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HEADER HYDROLASE 14-MAY-10 3N0T
TITLE HUMAN DIPEPTIDIL PEPTIDASE DPP7 COMPLEXED WITH INHIBITOR GSK237826A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: PEPTIDASE DOMAIN (UNP RESIDUES 28-492);
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE II, DPP II, DIPEPTIDYL AMINOPEPTIDASE
COMPND 6 II, QUIESCENT CELL PROLINE DIPEPTIDASE, DIPEPTIDYL PEPTIDASE 7;
COMPND 7 EC: 3.4.14.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP2, DPP7, QPP;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 AMINOPEPTIDASE, CLEAVAGE ON PAIR OF BASIC RESIDUES, CYTOPLASMIC
KEYWDS 3 VESICLE, GLYCOPROTEIN, HYDROLASE, LYSOSOME, PROTEASE, SERINE
KEYWDS 4 PROTEASE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DOBROVETSKY,G.KHUTORESKAYA,A.SEITOVA,L.CROMBET,D.COSSAR,S.PAGANNON,
AUTHOR 2 C.H.ARROWSMITH,C.BOUNTRA,J.WEIGELT,A.M.EDWARDS,A.HASSELL,L.SHEWCHUK,
AUTHOR 3 C.HAFFNER,A.BOCHKAREV,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 1 21-JUL-10 3N0T 0
JRNL AUTH E.DOBROVETSKY,G.KHUTORESKAYA,A.SEITOVA,L.CROMBET,D.COSSAR,
JRNL AUTH 2 S.PAGANNON,C.H.ARROWSMITH,C.BOUNTRA,A.M.EDWARDS,A.HASSELL,
JRNL AUTH 3 L.SHEWCHUK,C.HAFFNER,A.BOCHKAREV
JRNL TITL HUMAN DIPEPTIDYL PEPTIDASE DPP7
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 91963
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4609
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.51
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6674
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2530
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6324
REMARK 3 BIN R VALUE (WORKING SET) : 0.2498
REMARK 3 BIN FREE R VALUE : 0.3102
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.24
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 350
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13833
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 248
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.90670
REMARK 3 B22 (A**2) : -2.65200
REMARK 3 B33 (A**2) : 0.74530
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.93630
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.899
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.862
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 14293 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 19476 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4565 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 313 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2169 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 14241 ; 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 : 1884 ; 5.000 ; NULL
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 : 16779 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.75
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.74
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: A 1001 A 1001
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4764 0.2164 14.7866
REMARK 3 T TENSOR
REMARK 3 T11: -0.0604 T22: -0.1058
REMARK 3 T33: -0.0107 T12: -0.0072
REMARK 3 T13: -0.0841 T23: -0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 0.3572 L22: 0.7273
REMARK 3 L33: 0.9603 L12: -0.1996
REMARK 3 L13: 0.0574 L23: -0.3600
REMARK 3 S TENSOR
REMARK 3 S11: -0.0603 S12: -0.0100 S13: 0.0137
REMARK 3 S21: 0.0414 S22: 0.0153 S23: -0.0971
REMARK 3 S31: 0.0403 S32: -0.0207 S33: 0.0450
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: B 1001 B 1001
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3776 34.0102 -14.3854
REMARK 3 T TENSOR
REMARK 3 T11: -0.0325 T22: -0.1183
REMARK 3 T33: -0.0121 T12: 0.0042
REMARK 3 T13: -0.0698 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 0.4740 L22: 0.5665
REMARK 3 L33: 0.7845 L12: 0.1860
REMARK 3 L13: 0.0014 L23: -0.3300
REMARK 3 S TENSOR
REMARK 3 S11: -0.0609 S12: 0.0103 S13: -0.0162
REMARK 3 S21: -0.0199 S22: 0.0430 S23: -0.0549
REMARK 3 S31: -0.0320 S32: -0.0257 S33: 0.0179
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: C 1001 C 1001
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8609 20.4232 65.3980
REMARK 3 T TENSOR
REMARK 3 T11: 0.0183 T22: -0.1164
REMARK 3 T33: -0.1097 T12: -0.0684
REMARK 3 T13: -0.0962 T23: -0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 0.8979 L22: 0.8973
REMARK 3 L33: 1.0921 L12: -0.4025
REMARK 3 L13: 0.6301 L23: -0.5916
REMARK 3 S TENSOR
REMARK 3 S11: 0.0142 S12: -0.1446 S13: 0.1470
REMARK 3 S21: -0.1327 S22: 0.0363 S23: -0.0213
REMARK 3 S31: 0.0235 S32: -0.0974 S33: -0.0505
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: D 1001 D 1001
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4180 -13.4173 84.9288
REMARK 3 T TENSOR
REMARK 3 T11: 0.0856 T22: -0.1147
REMARK 3 T33: -0.1731 T12: -0.0755
REMARK 3 T13: -0.0837 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 1.1310 L22: 1.0245
REMARK 3 L33: 0.6727 L12: -0.5964
REMARK 3 L13: 0.5660 L23: -0.2447
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: -0.0878 S13: -0.0527
REMARK 3 S21: -0.1221 S22: 0.0689 S23: -0.0313
REMARK 3 S31: 0.2604 S32: -0.0905 S33: -0.1014
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3N0T COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-10.
