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HEADER HYDROLASE 28-JUL-16 5LLS
TITLE PORCINE DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH 8-(3-AMINOPIPERIDIN-1-
TITLE 2 YL)-7-[(2-BROMOPHENYL)METHYL]-1,3-DIMETHYL-2,3,6,7-TETRAHYDRO-1H-
TITLE 3 PURINE-2,6-DIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV,DPP IV,T-CELL ACTIVATION ANTIGEN
COMPND 5 CD26;
COMPND 6 EC: 3.4.14.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823
KEYWDS PEPTIDASE, INHIBITOR, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.NAR,M.BLAESSE
REVDAT 1 14-SEP-16 5LLS 0
JRNL AUTH G.SCHNAPP,T.KLEIN,Y.HOEVELS,R.A.BAKKER,H.NAR
JRNL TITL COMPARATIVE ANALYSIS OF BINDING KINETICS AND THERMODYNAMICS
JRNL TITL 2 OF DIPEPTIDYL PEPTIDASE-4 INHIBITORS AND THEIR RELATIONSHIP
JRNL TITL 3 TO STRUCTURE.
JRNL REF J.MED.CHEM. V. 59 7466 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 27438064
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00475
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.3
REMARK 3 NUMBER OF REFLECTIONS : 106928
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 5218
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.030
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.47
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 21.59
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2121
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2280
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2014
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.04
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 107
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23840
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 706
REMARK 3 SOLVENT ATOMS : 1021
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.43530
REMARK 3 B22 (A**2) : 12.35410
REMARK 3 B33 (A**2) : 2.08120
REMARK 3 B12 (A**2) : 3.76680
REMARK 3 B13 (A**2) : -1.84550
REMARK 3 B23 (A**2) : -0.89440
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.310
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.916
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.280
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.152
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.288
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.903
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 25315 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 34538 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 8589 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 612 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 3637 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 25315 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 3293 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 29238 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.96
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.26
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8160 27.4676 5.7138
REMARK 3 T TENSOR
REMARK 3 T11: -0.2435 T22: -0.0277
REMARK 3 T33: 0.0261 T12: 0.0601
REMARK 3 T13: -0.0182 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.4085 L22: 0.8401
REMARK 3 L33: 0.4688 L12: -0.1490
REMARK 3 L13: 0.0147 L23: 0.0729
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: -0.0024 S13: 0.1411
REMARK 3 S21: -0.0569 S22: -0.0050 S23: -0.0329
REMARK 3 S31: -0.0311 S32: 0.0114 S33: -0.0027
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3634 -27.4398 -5.9478
REMARK 3 T TENSOR
REMARK 3 T11: -0.1685 T22: -0.0375
REMARK 3 T33: -0.0566 T12: 0.0549
REMARK 3 T13: -0.0086 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.4225 L22: 1.0791
REMARK 3 L33: 0.3753 L12: -0.0759
REMARK 3 L13: 0.0537 L23: 0.0413
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: 0.0180 S13: -0.0983
REMARK 3 S21: -0.1349 S22: 0.0107 S23: 0.1226
REMARK 3 S31: 0.0564 S32: -0.0525 S33: 0.0079
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1652 12.8398 74.4074
REMARK 3 T TENSOR
REMARK 3 T11: -0.2074 T22: -0.0349
REMARK 3 T33: -0.0550 T12: 0.0304
REMARK 3 T13: -0.0183 T23: -0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.3238 L22: 1.0496
REMARK 3 L33: 0.7260 L12: -0.0659
REMARK 3 L13: -0.0339 L23: 0.0502
REMARK 3 S TENSOR
REMARK 3 S11: -0.0530 S12: -0.0446 S13: 0.0295
REMARK 3 S21: 0.1660 S22: 0.0074 S23: -0.0300
REMARK 3 S31: -0.0527 S32: -0.0482 S33: 0.0456
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5271 -42.0329 65.0060
REMARK 3 T TENSOR
REMARK 3 T11: -0.1504 T22: -0.1013
REMARK 3 T33: -0.0569 T12: 0.0109
REMARK 3 T13: 0.0119 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.4270 L22: 0.7921
REMARK 3 L33: 0.9921 L12: 0.2129
REMARK 3 L13: 0.2324 L23: 0.1167
REMARK 3 S TENSOR
REMARK 3 S11: 0.0595 S12: 0.0158 S13: -0.1142
REMARK 3 S21: 0.0254 S22: -0.0176 S23: -0.0467
REMARK 3 S31: 0.2570 S32: -0.0132 S33: -0.0419
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3446 22.9707 16.4885
REMARK 3 T TENSOR
REMARK 3 T11: -0.1439 T22: 0.0443
REMARK 3 T33: 0.0438 T12: 0.1228
REMARK 3 T13: 0.0528 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.4540 L22: 1.5880
REMARK 3 L33: 0.4021 L12: -0.0629
REMARK 3 L13: 0.8391 L23: -0.0869
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: -0.0335 S13: 0.0132
REMARK 3 S21: 0.1432 S22: 0.0090 S23: 0.0213
REMARK 3 S31: 0.1205 S32: -0.0036 S33: -0.0255
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { F|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1266 -29.3217 0.2190
REMARK 3 T TENSOR
REMARK 3 T11: -0.1618 T22: -0.0006
REMARK 3 T33: 0.0709 T12: 0.0694
REMARK 3 T13: -0.0758 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.4966 L22: 1.5367
REMARK 3 L33: 0.7879 L12: -0.0015
REMARK 3 L13: -0.8376 L23: -0.2235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: -0.0059 S13: -0.0457
REMARK 3 S21: 0.1541 S22: -0.0137 S23: 0.0142
REMARK 3 S31: -0.1124 S32: 0.0003 S33: -0.0011
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { H|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7804 -38.3779 57.3089
REMARK 3 T TENSOR
REMARK 3 T11: -0.0795 T22: 0.0122
REMARK 3 T33: -0.0717 T12: 0.0080
REMARK 3 T13: -0.0856 T23: 0.0809
REMARK 3 L TENSOR
REMARK 3 L11: 2.6827 L22: 1.6602
REMARK 3 L33: 1.2481 L12: -0.2838
REMARK 3 L13: -1.0861 L23: 0.8553
REMARK 3 S TENSOR
REMARK 3 S11: 0.0222 S12: 0.0093 S13: -0.0430
REMARK 3 S21: -0.0385 S22: -0.0234 S23: 0.1225
REMARK 3 S31: 0.0000 S32: -0.0979 S33: 0.0012
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5LLS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000932.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 111933
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.410
REMARK 200 RESOLUTION RANGE LOW (A) : 35.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.3
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: 2AJ8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 2000, 0.1 M TRIS PH 8, 0.1 M
REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, TEMPERATURE 293K
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: 9330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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: 9520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 TRP A 5
REMARK 465 LYS A 6
REMARK 465 VAL A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 LEU A 12
REMARK 465 GLY A 13
REMARK 465 ILE A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 VAL A 18
REMARK 465 THR A 19
REMARK 465 VAL A 20
REMARK 465 ILE A 21
REMARK 465 THR A 22
REMARK 465 VAL A 23
REMARK 465 PRO A 24
REMARK 465 VAL A 25
REMARK 465 VAL A 26
REMARK 465 LEU A 27
REMARK 465 LEU A 28
REMARK 465 ASN A 29
REMARK 465 LYS A 30
REMARK 465 GLY A 31
REMARK 465 THR A 32
REMARK 465 ASP A 33
REMARK 465 ASP A 34
REMARK 465 ALA A 35
REMARK 465 ALA A 36
REMARK 465 ALA A 37
REMARK 465 ASP A 38
REMARK 465 SER A 39
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 THR B 3
REMARK 465 PRO B 4
REMARK 465 TRP B 5
REMARK 465 LYS B 6
REMARK 465 VAL B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 LEU B 12
REMARK 465 GLY B 13
REMARK 465 ILE B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 VAL B 18
REMARK 465 THR B 19
REMARK 465 VAL B 20
REMARK 465 ILE B 21
REMARK 465 THR B 22
REMARK 465 VAL B 23
REMARK 465 PRO B 24
REMARK 465 VAL B 25
REMARK 465 VAL B 26
REMARK 465 LEU B 27
REMARK 465 LEU B 28
REMARK 465 ASN B 29
REMARK 465 LYS B 30
REMARK 465 GLY B 31
REMARK 465 THR B 32
REMARK 465 ASP B 33
REMARK 465 ASP B 34
REMARK 465 ALA B 35
REMARK 465 ALA B 36
REMARK 465 ALA B 37
REMARK 465 ASP B 38
REMARK 465 SER B 39
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 THR C 3
REMARK 465 PRO C 4
REMARK 465 TRP C 5
REMARK 465 LYS C 6
REMARK 465 VAL C 7
REMARK 465 LEU C 8
REMARK 465 LEU C 9
REMARK 465 GLY C 10
REMARK 465 LEU C 11
REMARK 465 LEU C 12
REMARK 465 GLY C 13
REMARK 465 ILE C 14
REMARK 465 ALA C 15
REMARK 465 ALA C 16
REMARK 465 LEU C 17
REMARK 465 VAL C 18
REMARK 465 THR C 19
REMARK 465 VAL C 20
REMARK 465 ILE C 21
REMARK 465 THR C 22
REMARK 465 VAL C 23
REMARK 465 PRO C 24
REMARK 465 VAL C 25
REMARK 465 VAL C 26
REMARK 465 LEU C 27
REMARK 465 LEU C 28
REMARK 465 ASN C 29
REMARK 465 LYS C 30
REMARK 465 GLY C 31
REMARK 465 THR C 32
REMARK 465 ASP C 33
REMARK 465 ASP C 34
REMARK 465 ALA C 35
REMARK 465 ALA C 36
REMARK 465 ALA C 37
REMARK 465 ASP C 38
REMARK 465 SER C 39
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 THR D 3
REMARK 465 PRO D 4
REMARK 465 TRP D 5
REMARK 465 LYS D 6
REMARK 465 VAL D 7
REMARK 465 LEU D 8
REMARK 465 LEU D 9
REMARK 465 GLY D 10
REMARK 465 LEU D 11
REMARK 465 LEU D 12
REMARK 465 GLY D 13
REMARK 465 ILE D 14
REMARK 465 ALA D 15
REMARK 465 ALA D 16
REMARK 465 LEU D 17
REMARK 465 VAL D 18
REMARK 465 THR D 19
REMARK 465 VAL D 20
REMARK 465 ILE D 21
REMARK 465 THR D 22
REMARK 465 VAL D 23
REMARK 465 PRO D 24
REMARK 465 VAL D 25
REMARK 465 VAL D 26
REMARK 465 LEU D 27
REMARK 465 LEU D 28
REMARK 465 ASN D 29
REMARK 465 LYS D 30
REMARK 465 GLY D 31
REMARK 465 THR D 32
REMARK 465 ASP D 33
REMARK 465 ASP D 34
REMARK 465 ALA D 35
REMARK 465 ALA D 36
REMARK 465 ALA D 37
REMARK 465 ASP D 38
REMARK 465 SER D 39
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 GLN A 123 -90.48 -110.60
REMARK 500 TRP A 124 -145.11 -101.02
REMARK 500 ASN A 151 33.25 73.15
REMARK 500 HIS A 162 36.33 -143.63
REMARK 500 VAL A 193 -66.25 -121.30
REMARK 500 ALA A 213 40.17 -140.44
REMARK 500 SER A 242 -162.30 60.84
REMARK 500 GLN A 320 31.65 72.32
REMARK 500 LYS A 423 17.32 58.34
REMARK 500 TYR A 547 -71.35 -122.37
REMARK 500 ALA A 548 14.81 59.08
REMARK 500 ARG A 597 56.66 -150.92
REMARK 500 THR A 600 -94.51 -103.78
REMARK 500 SER A 630 -122.70 55.31
REMARK 500 ASP A 678 -108.16 -105.28
REMARK 500 ASN A 710 -76.56 -78.91
REMARK 500 MET A 733 104.82 -166.14
REMARK 500 ASP A 739 -152.55 -96.51
REMARK 500 GLN B 123 -90.54 -110.69
REMARK 500 TRP B 124 -144.97 -101.01
REMARK 500 ASN B 151 32.66 73.34
REMARK 500 HIS B 162 36.40 -141.75
REMARK 500 VAL B 193 -66.00 -120.35
REMARK 500 SER B 242 -162.43 61.93
REMARK 500 GLN B 320 31.25 72.02
REMARK 500 LYS B 423 18.51 58.81
REMARK 500 TYR B 547 -70.67 -124.42
REMARK 500 ALA B 548 16.38 57.26
REMARK 500 GLN B 586 15.43 -140.42
REMARK 500 ARG B 597 55.91 -152.92
REMARK 500 THR B 600 -94.33 -103.72
REMARK 500 SER B 630 -107.47 52.85
REMARK 500 ASP B 678 -104.32 -105.97
REMARK 500 ALA B 707 32.12 -94.65
REMARK 500 ASN B 710 -71.09 -90.44
REMARK 500 MET B 733 104.53 -164.00
REMARK 500 ASP B 739 -152.45 -95.06
REMARK 500 GLN C 123 -90.63 -110.67
REMARK 500 TRP C 124 -145.86 -101.06
REMARK 500 ASN C 151 33.16 72.72
REMARK 500 HIS C 162 36.48 -142.09
REMARK 500 VAL C 193 -66.26 -121.77
REMARK 500 VAL C 207 -60.12 -105.12
REMARK 500 SER C 242 -160.41 61.67
REMARK 500 GLN C 320 31.59 71.90
REMARK 500 LYS C 423 16.94 59.70
REMARK 500 TYR C 547 -71.36 -124.47
REMARK 500 ALA C 548 16.19 58.54
REMARK 500 ARG C 597 56.04 -150.12
REMARK 500 THR C 600 -94.55 -103.51
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
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 A1144 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A1145 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A1146 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH A1147 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH A1148 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH A1149 DISTANCE = 7.52 ANGSTROMS
REMARK 525 HOH A1150 DISTANCE = 7.74 ANGSTROMS
REMARK 525 HOH A1151 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH A1152 DISTANCE = 8.30 ANGSTROMS
REMARK 525 HOH A1153 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH A1154 DISTANCE = 12.74 ANGSTROMS
REMARK 525 HOH B1172 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B1173 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH B1174 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B1175 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B1176 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH B1177 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH B1178 DISTANCE = 7.67 ANGSTROMS
REMARK 525 HOH B1179 DISTANCE = 8.84 ANGSTROMS
REMARK 525 HOH B1180 DISTANCE = 11.36 ANGSTROMS
REMARK 525 HOH C1164 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C1165 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C1166 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH C1167 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH C1168 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH C1169 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH C1170 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH C1171 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH C1172 DISTANCE = 9.10 ANGSTROMS
