0 1 65 200 0 0 624449 4 71 224
END |