REMARK 100 THE RCSB ID CODE IS RCSB059236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92014
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 122.213
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.79300
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3JYH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.2M SODIUM
REMARK 280 ACETATE, 0.1M HEPES, 5% MPD, PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 300K
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,Y+1/2,-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 65.25000
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/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: 4250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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: 4180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 GLY A 24
REMARK 465 ALA A 25
REMARK 465 MET A 26
REMARK 465 ASP A 27
REMARK 465 GLN A 480
REMARK 465 GLN A 481
REMARK 465 PRO A 482
REMARK 465 ALA A 483
REMARK 465 LEU A 484
REMARK 465 ARG A 485
REMARK 465 GLY A 486
REMARK 465 GLY A 487
REMARK 465 PRO A 488
REMARK 465 ARG A 489
REMARK 465 LEU A 490
REMARK 465 SER A 491
REMARK 465 LEU A 492
REMARK 465 GLY B 24
REMARK 465 ALA B 25
REMARK 465 MET B 26
REMARK 465 ASP B 27
REMARK 465 GLN B 480
REMARK 465 GLN B 481
REMARK 465 PRO B 482
REMARK 465 ALA B 483
REMARK 465 LEU B 484
REMARK 465 ARG B 485
REMARK 465 GLY B 486
REMARK 465 GLY B 487
REMARK 465 PRO B 488
REMARK 465 ARG B 489
REMARK 465 LEU B 490
REMARK 465 SER B 491
REMARK 465 LEU B 492
REMARK 465 GLY C 24
REMARK 465 ALA C 25
REMARK 465 MET C 26
REMARK 465 ASP C 27
REMARK 465 GLU C 479
REMARK 465 GLN C 480
REMARK 465 GLN C 481
REMARK 465 PRO C 482
REMARK 465 ALA C 483
REMARK 465 LEU C 484
REMARK 465 ARG C 485
REMARK 465 GLY C 486
REMARK 465 GLY C 487
REMARK 465 PRO C 488
REMARK 465 ARG C 489
REMARK 465 LEU C 490
REMARK 465 SER C 491
REMARK 465 LEU C 492
REMARK 465 GLY D 24
REMARK 465 ALA D 25
REMARK 465 MET D 26
REMARK 465 ASP D 27
REMARK 465 ASP D 28
REMARK 465 ARG D 478
REMARK 465 GLU D 479
REMARK 465 GLN D 480
REMARK 465 GLN D 481
REMARK 465 PRO D 482
REMARK 465 ALA D 483
REMARK 465 LEU D 484
REMARK 465 ARG D 485
REMARK 465 GLY D 486
REMARK 465 GLY D 487
REMARK 465 PRO D 488
REMARK 465 ARG D 489
REMARK 465 LEU D 490
REMARK 465 SER D 491
REMARK 465 LEU D 492
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 34 NH1 NH2
REMARK 470 ARG A 47 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 62 CZ NH1 NH2
REMARK 470 ARG A 66 CZ NH1 NH2
REMARK 470 GLU A 68 CG CD OE1 OE2
REMARK 470 ALA A 89 CB
REMARK 470 GLN A 119 CG CD OE1 NE2
REMARK 470 ASP A 208 CG OD1 OD2
REMARK 470 GLN A 212 CG CD OE1 NE2
REMARK 470 LYS A 215 CE NZ
REMARK 470 GLU A 252 CG CD OE1 OE2
REMARK 470 LYS A 253 CG CD CE NZ
REMARK 470 ARG A 380 CZ NH1 NH2
REMARK 470 ARG A 427 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 471 CD OE1 OE2
REMARK 470 LYS A 474 CG CD CE NZ
REMARK 470 ARG A 478 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 479 CG CD OE1 OE2
REMARK 470 ASP B 28 CG OD1 OD2
REMARK 470 GLN B 32 CD OE1 NE2
REMARK 470 ARG B 47 CZ NH1 NH2
REMARK 470 ARG B 62 NE CZ NH1 NH2
REMARK 470 ARG B 66 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 68 CG CD OE1 OE2
REMARK 470 ALA B 89 CB
REMARK 470 GLN B 119 CG CD OE1 NE2
REMARK 470 LYS B 215 CE NZ
REMARK 470 ARG B 221 CZ NH1 NH2
REMARK 470 GLN B 233 CG CD OE1 NE2
REMARK 470 LYS B 253 NZ
REMARK 470 ARG B 327 NE CZ NH1 NH2
REMARK 470 GLU B 376 CG CD OE1 OE2
REMARK 470 ARG B 380 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 460 CD OE1 OE2
REMARK 470 LYS B 463 CD CE NZ