REMARK 525 HOH C1173 DISTANCE = 11.62 ANGSTROMS
REMARK 525 HOH D1103 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH D1104 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH D1105 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH D1106 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH D1107 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH D1108 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH D1109 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH D1110 DISTANCE = 8.36 ANGSTROMS
REMARK 525 HOH D1111 DISTANCE = 8.37 ANGSTROMS
REMARK 525 HOH D1112 DISTANCE = 10.63 ANGSTROMS
REMARK 525 HOH D1113 DISTANCE = 11.46 ANGSTROMS
REMARK 525 HOH D1114 DISTANCE = 12.48 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Z8 A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Z8 A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Z8 B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Z8 B 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Z8 C 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Z8 C 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Z8 D 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Z8 D 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 801 bound
REMARK 800 to ASN A 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound
REMARK 800 to ASN A 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 803 through NAG A 804 bound to ASN A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 805 bound
REMARK 800 to ASN A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 806 bound
REMARK 800 to ASN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 807 through NAG A 808 bound to ASN A 685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 801 bound
REMARK 800 to ASN B 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 802 through NAG B 803 bound to ASN B 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 804 bound
REMARK 800 to ASN B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 805 bound
REMARK 800 to ASN B 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 806 bound
REMARK 800 to ASN B 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 807 through NAG B 808 bound to ASN B 685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 801 bound
REMARK 800 to ASN C 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 802 bound
REMARK 800 to ASN C 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 803 bound
REMARK 800 to ASN C 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 804 bound
REMARK 800 to ASN C 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 805 bound
REMARK 800 to ASN C 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 806 through NAG C 807 bound to ASN C 685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 801 bound
REMARK 800 to ASN D 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 802 through NAG D 803 bound to ASN D 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 804 through NAG D 805 bound to ASN D 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 806 bound
REMARK 800 to ASN D 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 807 through NAG D 808 bound to ASN D 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 809 through NAG D 810 bound to ASN D 685
DBREF 5LLS A 1 766 UNP P22411 DPP4_PIG 1 766
DBREF 5LLS B 1 766 UNP P22411 DPP4_PIG 1 766
DBREF 5LLS C 1 766 UNP P22411 DPP4_PIG 1 766
DBREF 5LLS D 1 766 UNP P22411 DPP4_PIG 1 766
SEQRES 1 A 766 MET LYS THR PRO TRP LYS VAL LEU LEU GLY LEU LEU GLY
SEQRES 2 A 766 ILE ALA ALA LEU VAL THR VAL ILE THR VAL PRO VAL VAL
SEQRES 3 A 766 LEU LEU ASN LYS GLY THR ASP ASP ALA ALA ALA ASP SER
SEQRES 4 A 766 ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER THR
SEQRES 5 A 766 PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER ASP
SEQRES 6 A 766 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 7 A 766 PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU GLU
SEQRES 8 A 766 ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN ASP
SEQRES 9 A 766 TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE GLU
SEQRES 10 A 766 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 11 A 766 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 12 A 766 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 13 A 766 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 14 A 766 ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER SER
SEQRES 15 A 766 GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE TYR
SEQRES 16 A 766 ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 17 A 766 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 18 A 766 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 19 A 766 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 20 A 766 TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA GLY
SEQRES 21 A 766 ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP THR
SEQRES 22 A 766 ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR GLN
SEQRES 23 A 766 ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS TYR
SEQRES 24 A 766 LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE SER
SEQRES 25 A 766 LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE ILE
SEQRES 26 A 766 ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP ILE
SEQRES 27 A 766 SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR THR
SEQRES 28 A 766 GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE
SEQRES 29 A 766 THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 30 A 766 GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR ASP
SEQRES 31 A 766 LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP GLU
SEQRES 32 A 766 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 33 A 766 TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY ARG
SEQRES 34 A 766 ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS VAL
SEQRES 35 A 766 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 36 A 766 TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR TYR
SEQRES 37 A 766 GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 38 A 766 LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL LEU
SEQRES 39 A 766 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP VAL
SEQRES 40 A 766 GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU HIS
SEQRES 41 A 766 GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 42 A 766 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU VAL
SEQRES 43 A 766 TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL PHE
SEQRES 44 A 766 ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 45 A 766 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 46 A 766 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 47 A 766 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR ARG