REMARK 470 GLU B 471 CG CD OE1 OE2
REMARK 470 LYS B 474 CG CD CE NZ
REMARK 470 ARG B 478 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 479 CG CD OE1 OE2
REMARK 470 ASP C 28 CG OD1 OD2
REMARK 470 ARG C 47 CZ NH1 NH2
REMARK 470 ARG C 62 CD NE CZ NH1 NH2
REMARK 470 ARG C 66 NE CZ NH1 NH2
REMARK 470 ALA C 89 CB
REMARK 470 GLU C 97 CG CD OE1 OE2
REMARK 470 ARG C 98 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 119 CG CD OE1 NE2
REMARK 470 GLU C 127 CG CD OE1 OE2
REMARK 470 ASP C 153 CG OD1 OD2
REMARK 470 ASP C 197 CG OD1 OD2
REMARK 470 ASN C 199 CG OD1 ND2
REMARK 470 LYS C 215 CG CD CE NZ
REMARK 470 GLN C 218 CG CD OE1 NE2
REMARK 470 LEU C 232 CG CD1 CD2
REMARK 470 GLU C 252 CG CD OE1 OE2
REMARK 470 LYS C 253 CE NZ
REMARK 470 LYS C 290 CD CE NZ
REMARK 470 ARG C 327 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 427 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 471 CD OE1 OE2
REMARK 470 LYS C 474 CG CD CE NZ
REMARK 470 ARG C 477 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 478 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 47 NE CZ NH1 NH2
REMARK 470 ARG D 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 66 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 68 CG CD OE1 OE2
REMARK 470 ALA D 89 CB
REMARK 470 GLU D 97 CG CD OE1 OE2
REMARK 470 ARG D 98 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 112 CD CE NZ
REMARK 470 GLN D 119 CG CD OE1 NE2
REMARK 470 ASP D 153 CG OD1 OD2
REMARK 470 LYS D 215 CE NZ
REMARK 470 GLN D 218 CG CD OE1 NE2
REMARK 470 GLU D 222 CG CD OE1 OE2
REMARK 470 ARG D 225 CD NE CZ NH1 NH2
REMARK 470 LEU D 232 CG CD1 CD2
REMARK 470 GLU D 252 CG CD OE1 OE2
REMARK 470 LYS D 253 CG CD CE NZ
REMARK 470 ARG D 327 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 376 CG CD OE1 OE2
REMARK 470 ARG D 380 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 384 CG OD1 OD2
REMARK 470 LYS D 463 CG CD CE NZ
REMARK 470 GLU D 471 CG CD OE1 OE2
REMARK 470 LYS D 474 CE NZ
REMARK 470 ARG D 477 CG CD NE CZ NH1 NH2
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 GLU A 68 -24.51 -148.12
REMARK 500 ASN A 77 -151.76 -105.77
REMARK 500 GLU A 78 54.72 -67.36
REMARK 500 TYR A 109 -4.21 83.29
REMARK 500 ALA A 151 44.04 -143.57
REMARK 500 SER A 162 -126.07 61.98
REMARK 500 ALA A 235 53.05 -90.52
REMARK 500 SER A 250 -30.82 -149.48
REMARK 500 PHE A 280 -72.30 -90.40
REMARK 500 THR A 353 -64.56 -122.02
REMARK 500 SER A 430 -178.22 -173.65
REMARK 500 ALA A 442 -137.27 -102.34
REMARK 500 HIS A 444 53.45 35.33
REMARK 500 ASN B 77 -155.54 -101.18
REMARK 500 GLU B 78 48.23 -65.95
REMARK 500 TYR B 109 6.68 80.15
REMARK 500 SER B 162 -133.53 65.58
REMARK 500 SER B 250 -31.64 -149.99
REMARK 500 PHE B 280 -69.85 -93.02
REMARK 500 THR B 353 -69.73 -120.46
REMARK 500 LEU B 357 59.58 -117.18
REMARK 500 THR B 358 46.76 -77.24
REMARK 500 ASP B 370 98.04 -69.15
REMARK 500 TRP B 400 -4.63 62.81
REMARK 500 ALA B 442 -132.09 -97.05
REMARK 500 GLU C 46 -60.53 -94.83
REMARK 500 ARG C 66 131.33 -38.14
REMARK 500 GLU C 68 -67.73 -149.85
REMARK 500 ASN C 77 -152.15 -108.35
REMARK 500 GLU C 78 44.65 -70.04
REMARK 500 SER C 162 -127.56 62.67
REMARK 500 SER C 250 -36.24 -153.11
REMARK 500 PHE C 280 -71.41 -97.15
REMARK 500 ASN C 315 41.19 -143.06
REMARK 500 THR C 353 -67.57 -125.58
REMARK 500 LEU C 357 56.85 -114.60
REMARK 500 VAL C 364 -55.42 -131.88
REMARK 500 TRP C 400 -10.05 64.71
REMARK 500 ALA C 442 -134.46 -93.60
REMARK 500 LYS D 51 125.96 -7.42
REMARK 500 ARG D 66 105.48 -51.27
REMARK 500 ASN D 77 -148.28 -115.50
REMARK 500 GLU D 78 45.88 -67.34
REMARK 500 SER D 88 60.09 -114.95
REMARK 500 TYR D 109 -8.26 72.86
REMARK 500 HIS D 125 -1.62 -143.24
REMARK 500 SER D 162 -128.61 63.40
REMARK 500 SER D 250 -38.43 -133.89
REMARK 500 MET D 272 35.75 -96.86
REMARK 500 PHE D 280 -75.17 -100.43
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 78 23.9 L L OUTSIDE RANGE
REMARK 500 TRP A 394 24.9 L L OUTSIDE RANGE
REMARK 500 PHE A 399 24.7 L L OUTSIDE RANGE
REMARK 500 HIS A 444 24.9 L L OUTSIDE RANGE
REMARK 500 GLU B 78 24.7 L L OUTSIDE RANGE
REMARK 500 GLU B 127 24.5 L L OUTSIDE RANGE
REMARK 500 PHE B 399 23.5 L L OUTSIDE RANGE
REMARK 500 TRP B 400 24.3 L L OUTSIDE RANGE
REMARK 500 HIS B 444 24.4 L L OUTSIDE RANGE
REMARK 500 ASN C 77 23.7 L L OUTSIDE RANGE
REMARK 500 GLU C 78 24.1 L L OUTSIDE RANGE
REMARK 500 VAL C 189 24.7 L L OUTSIDE RANGE
REMARK 500 TRP D 394 24.3 L L OUTSIDE RANGE
REMARK 500 PHE D 399 24.5 L L OUTSIDE RANGE
REMARK 500 TRP D 400 23.7 L L OUTSIDE RANGE
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 D 506 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH A 529 DISTANCE = 7.99 ANGSTROMS
REMARK 525 HOH A 573 DISTANCE = 5.25 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OPY A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OPY B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OPY C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OPY D 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JYH RELATED DB: PDB
REMARK 900 HUMAN DPP7 IN APO FORM
DBREF 3N0T A 28 492 UNP Q9UHL4 DPP2_HUMAN 28 492
DBREF 3N0T B 28 492 UNP Q9UHL4 DPP2_HUMAN 28 492
DBREF 3N0T C 28 492 UNP Q9UHL4 DPP2_HUMAN 28 492
DBREF 3N0T D 28 492 UNP Q9UHL4 DPP2_HUMAN 28 492
SEQADV 3N0T GLY A 24 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T ALA A 25 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T MET A 26 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T ASP A 27 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T GLY B 24 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T ALA B 25 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T MET B 26 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T ASP B 27 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T GLY C 24 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T ALA C 25 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T MET C 26 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T ASP C 27 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T GLY D 24 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T ALA D 25 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T MET D 26 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3N0T ASP D 27 UNP Q9UHL4 EXPRESSION TAG
SEQRES 1 A 469 GLY ALA MET ASP ASP PRO GLY PHE GLN GLU ARG PHE PHE
SEQRES 2 A 469 GLN GLN ARG LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY
SEQRES 3 A 469 ASN LYS THR PHE PRO GLN ARG PHE LEU VAL SER ASP ARG
SEQRES 4 A 469 PHE TRP VAL ARG GLY GLU GLY PRO ILE PHE PHE TYR THR
SEQRES 5 A 469 GLY ASN GLU GLY ASP VAL TRP ALA PHE ALA ASN ASN SER
SEQRES 6 A 469 ALA PHE VAL ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU
SEQRES 7 A 469 LEU VAL PHE ALA GLU HIS ARG TYR TYR GLY LYS SER LEU
SEQRES 8 A 469 PRO PHE GLY ALA GLN SER THR GLN ARG GLY HIS THR GLU
SEQRES 9 A 469 LEU LEU THR VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU
SEQRES 10 A 469 LEU LEU ARG ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP
SEQRES 11 A 469 ALA PRO ALA ILE ALA PHE GLY GLY SER TYR GLY GLY MET
SEQRES 12 A 469 LEU SER ALA TYR LEU ARG MET LYS TYR PRO HIS LEU VAL
SEQRES 13 A 469 ALA GLY ALA LEU ALA ALA SER ALA PRO VAL LEU ALA VAL