SEQRES 48 A 766 GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG ILE
SEQRES 49 A 766 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 50 A 766 MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 51 A 766 ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR ASP
SEQRES 52 A 766 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 53 A 766 GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL MET
SEQRES 54 A 766 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 55 A 766 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 56 A 766 SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY VAL
SEQRES 57 A 766 ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 58 A 766 ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 59 A 766 MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 766 MET LYS THR PRO TRP LYS VAL LEU LEU GLY LEU LEU GLY
SEQRES 2 B 766 ILE ALA ALA LEU VAL THR VAL ILE THR VAL PRO VAL VAL
SEQRES 3 B 766 LEU LEU ASN LYS GLY THR ASP ASP ALA ALA ALA ASP SER
SEQRES 4 B 766 ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER THR
SEQRES 5 B 766 PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER ASP
SEQRES 6 B 766 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 7 B 766 PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU GLU
SEQRES 8 B 766 ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN ASP
SEQRES 9 B 766 TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE GLU
SEQRES 10 B 766 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 11 B 766 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 12 B 766 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 13 B 766 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 14 B 766 ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER SER
SEQRES 15 B 766 GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE TYR
SEQRES 16 B 766 ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 17 B 766 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 18 B 766 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 19 B 766 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 20 B 766 TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA GLY
SEQRES 21 B 766 ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP THR
SEQRES 22 B 766 ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR GLN
SEQRES 23 B 766 ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS TYR
SEQRES 24 B 766 LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE SER
SEQRES 25 B 766 LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE ILE
SEQRES 26 B 766 ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP ILE
SEQRES 27 B 766 SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR THR
SEQRES 28 B 766 GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE
SEQRES 29 B 766 THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 30 B 766 GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR ASP
SEQRES 31 B 766 LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP GLU
SEQRES 32 B 766 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 33 B 766 TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY ARG
SEQRES 34 B 766 ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS VAL
SEQRES 35 B 766 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 36 B 766 TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR TYR
SEQRES 37 B 766 GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 38 B 766 LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL LEU
SEQRES 39 B 766 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP VAL
SEQRES 40 B 766 GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU HIS
SEQRES 41 B 766 GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 42 B 766 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU VAL
SEQRES 43 B 766 TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL PHE
SEQRES 44 B 766 ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 45 B 766 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 46 B 766 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 47 B 766 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR ARG
SEQRES 48 B 766 GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG ILE
SEQRES 49 B 766 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 50 B 766 MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 51 B 766 ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR ASP
SEQRES 52 B 766 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 53 B 766 GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL MET
SEQRES 54 B 766 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 55 B 766 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 56 B 766 SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY VAL
SEQRES 57 B 766 ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 58 B 766 ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 59 B 766 MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 766 MET LYS THR PRO TRP LYS VAL LEU LEU GLY LEU LEU GLY
SEQRES 2 C 766 ILE ALA ALA LEU VAL THR VAL ILE THR VAL PRO VAL VAL
SEQRES 3 C 766 LEU LEU ASN LYS GLY THR ASP ASP ALA ALA ALA ASP SER
SEQRES 4 C 766 ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER THR
SEQRES 5 C 766 PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER ASP
SEQRES 6 C 766 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 7 C 766 PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU GLU
SEQRES 8 C 766 ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN ASP
SEQRES 9 C 766 TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE GLU
SEQRES 10 C 766 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 11 C 766 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 12 C 766 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 13 C 766 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 14 C 766 ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER SER
SEQRES 15 C 766 GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE TYR
SEQRES 16 C 766 ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 17 C 766 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 18 C 766 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 19 C 766 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 20 C 766 TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA GLY
SEQRES 21 C 766 ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP THR
SEQRES 22 C 766 ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR GLN
SEQRES 23 C 766 ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS TYR
SEQRES 24 C 766 LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE SER
SEQRES 25 C 766 LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE ILE
SEQRES 26 C 766 ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP ILE
SEQRES 27 C 766 SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR THR