SEQRES 14 A 469 ALA GLY LEU GLY ASP SER ASN GLN PHE PHE ARG ASP VAL
SEQRES 15 A 469 THR ALA ASP PHE GLU GLY GLN SER PRO LYS CYS THR GLN
SEQRES 16 A 469 GLY VAL ARG GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE
SEQRES 17 A 469 LEU GLN GLY ALA TYR ASP THR VAL ARG TRP GLU PHE GLY
SEQRES 18 A 469 THR CYS GLN PRO LEU SER ASP GLU LYS ASP LEU THR GLN
SEQRES 19 A 469 LEU PHE MET PHE ALA ARG ASN ALA PHE THR VAL LEU ALA
SEQRES 20 A 469 MET MET ASP TYR PRO TYR PRO THR ASP PHE LEU GLY PRO
SEQRES 21 A 469 LEU PRO ALA ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU
SEQRES 22 A 469 LEU SER GLU ALA GLN ARG ILE THR GLY LEU ARG ALA LEU
SEQRES 23 A 469 ALA GLY LEU VAL TYR ASN ALA SER GLY SER GLU HIS CYS
SEQRES 24 A 469 TYR ASP ILE TYR ARG LEU TYR HIS SER CYS ALA ASP PRO
SEQRES 25 A 469 THR GLY CYS GLY THR GLY PRO ASP ALA ARG ALA TRP ASP
SEQRES 26 A 469 TYR GLN ALA CYS THR GLU ILE ASN LEU THR PHE ALA SER
SEQRES 27 A 469 ASN ASN VAL THR ASP MET PHE PRO ASP LEU PRO PHE THR
SEQRES 28 A 469 ASP GLU LEU ARG GLN ARG TYR CYS LEU ASP THR TRP GLY
SEQRES 29 A 469 VAL TRP PRO ARG PRO ASP TRP LEU LEU THR SER PHE TRP
SEQRES 30 A 469 GLY GLY ASP LEU ARG ALA ALA SER ASN ILE ILE PHE SER
SEQRES 31 A 469 ASN GLY ASN LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG
SEQRES 32 A 469 ARG ASN LEU SER ALA SER VAL ILE ALA VAL THR ILE GLN
SEQRES 33 A 469 GLY GLY ALA HIS HIS LEU ASP LEU ARG ALA SER HIS PRO
SEQRES 34 A 469 GLU ASP PRO ALA SER VAL VAL GLU ALA ARG LYS LEU GLU
SEQRES 35 A 469 ALA THR ILE ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG
SEQRES 36 A 469 GLU GLN GLN PRO ALA LEU ARG GLY GLY PRO ARG LEU SER
SEQRES 37 A 469 LEU
SEQRES 1 B 469 GLY ALA MET ASP ASP PRO GLY PHE GLN GLU ARG PHE PHE
SEQRES 2 B 469 GLN GLN ARG LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY
SEQRES 3 B 469 ASN LYS THR PHE PRO GLN ARG PHE LEU VAL SER ASP ARG
SEQRES 4 B 469 PHE TRP VAL ARG GLY GLU GLY PRO ILE PHE PHE TYR THR
SEQRES 5 B 469 GLY ASN GLU GLY ASP VAL TRP ALA PHE ALA ASN ASN SER
SEQRES 6 B 469 ALA PHE VAL ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU
SEQRES 7 B 469 LEU VAL PHE ALA GLU HIS ARG TYR TYR GLY LYS SER LEU
SEQRES 8 B 469 PRO PHE GLY ALA GLN SER THR GLN ARG GLY HIS THR GLU
SEQRES 9 B 469 LEU LEU THR VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU
SEQRES 10 B 469 LEU LEU ARG ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP
SEQRES 11 B 469 ALA PRO ALA ILE ALA PHE GLY GLY SER TYR GLY GLY MET
SEQRES 12 B 469 LEU SER ALA TYR LEU ARG MET LYS TYR PRO HIS LEU VAL
SEQRES 13 B 469 ALA GLY ALA LEU ALA ALA SER ALA PRO VAL LEU ALA VAL
SEQRES 14 B 469 ALA GLY LEU GLY ASP SER ASN GLN PHE PHE ARG ASP VAL
SEQRES 15 B 469 THR ALA ASP PHE GLU GLY GLN SER PRO LYS CYS THR GLN
SEQRES 16 B 469 GLY VAL ARG GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE
SEQRES 17 B 469 LEU GLN GLY ALA TYR ASP THR VAL ARG TRP GLU PHE GLY
SEQRES 18 B 469 THR CYS GLN PRO LEU SER ASP GLU LYS ASP LEU THR GLN
SEQRES 19 B 469 LEU PHE MET PHE ALA ARG ASN ALA PHE THR VAL LEU ALA
SEQRES 20 B 469 MET MET ASP TYR PRO TYR PRO THR ASP PHE LEU GLY PRO
SEQRES 21 B 469 LEU PRO ALA ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU
SEQRES 22 B 469 LEU SER GLU ALA GLN ARG ILE THR GLY LEU ARG ALA LEU
SEQRES 23 B 469 ALA GLY LEU VAL TYR ASN ALA SER GLY SER GLU HIS CYS
SEQRES 24 B 469 TYR ASP ILE TYR ARG LEU TYR HIS SER CYS ALA ASP PRO
SEQRES 25 B 469 THR GLY CYS GLY THR GLY PRO ASP ALA ARG ALA TRP ASP
SEQRES 26 B 469 TYR GLN ALA CYS THR GLU ILE ASN LEU THR PHE ALA SER
SEQRES 27 B 469 ASN ASN VAL THR ASP MET PHE PRO ASP LEU PRO PHE THR
SEQRES 28 B 469 ASP GLU LEU ARG GLN ARG TYR CYS LEU ASP THR TRP GLY