SEQRES 28 C 766 GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE
SEQRES 29 C 766 THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 30 C 766 GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR ASP
SEQRES 31 C 766 LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP GLU
SEQRES 32 C 766 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 33 C 766 TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY ARG
SEQRES 34 C 766 ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS VAL
SEQRES 35 C 766 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 36 C 766 TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR TYR
SEQRES 37 C 766 GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 38 C 766 LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL LEU
SEQRES 39 C 766 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP VAL
SEQRES 40 C 766 GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU HIS
SEQRES 41 C 766 GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 42 C 766 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU VAL
SEQRES 43 C 766 TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL PHE
SEQRES 44 C 766 ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 45 C 766 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 46 C 766 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 47 C 766 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR ARG
SEQRES 48 C 766 GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG ILE
SEQRES 49 C 766 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 50 C 766 MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 51 C 766 ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR ASP
SEQRES 52 C 766 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 53 C 766 GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL MET
SEQRES 54 C 766 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 55 C 766 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 56 C 766 SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY VAL
SEQRES 57 C 766 ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 58 C 766 ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 59 C 766 MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 766 MET LYS THR PRO TRP LYS VAL LEU LEU GLY LEU LEU GLY
SEQRES 2 D 766 ILE ALA ALA LEU VAL THR VAL ILE THR VAL PRO VAL VAL
SEQRES 3 D 766 LEU LEU ASN LYS GLY THR ASP ASP ALA ALA ALA ASP SER
SEQRES 4 D 766 ARG ARG THR TYR THR LEU THR ASP TYR LEU LYS SER THR
SEQRES 5 D 766 PHE ARG VAL LYS PHE TYR THR LEU GLN TRP ILE SER ASP
SEQRES 6 D 766 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU LEU
SEQRES 7 D 766 PHE ASN ALA GLU TYR GLY ASN SER SER ILE PHE LEU GLU
SEQRES 8 D 766 ASN SER THR PHE ASP GLU LEU GLY TYR SER THR ASN ASP
SEQRES 9 D 766 TYR SER VAL SER PRO ASP ARG GLN PHE ILE LEU PHE GLU
SEQRES 10 D 766 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 11 D 766 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 12 D 766 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP ILE THR
SEQRES 13 D 766 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 14 D 766 ASN ASP ILE TYR VAL LYS ASN GLU PRO ASN LEU SER SER
SEQRES 15 D 766 GLN ARG ILE THR TRP THR GLY LYS GLU ASN VAL ILE TYR
SEQRES 16 D 766 ASN GLY VAL THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 17 D 766 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 18 D 766 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 19 D 766 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 20 D 766 TYR PRO LYS THR VAL ARG ILE PRO TYR PRO LYS ALA GLY
SEQRES 21 D 766 ALA GLU ASN PRO THR VAL LYS PHE PHE VAL VAL ASP THR
SEQRES 22 D 766 ARG THR LEU SER PRO ASN ALA SER VAL THR SER TYR GLN
SEQRES 23 D 766 ILE VAL PRO PRO ALA SER VAL LEU ILE GLY ASP HIS TYR
SEQRES 24 D 766 LEU CYS GLY VAL THR TRP VAL THR GLU GLU ARG ILE SER
SEQRES 25 D 766 LEU GLN TRP ILE ARG ARG ALA GLN ASN TYR SER ILE ILE
SEQRES 26 D 766 ASP ILE CYS ASP TYR ASP GLU SER THR GLY ARG TRP ILE
SEQRES 27 D 766 SER SER VAL ALA ARG GLN HIS ILE GLU ILE SER THR THR
SEQRES 28 D 766 GLY TRP VAL GLY ARG PHE ARG PRO ALA GLU PRO HIS PHE
SEQRES 29 D 766 THR SER ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 30 D 766 GLU GLU GLY TYR LYS HIS ILE CYS HIS PHE GLN THR ASP
SEQRES 31 D 766 LYS SER ASN CYS THR PHE ILE THR LYS GLY ALA TRP GLU
SEQRES 32 D 766 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 33 D 766 TYR ILE SER ASN GLU HIS LYS GLY MET PRO GLY GLY ARG
SEQRES 34 D 766 ASN LEU TYR ARG ILE GLN LEU ASN ASP TYR THR LYS VAL
SEQRES 35 D 766 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 36 D 766 TYR TYR SER ALA SER PHE SER ASN LYS ALA LYS TYR TYR
SEQRES 37 D 766 GLN LEU ARG CYS PHE GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 38 D 766 LEU HIS SER SER SER SER ASP LYS GLU LEU ARG VAL LEU
SEQRES 39 D 766 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASP VAL
SEQRES 40 D 766 GLN MET PRO SER LYS LYS LEU ASP VAL ILE ASN LEU HIS
SEQRES 41 D 766 GLY THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 42 D 766 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU ILE GLU VAL
SEQRES 43 D 766 TYR ALA GLY PRO CYS SER GLN LYS VAL ASP THR VAL PHE
SEQRES 44 D 766 ARG LEU SER TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 45 D 766 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 46 D 766 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 47 D 766 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA THR ARG
SEQRES 48 D 766 GLN PHE SER LYS MET GLY PHE VAL ASP ASP LYS ARG ILE
SEQRES 49 D 766 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 50 D 766 MET VAL LEU GLY ALA GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 51 D 766 ILE ALA VAL ALA PRO VAL SER LYS TRP GLU TYR TYR ASP
SEQRES 52 D 766 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 53 D 766 GLU ASP ASN LEU ASP TYR TYR ARG ASN SER THR VAL MET
SEQRES 54 D 766 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 55 D 766 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 56 D 766 SER ALA GLN LEU SER LYS ALA LEU VAL ASP ALA GLY VAL
SEQRES 57 D 766 ASP PHE GLN THR MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 58 D 766 ILE ALA SER ASN MET ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 59 D 766 MET SER HIS PHE LEU LYS GLN CYS PHE SER LEU PRO
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET NAG A 807 14
HET NAG A 808 14
HET 6Z8 A 809 28
HET SO4 A 810 5
HET 6Z8 A 811 28
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 805 14
HET NAG B 806 14
HET NAG B 807 14
HET NAG B 808 14
HET 6Z8 B 809 28
HET SO4 B 810 5
HET 6Z8 B 811 28
HET NAG C 801 14
HET NAG C 802 14
HET NAG C 803 14
HET NAG C 804 14
HET NAG C 805 14
HET NAG C 806 14
HET NAG C 807 14
HET 6Z8 C 808 28
HET SO4 C 809 5
HET 6Z8 C 810 28
HET NAG D 801 14
HET NAG D 802 14
HET NAG D 803 14
HET NAG D 804 14
HET NAG D 805 14
HET NAG D 806 14
HET NAG D 807 14
HET NAG D 808 14
HET NAG D 809 14
HET NAG D 810 14
HET 6Z8 D 811 28
HET SO4 D 812 5
HET 6Z8 D 813 28
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 6Z8 8-[(3~{R})-3-AZANYLPIPERIDIN-1-YL]-7-[(2-BROMOPHENYL)
HETNAM 2 6Z8 METHYL]-1,3-DIMETHYL-PURINE-2,6-DIONE
HETNAM SO4 SULFATE ION
FORMUL 5 NAG 33(C8 H15 N O6)
FORMUL 11 6Z8 8(C19 H23 BR N6 O2)
FORMUL 12 SO4 4(O4 S 2-)
FORMUL 41 HOH *1021(H2 O)
HELIX 1 AA1 THR A 44 LYS A 50 1 7
HELIX 2 AA2 GLU A 91 LEU A 98 1 8
HELIX 3 AA3 ASP A 200 VAL A 207 1 8
HELIX 4 AA4 ARG A 274 LEU A 276 5 3
HELIX 5 AA5 PRO A 290 ILE A 295 1 6
HELIX 6 AA6 SER A 340 ALA A 342 5 3
HELIX 7 AA7 GLU A 421 MET A 425 5 5
HELIX 8 AA8 ASN A 497 GLN A 505 1 9
HELIX 9 AA9 SER A 562 THR A 570 1 9
HELIX 10 AB1 GLY A 587 HIS A 592 1 6
HELIX 11 AB2 ALA A 593 ASN A 595 5 3
HELIX 12 AB3 THR A 600 MET A 616 1 17
HELIX 13 AB4 SER A 630 GLY A 641 1 12
HELIX 14 AB5 LYS A 658 TYR A 662 5 5
HELIX 15 AB6 ASP A 663 GLY A 672 1 10
HELIX 16 AB7 ASN A 679 ASN A 685 1 7
HELIX 17 AB8 SER A 686 THR A 687 5 2
HELIX 18 AB9 VAL A 688 VAL A 698 5 11
HELIX 19 AC1 HIS A 712 ALA A 726 1 15
HELIX 20 AC2 SER A 744 PHE A 763 1 20
HELIX 21 AC3 THR B 44 LYS B 50 1 7
HELIX 22 AC4 GLU B 91 GLY B 99 1 9
HELIX 23 AC5 ASP B 200 VAL B 207 1 8
HELIX 24 AC6 ARG B 274 LEU B 276 5 3
HELIX 25 AC7 PRO B 290 ILE B 295 1 6
HELIX 26 AC8 SER B 340 ALA B 342 5 3
HELIX 27 AC9 GLU B 421 MET B 425 5 5
HELIX 28 AD1 ASN B 497 GLN B 505 1 9
HELIX 29 AD2 SER B 562 THR B 570 1 9
HELIX 30 AD3 GLY B 587 HIS B 592 1 6
HELIX 31 AD4 ALA B 593 ASN B 595 5 3
HELIX 32 AD5 THR B 600 MET B 616 1 17
HELIX 33 AD6 SER B 630 GLY B 641 1 12
HELIX 34 AD7 LYS B 658 TYR B 662 5 5
HELIX 35 AD8 ASP B 663 GLY B 672 1 10
HELIX 36 AD9 ASN B 679 ASN B 685 1 7
HELIX 37 AE1 SER B 686 THR B 687 5 2
HELIX 38 AE2 VAL B 688 VAL B 698 5 11
HELIX 39 AE3 HIS B 712 ALA B 726 1 15
HELIX 40 AE4 SER B 744 PHE B 763 1 20
HELIX 41 AE5 THR C 44 LYS C 50 1 7
HELIX 42 AE6 GLU C 91 LEU C 98 1 8
HELIX 43 AE7 ASP C 200 GLU C 206 1 7
HELIX 44 AE8 ARG C 274 LEU C 276 5 3
HELIX 45 AE9 PRO C 290 ILE C 295 1 6
HELIX 46 AF1 SER C 340 ALA C 342 5 3
HELIX 47 AF2 GLU C 421 MET C 425 5 5
HELIX 48 AF3 ASN C 497 GLN C 505 1 9
HELIX 49 AF4 SER C 562 THR C 570 1 9
HELIX 50 AF5 GLY C 587 HIS C 592 1 6
HELIX 51 AF6 ALA C 593 ASN C 595 5 3
HELIX 52 AF7 THR C 600 MET C 616 1 17
HELIX 53 AF8 SER C 630 GLY C 641 1 12
HELIX 54 AF9 LYS C 658 TYR C 662 5 5
HELIX 55 AG1 ASP C 663 GLY C 672 1 10
HELIX 56 AG2 ASN C 679 ASN C 685 1 7
HELIX 57 AG3 SER C 686 THR C 687 5 2
HELIX 58 AG4 VAL C 688 VAL C 698 5 11
HELIX 59 AG5 PHE C 713 ALA C 726 1 14
HELIX 60 AG6 SER C 744 SER C 764 1 21
HELIX 61 AG7 THR D 44 LYS D 50 1 7
HELIX 62 AG8 GLU D 91 LEU D 98 1 8
HELIX 63 AG9 ASP D 200 GLU D 206 1 7
HELIX 64 AH1 ARG D 274 LEU D 276 5 3
HELIX 65 AH2 PRO D 290 ILE D 295 1 6
HELIX 66 AH3 SER D 340 ALA D 342 5 3
HELIX 67 AH4 GLU D 421 MET D 425 5 5
HELIX 68 AH5 ASN D 497 GLN D 505 1 9
HELIX 69 AH6 SER D 562 THR D 570 1 9
HELIX 70 AH7 GLY D 587 HIS D 592 1 6
HELIX 71 AH8 ALA D 593 ASN D 595 5 3
HELIX 72 AH9 THR D 600 MET D 616 1 17
HELIX 73 AI1 SER D 630 GLY D 641 1 12
HELIX 74 AI2 LYS D 658 TYR D 662 5 5
HELIX 75 AI3 ASP D 663 GLY D 672 1 10
HELIX 76 AI4 ASN D 679 ASN D 685 1 7
HELIX 77 AI5 SER D 686 THR D 687 5 2
HELIX 78 AI6 VAL D 688 VAL D 698 5 11
HELIX 79 AI7 PHE D 713 ALA D 726 1 14
HELIX 80 AI8 SER D 744 PHE D 763 1 20
SHEET 1 AA1 2 ARG A 41 THR A 42 0
SHEET 2 AA1 2 VAL A 507 GLN A 508 1 O GLN A 508 N ARG A 41
SHEET 1 AA2 4 GLN A 61 TRP A 62 0
SHEET 2 AA2 4 GLU A 67 GLN A 72 -1 O LEU A 69 N GLN A 61
SHEET 3 AA2 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 AA2 4 SER A 86 LEU A 90 -1 O SER A 87 N LEU A 78
SHEET 1 AA3 4 ASP A 104 VAL A 107 0
SHEET 2 AA3 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AA3 4 TYR A 128 ASP A 136 -1 O ASP A 133 N PHE A 116
SHEET 4 AA3 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AA4 4 THR A 152 TRP A 157 0
SHEET 2 AA4 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 AA4 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 AA4 4 GLN A 183 ARG A 184 -1 O GLN A 183 N VAL A 174
SHEET 1 AA5 3 ILE A 194 ASN A 196 0
SHEET 2 AA5 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA6 4 ILE A 194 ASN A 196 0
SHEET 2 AA6 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA6 4 THR A 265 ASP A 272 -1 O THR A 265 N ASN A 229
SHEET 4 AA6 4 SER A 284 ILE A 287 -1 O ILE A 287 N PHE A 268
SHEET 1 AA7 2 LEU A 235 PHE A 240 0
SHEET 2 AA7 2 LYS A 250 PRO A 255 -1 O ILE A 254 N ILE A 236
SHEET 1 AA8 4 HIS A 298 THR A 307 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AA8 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 AA8 4 TRP A 337 ILE A 338 -1 O ILE A 338 N ASP A 329
SHEET 1 AA9 4 HIS A 298 THR A 307 0
SHEET 2 AA9 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AA9 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 AA9 4 GLN A 344 ILE A 348 -1 O GLU A 347 N SER A 323
SHEET 1 AB1 4 HIS A 363 PHE A 364 0
SHEET 2 AB1 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AB1 4 LYS A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 AB1 4 CYS A 394 PHE A 396 -1 O THR A 395 N HIS A 386
SHEET 1 AB2 4 VAL A 404 LEU A 410 0
SHEET 2 AB2 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 AB2 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB2 4 ASP A 438 CYS A 444 -1 O THR A 443 N ARG A 433
SHEET 1 AB3 4 TYR A 457 PHE A 461 0
SHEET 2 AB3 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 AB3 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 AB3 4 GLU A 490 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB4 8 SER A 511 LEU A 519 0
SHEET 2 AB4 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 AB4 8 ILE A 574 ASP A 579 -1 O VAL A 575 N ILE A 529
SHEET 4 AB4 8 TYR A 540 GLU A 545 1 N LEU A 543 O ILE A 574
SHEET 5 AB4 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB4 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 AB4 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB5 2 ARG B 41 THR B 42 0
SHEET 2 AB5 2 VAL B 507 GLN B 508 1 O GLN B 508 N ARG B 41
SHEET 1 AB6 4 GLN B 61 TRP B 62 0
SHEET 2 AB6 4 GLU B 67 GLN B 72 -1 O LEU B 69 N GLN B 61
SHEET 3 AB6 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 AB6 4 SER B 86 LEU B 90 -1 O SER B 87 N LEU B 78
SHEET 1 AB7 4 ASP B 104 VAL B 107 0
SHEET 2 AB7 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 AB7 4 TYR B 128 ASP B 136 -1 O ASP B 133 N PHE B 116
SHEET 4 AB7 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 AB8 4 TRP B 154 TRP B 157 0
SHEET 2 AB8 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 AB8 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 AB8 4 GLN B 183 ARG B 184 -1 O GLN B 183 N VAL B 174
SHEET 1 AB9 3 ILE B 194 ASN B 196 0