SEQRES 29 B 469 VAL TRP PRO ARG PRO ASP TRP LEU LEU THR SER PHE TRP
SEQRES 30 B 469 GLY GLY ASP LEU ARG ALA ALA SER ASN ILE ILE PHE SER
SEQRES 31 B 469 ASN GLY ASN LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG
SEQRES 32 B 469 ARG ASN LEU SER ALA SER VAL ILE ALA VAL THR ILE GLN
SEQRES 33 B 469 GLY GLY ALA HIS HIS LEU ASP LEU ARG ALA SER HIS PRO
SEQRES 34 B 469 GLU ASP PRO ALA SER VAL VAL GLU ALA ARG LYS LEU GLU
SEQRES 35 B 469 ALA THR ILE ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG
SEQRES 36 B 469 GLU GLN GLN PRO ALA LEU ARG GLY GLY PRO ARG LEU SER
SEQRES 37 B 469 LEU
SEQRES 1 C 469 GLY ALA MET ASP ASP PRO GLY PHE GLN GLU ARG PHE PHE
SEQRES 2 C 469 GLN GLN ARG LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY
SEQRES 3 C 469 ASN LYS THR PHE PRO GLN ARG PHE LEU VAL SER ASP ARG
SEQRES 4 C 469 PHE TRP VAL ARG GLY GLU GLY PRO ILE PHE PHE TYR THR
SEQRES 5 C 469 GLY ASN GLU GLY ASP VAL TRP ALA PHE ALA ASN ASN SER
SEQRES 6 C 469 ALA PHE VAL ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU
SEQRES 7 C 469 LEU VAL PHE ALA GLU HIS ARG TYR TYR GLY LYS SER LEU
SEQRES 8 C 469 PRO PHE GLY ALA GLN SER THR GLN ARG GLY HIS THR GLU
SEQRES 9 C 469 LEU LEU THR VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU
SEQRES 10 C 469 LEU LEU ARG ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP
SEQRES 11 C 469 ALA PRO ALA ILE ALA PHE GLY GLY SER TYR GLY GLY MET
SEQRES 12 C 469 LEU SER ALA TYR LEU ARG MET LYS TYR PRO HIS LEU VAL
SEQRES 13 C 469 ALA GLY ALA LEU ALA ALA SER ALA PRO VAL LEU ALA VAL
SEQRES 14 C 469 ALA GLY LEU GLY ASP SER ASN GLN PHE PHE ARG ASP VAL
SEQRES 15 C 469 THR ALA ASP PHE GLU GLY GLN SER PRO LYS CYS THR GLN
SEQRES 16 C 469 GLY VAL ARG GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE
SEQRES 17 C 469 LEU GLN GLY ALA TYR ASP THR VAL ARG TRP GLU PHE GLY
SEQRES 18 C 469 THR CYS GLN PRO LEU SER ASP GLU LYS ASP LEU THR GLN
SEQRES 19 C 469 LEU PHE MET PHE ALA ARG ASN ALA PHE THR VAL LEU ALA
SEQRES 20 C 469 MET MET ASP TYR PRO TYR PRO THR ASP PHE LEU GLY PRO
SEQRES 21 C 469 LEU PRO ALA ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU
SEQRES 22 C 469 LEU SER GLU ALA GLN ARG ILE THR GLY LEU ARG ALA LEU
SEQRES 23 C 469 ALA GLY LEU VAL TYR ASN ALA SER GLY SER GLU HIS CYS
SEQRES 24 C 469 TYR ASP ILE TYR ARG LEU TYR HIS SER CYS ALA ASP PRO
SEQRES 25 C 469 THR GLY CYS GLY THR GLY PRO ASP ALA ARG ALA TRP ASP
SEQRES 26 C 469 TYR GLN ALA CYS THR GLU ILE ASN LEU THR PHE ALA SER
SEQRES 27 C 469 ASN ASN VAL THR ASP MET PHE PRO ASP LEU PRO PHE THR
SEQRES 28 C 469 ASP GLU LEU ARG GLN ARG TYR CYS LEU ASP THR TRP GLY
SEQRES 29 C 469 VAL TRP PRO ARG PRO ASP TRP LEU LEU THR SER PHE TRP
SEQRES 30 C 469 GLY GLY ASP LEU ARG ALA ALA SER ASN ILE ILE PHE SER
SEQRES 31 C 469 ASN GLY ASN LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG
SEQRES 32 C 469 ARG ASN LEU SER ALA SER VAL ILE ALA VAL THR ILE GLN
SEQRES 33 C 469 GLY GLY ALA HIS HIS LEU ASP LEU ARG ALA SER HIS PRO
SEQRES 34 C 469 GLU ASP PRO ALA SER VAL VAL GLU ALA ARG LYS LEU GLU
SEQRES 35 C 469 ALA THR ILE ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG
SEQRES 36 C 469 GLU GLN GLN PRO ALA LEU ARG GLY GLY PRO ARG LEU SER
SEQRES 37 C 469 LEU
SEQRES 1 D 469 GLY ALA MET ASP ASP PRO GLY PHE GLN GLU ARG PHE PHE
SEQRES 2 D 469 GLN GLN ARG LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY
SEQRES 3 D 469 ASN LYS THR PHE PRO GLN ARG PHE LEU VAL SER ASP ARG
SEQRES 4 D 469 PHE TRP VAL ARG GLY GLU GLY PRO ILE PHE PHE TYR THR
SEQRES 5 D 469 GLY ASN GLU GLY ASP VAL TRP ALA PHE ALA ASN ASN SER