SHEET 2 AB9 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB9 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AC1 4 ILE B 194 ASN B 196 0
SHEET 2 AC1 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AC1 4 THR B 265 ASP B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 AC1 4 SER B 284 ILE B 287 -1 O ILE B 287 N PHE B 268
SHEET 1 AC2 2 LEU B 235 PHE B 240 0
SHEET 2 AC2 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AC3 4 HIS B 298 THR B 307 0
SHEET 2 AC3 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 AC3 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 AC3 4 TRP B 337 ILE B 338 -1 O ILE B 338 N ASP B 329
SHEET 1 AC4 4 HIS B 298 THR B 307 0
SHEET 2 AC4 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 AC4 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 AC4 4 GLN B 344 ILE B 348 -1 O GLU B 347 N SER B 323
SHEET 1 AC5 4 HIS B 363 PHE B 364 0
SHEET 2 AC5 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC5 4 LYS B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 AC5 4 CYS B 394 PHE B 396 -1 O THR B 395 N HIS B 386
SHEET 1 AC6 4 VAL B 404 LEU B 410 0
SHEET 2 AC6 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 AC6 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC6 4 ASP B 438 CYS B 444 -1 O THR B 443 N ARG B 433
SHEET 1 AC7 4 CYS B 454 PHE B 461 0
SHEET 2 AC7 4 TYR B 467 PRO B 475 -1 O ARG B 471 N SER B 458
SHEET 3 AC7 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 AC7 4 GLU B 490 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AC8 8 SER B 511 LEU B 519 0
SHEET 2 AC8 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 AC8 8 ILE B 574 ASP B 579 -1 O VAL B 575 N ILE B 529
SHEET 4 AC8 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 AC8 8 VAL B 619 TRP B 629 1 O ALA B 625 N ILE B 544
SHEET 6 AC8 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 AC8 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 AC8 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AC9 2 ARG C 41 THR C 42 0
SHEET 2 AC9 2 VAL C 507 GLN C 508 1 O GLN C 508 N ARG C 41
SHEET 1 AD1 4 GLN C 61 TRP C 62 0
SHEET 2 AD1 4 GLU C 67 GLN C 72 -1 O LEU C 69 N GLN C 61
SHEET 3 AD1 4 ASN C 75 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 4 AD1 4 SER C 86 LEU C 90 -1 O SER C 87 N LEU C 78
SHEET 1 AD2 4 ASP C 104 VAL C 107 0
SHEET 2 AD2 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AD2 4 TYR C 128 ASP C 136 -1 O TYR C 135 N ILE C 114
SHEET 4 AD2 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AD3 4 THR C 152 TRP C 157 0
SHEET 2 AD3 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AD3 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AD3 4 GLN C 183 ARG C 184 -1 O GLN C 183 N VAL C 174
SHEET 1 AD4 3 ILE C 194 ASN C 196 0
SHEET 2 AD4 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD4 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AD5 4 ILE C 194 ASN C 196 0
SHEET 2 AD5 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD5 4 THR C 265 ASP C 272 -1 O PHE C 269 N TYR C 225
SHEET 4 AD5 4 SER C 284 ILE C 287 -1 O ILE C 287 N PHE C 268
SHEET 1 AD6 2 LEU C 235 PHE C 240 0
SHEET 2 AD6 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AD7 4 HIS C 298 THR C 307 0
SHEET 2 AD7 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AD7 4 TYR C 322 TYR C 330 -1 O ILE C 324 N TRP C 315
SHEET 4 AD7 4 TRP C 337 ILE C 338 -1 O ILE C 338 N ASP C 329
SHEET 1 AD8 4 HIS C 298 THR C 307 0
SHEET 2 AD8 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AD8 4 TYR C 322 TYR C 330 -1 O ILE C 324 N TRP C 315
SHEET 4 AD8 4 GLN C 344 ILE C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AD9 4 HIS C 363 PHE C 364 0
SHEET 2 AD9 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AD9 4 LYS C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AD9 4 CYS C 394 PHE C 396 -1 O THR C 395 N HIS C 386
SHEET 1 AE1 4 VAL C 404 LEU C 410 0
SHEET 2 AE1 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AE1 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AE1 4 ASP C 438 CYS C 444 -1 O THR C 443 N ARG C 433
SHEET 1 AE2 4 CYS C 454 PHE C 461 0
SHEET 2 AE2 4 TYR C 467 PRO C 475 -1 O ARG C 471 N SER C 458
SHEET 3 AE2 4 LEU C 479 SER C 484 -1 O HIS C 483 N TYR C 468
SHEET 4 AE2 4 GLU C 490 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AE3 8 SER C 511 LEU C 519 0
SHEET 2 AE3 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AE3 8 ILE C 574 ASP C 579 -1 O VAL C 575 N ILE C 529
SHEET 4 AE3 8 TYR C 540 VAL C 546 1 N LEU C 543 O ILE C 574
SHEET 5 AE3 8 VAL C 619 TRP C 629 1 O TRP C 627 N ILE C 544
SHEET 6 AE3 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AE3 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 652
SHEET 8 AE3 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AE4 2 ARG D 41 THR D 42 0
SHEET 2 AE4 2 VAL D 507 GLN D 508 1 O GLN D 508 N ARG D 41
SHEET 1 AE5 4 GLN D 61 TRP D 62 0
SHEET 2 AE5 4 GLU D 67 GLN D 72 -1 O LEU D 69 N GLN D 61
SHEET 3 AE5 4 ASN D 75 ASN D 80 -1 O LEU D 77 N TYR D 70
SHEET 4 AE5 4 SER D 86 LEU D 90 -1 O SER D 87 N LEU D 78
SHEET 1 AE6 4 ASP D 104 VAL D 107 0
SHEET 2 AE6 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AE6 4 TYR D 128 ASP D 136 -1 O TYR D 135 N ILE D 114
SHEET 4 AE6 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AE7 4 TRP D 154 TRP D 157 0
SHEET 2 AE7 4 LEU D 164 TRP D 168 -1 O VAL D 167 N TRP D 154
SHEET 3 AE7 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AE7 4 GLN D 183 ARG D 184 -1 O GLN D 183 N VAL D 174
SHEET 1 AE8 3 ILE D 194 ASN D 196 0
SHEET 2 AE8 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AE8 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AE9 4 ILE D 194 ASN D 196 0
SHEET 2 AE9 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AE9 4 THR D 265 ASP D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AE9 4 SER D 284 ILE D 287 -1 O ILE D 287 N PHE D 268
SHEET 1 AF1 2 LEU D 235 PHE D 240 0
SHEET 2 AF1 2 LYS D 250 PRO D 255 -1 O ILE D 254 N ILE D 236
SHEET 1 AF2 4 HIS D 298 THR D 307 0
SHEET 2 AF2 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AF2 4 TYR D 322 TYR D 330 -1 O ASP D 326 N LEU D 313
SHEET 4 AF2 4 TRP D 337 ILE D 338 -1 O ILE D 338 N ASP D 329
SHEET 1 AF3 4 HIS D 298 THR D 307 0
SHEET 2 AF3 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AF3 4 TYR D 322 TYR D 330 -1 O ASP D 326 N LEU D 313
SHEET 4 AF3 4 GLN D 344 ILE D 348 -1 O GLU D 347 N SER D 323
SHEET 1 AF4 4 HIS D 363 PHE D 364 0
SHEET 2 AF4 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AF4 4 LYS D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AF4 4 CYS D 394 PHE D 396 -1 O THR D 395 N HIS D 386
SHEET 1 AF5 4 VAL D 404 LEU D 410 0
SHEET 2 AF5 4 TYR D 414 SER D 419 -1 O ILE D 418 N ILE D 405
SHEET 3 AF5 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AF5 4 ASP D 438 CYS D 444 -1 O THR D 443 N ARG D 433
SHEET 1 AF6 4 CYS D 454 PHE D 461 0
SHEET 2 AF6 4 TYR D 467 PRO D 475 -1 O ARG D 471 N SER D 458
SHEET 3 AF6 4 LEU D 479 SER D 484 -1 O HIS D 483 N TYR D 468
SHEET 4 AF6 4 GLU D 490 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AF7 8 SER D 511 LEU D 519 0
SHEET 2 AF7 8 THR D 522 LEU D 530 -1 O LEU D 530 N SER D 511
SHEET 3 AF7 8 ILE D 574 ASP D 579 -1 O VAL D 575 N ILE D 529
SHEET 4 AF7 8 TYR D 540 VAL D 546 1 N GLU D 545 O ALA D 576
SHEET 5 AF7 8 VAL D 619 TRP D 629 1 O TRP D 627 N ILE D 544
SHEET 6 AF7 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AF7 8 GLU D 699 GLY D 705 1 O ILE D 703 N ALA D 652
SHEET 8 AF7 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 2 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 3 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 4 CYS A 649 CYS A 762 1555 1555 2.04
SSBOND 5 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 6 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 7 CYS B 454 CYS B 472 1555 1555 2.03
SSBOND 8 CYS B 649 CYS B 762 1555 1555 2.04
SSBOND 9 CYS C 385 CYS C 394 1555 1555 2.05
SSBOND 10 CYS C 444 CYS C 447 1555 1555 2.03
SSBOND 11 CYS C 454 CYS C 472 1555 1555 2.04
SSBOND 12 CYS C 649 CYS C 762 1555 1555 2.03
SSBOND 13 CYS D 385 CYS D 394 1555 1555 2.05
SSBOND 14 CYS D 444 CYS D 447 1555 1555 2.03
SSBOND 15 CYS D 454 CYS D 472 1555 1555 2.04
SSBOND 16 CYS D 649 CYS D 762 1555 1555 2.04
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.43
LINK ND2 ASN A 92 C1 NAG A 802 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG A 804 1555 1555 1.43
LINK ND2 ASN A 279 C1 NAG A 805 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG A 806 1555 1555 1.43
LINK ND2 ASN A 685 C1 NAG A 807 1555 1555 1.43
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.43
LINK ND2 ASN B 92 C1 NAG B 802 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG B 804 1555 1555 1.44
LINK ND2 ASN B 279 C1 NAG B 805 1555 1555 1.44
LINK ND2 ASN B 321 C1 NAG B 806 1555 1555 1.44
LINK ND2 ASN B 685 C1 NAG B 807 1555 1555 1.43
LINK ND2 ASN C 85 C1 NAG C 801 1555 1555 1.43
LINK ND2 ASN C 92 C1 NAG C 802 1555 1555 1.43
LINK ND2 ASN C 229 C1 NAG C 803 1555 1555 1.43
LINK ND2 ASN C 279 C1 NAG C 804 1555 1555 1.43
LINK ND2 ASN C 321 C1 NAG C 805 1555 1555 1.44
LINK ND2 ASN C 685 C1 NAG C 806 1555 1555 1.43
LINK ND2 ASN D 85 C1 NAG D 801 1555 1555 1.43
LINK ND2 ASN D 92 C1 NAG D 803 1555 1555 1.43
LINK ND2 ASN D 229 C1 NAG D 805 1555 1555 1.43
LINK ND2 ASN D 279 C1 NAG D 806 1555 1555 1.44
LINK ND2 ASN D 321 C1 NAG D 808 1555 1555 1.43
LINK ND2 ASN D 685 C1 NAG D 810 1555 1555 1.43
LINK C1 NAG A 803 O4 NAG A 804 1555 1555 1.42
LINK O4 NAG A 807 C1 NAG A 808 1555 1555 1.43
LINK O4 NAG B 802 C1 NAG B 803 1555 1555 1.44
LINK O4 NAG B 807 C1 NAG B 808 1555 1555 1.43
LINK O4 NAG C 806 C1 NAG C 807 1555 1555 1.43
LINK C1 NAG D 802 O4 NAG D 803 1555 1555 1.43
LINK C1 NAG D 804 O4 NAG D 805 1555 1555 1.42
LINK C1 NAG D 807 O4 NAG D 808 1555 1555 1.44
LINK C1 NAG D 809 O4 NAG D 810 1555 1555 1.43
CISPEP 1 GLY A 474 PRO A 475 0 3.58
CISPEP 2 GLY B 474 PRO B 475 0 3.22
CISPEP 3 GLY C 474 PRO C 475 0 2.86
CISPEP 4 GLY D 474 PRO D 475 0 2.65
SITE 1 AC1 12 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC1 12 TRP A 629 SER A 630 TYR A 631 TYR A 662
SITE 3 AC1 12 TYR A 666 ASN A 710 VAL A 711 HIS A 740
SITE 1 AC2 8 ALA A 360 GLU A 361 HIS A 363 ILE A 374
SITE 2 AC2 8 GLY A 406 ILE A 407 HOH A 937 HOH A1008
SITE 1 AC3 6 TRP A 187 ALA A 280 SER A 281 VAL A 282
SITE 2 AC3 6 SER C 284 6Z8 C 810
SITE 1 AC4 12 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 AC4 12 TRP B 629 SER B 630 TYR B 631 TYR B 662
SITE 3 AC4 12 TYR B 666 ASN B 710 VAL B 711 HIS B 740
SITE 1 AC5 7 GLU B 361 HIS B 363 ILE B 374 GLY B 406
SITE 2 AC5 7 ILE B 407 HOH B 922 HOH B 930
SITE 1 AC6 8 TRP B 187 ALA B 280 SER B 281 VAL B 282
SITE 2 AC6 8 LYS D 267 PHE D 269 SER D 284 6Z8 D 813
SITE 1 AC7 12 ARG C 125 GLU C 205 GLU C 206 TYR C 547
SITE 2 AC7 12 TRP C 629 SER C 630 TYR C 631 TYR C 662
SITE 3 AC7 12 TYR C 666 ASN C 710 VAL C 711 HIS C 740
SITE 1 AC8 8 GLU C 361 HIS C 363 ILE C 374 GLY C 406
SITE 2 AC8 8 ILE C 407 HOH C 926 HOH C 958 HOH C1038
SITE 1 AC9 8 LYS A 267 PHE A 269 SER A 284 6Z8 A 811
SITE 2 AC9 8 TRP C 187 ALA C 280 SER C 281 VAL C 282
SITE 1 AD1 13 ARG D 125 GLU D 205 GLU D 206 TYR D 547
SITE 2 AD1 13 TRP D 629 SER D 630 TYR D 631 TYR D 662
SITE 3 AD1 13 TYR D 666 ASN D 710 VAL D 711 HIS D 740
SITE 4 AD1 13 HOH D 910
SITE 1 AD2 5 GLU D 361 HIS D 363 ILE D 374 GLY D 406
SITE 2 AD2 5 ILE D 407
SITE 1 AD3 7 PHE B 269 SER B 284 6Z8 B 811 TRP D 187
SITE 2 AD3 7 ALA D 280 SER D 281 VAL D 282
SITE 1 AD4 1 ASN A 85
SITE 1 AD5 6 GLU A 73 ASN A 75 ASN A 92 HIS A 520
SITE 2 AD5 6 GLY A 521 HOH A1041
SITE 1 AD6 7 ILE A 194 GLN A 227 ASN A 229 THR A 231
SITE 2 AD6 7 GLU A 232 LYS A 267 HOH A 988
SITE 1 AD7 3 ASN A 279 HOH A 977 TYR C 285
SITE 1 AD8 6 THR A 144 ALA A 319 ASN A 321 SER A 349
SITE 2 AD8 6 ARG A 596 ASP A 678
SITE 1 AD9 8 TYR A 100 ARG A 597 GLY A 599 THR A 600
SITE 2 AD9 8 TYR A 682 ASN A 685 ARG A 691 HOH A 950
SITE 1 AE1 2 LEU B 78 ASN B 85
SITE 1 AE2 8 GLU B 73 ASN B 74 ASN B 75 ASN B 92
SITE 2 AE2 8 ILE B 348 THR B 350 NAG B 806 HOH B1014
SITE 1 AE3 7 GLN B 227 ASN B 229 THR B 231 GLU B 232
SITE 2 AE3 7 LYS B 267 HOH B 988 HOH B1060
SITE 1 AE4 2 ASN B 279 VAL D 288
SITE 1 AE5 5 ASN B 321 SER B 349 THR B 350 NAG B 802
SITE 2 AE5 5 HOH B 937
SITE 1 AE6 8 ARG B 597 GLY B 599 THR B 600 TYR B 682
SITE 2 AE6 8 ASN B 685 ARG B 691 HOH B 929 HOH B1036
SITE 1 AE7 5 HOH B1064 LEU C 78 ASN C 85 SER C 87
SITE 2 AE7 5 HOH C 947
SITE 1 AE8 4 LYS B 423 GLU C 73 ASN C 75 ASN C 92
SITE 1 AE9 8 THR C 188 ILE C 194 ASN C 229 THR C 231
SITE 2 AE9 8 GLU C 232 LYS C 267 HOH C 951 HOH C 993
SITE 1 AF1 4 VAL A 288 ASN C 279 HOH C 949 HOH C 956
SITE 1 AF2 1 ASN C 321
SITE 1 AF3 9 ARG C 597 GLY C 599 THR C 600 TYR C 682
SITE 2 AF3 9 ASN C 685 ARG C 691 HOH C 920 HOH C 938
SITE 3 AF3 9 HOH C 965
SITE 1 AF4 2 ASN D 85 SER D 87
SITE 1 AF5 5 GLU D 73 ASN D 75 ASN D 92 THR D 350
SITE 2 AF5 5 HOH D 998
SITE 1 AF6 6 ILE D 194 GLN D 227 ASN D 229 THR D 231
SITE 2 AF6 6 GLU D 232 LYS D 267
SITE 1 AF7 4 VAL B 288 PRO D 278 ASN D 279 HOH D1006
SITE 1 AF8 6 ASN D 321 SER D 349 ARG D 596 GLU D 677
SITE 2 AF8 6 ASP D 678 HOH D 933
SITE 1 AF9 10 ARG D 597 GLY D 599 THR D 600 GLU D 604
SITE 2 AF9 10 TYR D 682 ASN D 685 ARG D 691 HOH D 912
SITE 3 AF9 10 HOH D 917 HOH D 982
CRYST1 61.900 117.680 133.120 112.70 94.60 91.20 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 0.016155 0.000338 0.001554 0.00000
SCALE2 0.000000 0.008499 0.003588 0.00000
SCALE3 0.000000 0.000000 0.008180 0.00000
TER 5961 PRO A 766
TER 11922 PRO B 766
TER 17883 PRO C 766
TER 23844 PRO D 766
MASTER 783 0 45 80 204 0 70 625567 4 762 236
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