SEQRES 6 D 469 ALA PHE VAL ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU
SEQRES 7 D 469 LEU VAL PHE ALA GLU HIS ARG TYR TYR GLY LYS SER LEU
SEQRES 8 D 469 PRO PHE GLY ALA GLN SER THR GLN ARG GLY HIS THR GLU
SEQRES 9 D 469 LEU LEU THR VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU
SEQRES 10 D 469 LEU LEU ARG ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP
SEQRES 11 D 469 ALA PRO ALA ILE ALA PHE GLY GLY SER TYR GLY GLY MET
SEQRES 12 D 469 LEU SER ALA TYR LEU ARG MET LYS TYR PRO HIS LEU VAL
SEQRES 13 D 469 ALA GLY ALA LEU ALA ALA SER ALA PRO VAL LEU ALA VAL
SEQRES 14 D 469 ALA GLY LEU GLY ASP SER ASN GLN PHE PHE ARG ASP VAL
SEQRES 15 D 469 THR ALA ASP PHE GLU GLY GLN SER PRO LYS CYS THR GLN
SEQRES 16 D 469 GLY VAL ARG GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE
SEQRES 17 D 469 LEU GLN GLY ALA TYR ASP THR VAL ARG TRP GLU PHE GLY
SEQRES 18 D 469 THR CYS GLN PRO LEU SER ASP GLU LYS ASP LEU THR GLN
SEQRES 19 D 469 LEU PHE MET PHE ALA ARG ASN ALA PHE THR VAL LEU ALA
SEQRES 20 D 469 MET MET ASP TYR PRO TYR PRO THR ASP PHE LEU GLY PRO
SEQRES 21 D 469 LEU PRO ALA ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU
SEQRES 22 D 469 LEU SER GLU ALA GLN ARG ILE THR GLY LEU ARG ALA LEU
SEQRES 23 D 469 ALA GLY LEU VAL TYR ASN ALA SER GLY SER GLU HIS CYS
SEQRES 24 D 469 TYR ASP ILE TYR ARG LEU TYR HIS SER CYS ALA ASP PRO
SEQRES 25 D 469 THR GLY CYS GLY THR GLY PRO ASP ALA ARG ALA TRP ASP
SEQRES 26 D 469 TYR GLN ALA CYS THR GLU ILE ASN LEU THR PHE ALA SER
SEQRES 27 D 469 ASN ASN VAL THR ASP MET PHE PRO ASP LEU PRO PHE THR
SEQRES 28 D 469 ASP GLU LEU ARG GLN ARG TYR CYS LEU ASP THR TRP GLY
SEQRES 29 D 469 VAL TRP PRO ARG PRO ASP TRP LEU LEU THR SER PHE TRP
SEQRES 30 D 469 GLY GLY ASP LEU ARG ALA ALA SER ASN ILE ILE PHE SER
SEQRES 31 D 469 ASN GLY ASN LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG
SEQRES 32 D 469 ARG ASN LEU SER ALA SER VAL ILE ALA VAL THR ILE GLN
SEQRES 33 D 469 GLY GLY ALA HIS HIS LEU ASP LEU ARG ALA SER HIS PRO
SEQRES 34 D 469 GLU ASP PRO ALA SER VAL VAL GLU ALA ARG LYS LEU GLU
SEQRES 35 D 469 ALA THR ILE ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG
SEQRES 36 D 469 GLU GLN GLN PRO ALA LEU ARG GLY GLY PRO ARG LEU SER
SEQRES 37 D 469 LEU
HET OPY A1001 13
HET OPY B1001 13
HET OPY C1001 13
HET OPY D1001 13
HETNAM OPY (3S)-4-OXO-4-PIPERIDIN-1-YLBUTANE-1,3-DIAMINE
HETSYN OPY GSK237826A
FORMUL 5 OPY 4(C9 H19 N3 O)
FORMUL 9 HOH *248(H2 O)
HELIX 1 1 ASP A 80 SER A 88 1 9
HELIX 2 2 ALA A 89 GLY A 99 1 11
HELIX 3 3 PHE A 116 SER A 120 5 5
HELIX 4 4 THR A 130 GLY A 150 1 21
HELIX 5 5 SER A 162 TYR A 175 1 14
HELIX 6 6 PRO A 188 ALA A 193 1 6
HELIX 7 7 ASN A 199 SER A 213 1 15
HELIX 8 8 SER A 213 GLN A 233 1 21
HELIX 9 9 ALA A 235 GLY A 244 1 10
HELIX 10 10 ASP A 251 MET A 272 1 22
HELIX 11 11 ASN A 287 SER A 298 1 12
HELIX 12 12 GLN A 301 ASN A 315 1 15
HELIX 13 13 GLY A 341 CYS A 352 1 12
HELIX 14 14 THR A 374 GLY A 387 1 14
HELIX 15 15 ASP A 393 TRP A 400 1 8
HELIX 16 16 TRP A 420 GLY A 424 5 5
HELIX 17 17 HIS A 444 ARG A 448 5 5
HELIX 18 18 PRO A 455 ARG A 477 1 23
HELIX 19 19 ASP B 80 SER B 88 1 9
HELIX 20 20 SER B 88 GLY B 99 1 12
HELIX 21 21 PHE B 116 SER B 120 5 5
HELIX 22 22 THR B 130 GLY B 150 1 21
HELIX 23 23 SER B 162 TYR B 175 1 14
HELIX 24 24 PRO B 188 ALA B 193 1 6
HELIX 25 25 ASN B 199 SER B 213 1 15
HELIX 26 26 SER B 213 GLN B 233 1 21
HELIX 27 27 ALA B 235 GLY B 244 1 10
HELIX 28 28 ASP B 251 MET B 272 1 22
HELIX 29 29 ASN B 287 SER B 298 1 12
HELIX 30 30 GLN B 301 ASN B 315 1 15
HELIX 31 31 GLY B 341 CYS B 352 1 12
HELIX 32 32 THR B 374 GLY B 387 1 14
HELIX 33 33 ASP B 393 TRP B 400 1 8
HELIX 34 34 TRP B 420 GLY B 424 5 5
HELIX 35 35 HIS B 444 ARG B 448 5 5
HELIX 36 36 PRO B 455 GLU B 479 1 25
HELIX 37 37 ASP C 80 SER C 88 1 9
HELIX 38 38 SER C 88 GLY C 99 1 12
HELIX 39 39 PHE C 116 GLN C 122 5 7
HELIX 40 40 THR C 130 LEU C 149 1 20
HELIX 41 41 SER C 162 TYR C 175 1 14
HELIX 42 42 LEU C 190 GLY C 194 5 5
HELIX 43 43 ASN C 199 GLY C 211 1 13
HELIX 44 44 SER C 213 GLY C 234 1 22
HELIX 45 45 ALA C 235 GLY C 244 1 10
HELIX 46 46 ASP C 251 MET C 272 1 22
HELIX 47 47 ASN C 287 GLU C 299 1 13
HELIX 48 48 GLN C 301 ASN C 315 1 15
HELIX 49 49 ASP C 324 TYR C 329 1 6
HELIX 50 50 GLY C 341 ALA C 351 1 11
HELIX 51 51 THR C 374 TRP C 386 1 13
HELIX 52 52 ASP C 393 TRP C 400 1 8
HELIX 53 53 TRP C 420 GLY C 424 5 5
HELIX 54 54 PRO C 455 ARG C 477 1 23
HELIX 55 55 ASP D 80 ASN D 86 1 7
HELIX 56 56 ALA D 89 GLY D 99 1 11
HELIX 57 57 PHE D 116 GLN D 122 5 7
HELIX 58 58 THR D 130 LEU D 149 1 20
HELIX 59 59 SER D 162 TYR D 175 1 14
HELIX 60 60 PRO D 188 ALA D 193 1 6
HELIX 61 61 ASN D 199 SER D 213 1 15
HELIX 62 62 SER D 213 GLY D 234 1 22
HELIX 63 63 ALA D 235 GLY D 244 1 10
HELIX 64 64 ASP D 251 MET D 272 1 22
HELIX 65 65 ASN D 287 GLU D 299 1 13
HELIX 66 66 GLN D 301 ASN D 315 1 15
HELIX 67 67 ASP D 324 TYR D 329 1 6
HELIX 68 68 GLY D 341 GLU D 354 1 14
HELIX 69 69 THR D 374 GLY D 387 1 14
HELIX 70 70 ASP D 393 TRP D 400 1 8
HELIX 71 71 TRP D 420 GLY D 424 5 5
HELIX 72 72 HIS D 444 ARG D 448 5 5
HELIX 73 73 PRO D 455 ARG D 477 1 23
SHEET 1 A 8 GLN A 32 ARG A 39 0
SHEET 2 A 8 THR A 52 SER A 60 -1 O PHE A 57 N ARG A 34
SHEET 3 A 8 LEU A 101 ALA A 105 -1 O LEU A 102 N SER A 60
SHEET 4 A 8 ILE A 71 THR A 75 1 N TYR A 74 O VAL A 103
SHEET 5 A 8 ALA A 156 GLY A 161 1 O ILE A 157 N ILE A 71
SHEET 6 A 8 GLY A 181 ALA A 185 1 O LEU A 183 N ALA A 158
SHEET 7 A 8 ILE A 410 GLY A 415 1 O ILE A 411 N ALA A 184
SHEET 8 A 8 VAL A 433 ILE A 438 1 O ILE A 434 N PHE A 412
SHEET 1 B 2 THR A 278 ASP A 279 0
SHEET 2 B 2 PRO A 283 LEU A 284 -1 O LEU A 284 N THR A 278
SHEET 1 C 8 GLN B 32 ARG B 39 0
SHEET 2 C 8 THR B 52 SER B 60 -1 O GLN B 55 N PHE B 36
SHEET 3 C 8 LEU B 101 ALA B 105 -1 O PHE B 104 N LEU B 58
SHEET 4 C 8 ILE B 71 THR B 75 1 N PHE B 72 O LEU B 101
SHEET 5 C 8 ALA B 156 GLY B 161 1 O PHE B 159 N PHE B 73
SHEET 6 C 8 GLY B 181 ALA B 185 1 O GLY B 181 N ALA B 158
SHEET 7 C 8 ILE B 410 GLY B 415 1 O ILE B 411 N ALA B 184
SHEET 8 C 8 VAL B 433 ILE B 438 1 O ILE B 434 N PHE B 412
SHEET 1 D 2 THR B 278 ASP B 279 0
SHEET 2 D 2 PRO B 283 LEU B 284 -1 O LEU B 284 N THR B 278
SHEET 1 E 8 GLN C 32 ARG C 39 0
SHEET 2 E 8 THR C 52 SER C 60 -1 O GLN C 55 N PHE C 36
SHEET 3 E 8 LEU C 101 ALA C 105 -1 O PHE C 104 N LEU C 58
SHEET 4 E 8 ILE C 71 THR C 75 1 N TYR C 74 O VAL C 103
SHEET 5 E 8 ALA C 156 GLY C 161 1 O ILE C 157 N ILE C 71
SHEET 6 E 8 GLY C 181 ALA C 185 1 O LEU C 183 N ALA C 158
SHEET 7 E 8 ILE C 410 GLY C 415 1 O ILE C 411 N ALA C 184
SHEET 8 E 8 VAL C 433 ILE C 438 1 O ILE C 434 N PHE C 412
SHEET 1 F 2 THR C 278 ASP C 279 0
SHEET 2 F 2 PRO C 283 LEU C 284 -1 O LEU C 284 N THR C 278
SHEET 1 G 8 GLN D 32 ARG D 39 0
SHEET 2 G 8 THR D 52 SER D 60 -1 O PHE D 53 N GLN D 38
SHEET 3 G 8 LEU D 101 ALA D 105 -1 O PHE D 104 N LEU D 58
SHEET 4 G 8 ILE D 71 THR D 75 1 N PHE D 72 O LEU D 101
SHEET 5 G 8 ALA D 156 GLY D 161 1 O ILE D 157 N ILE D 71
SHEET 6 G 8 GLY D 181 ALA D 185 1 O LEU D 183 N ALA D 158
SHEET 7 G 8 ILE D 410 GLY D 415 1 O ILE D 411 N ALA D 184
SHEET 8 G 8 VAL D 433 ILE D 438 1 O ILE D 434 N PHE D 412
SHEET 1 H 2 THR D 278 ASP D 279 0
SHEET 2 H 2 PRO D 283 LEU D 284 -1 O LEU D 284 N THR D 278
SSBOND 1 CYS A 293 CYS A 216 1555 1555 2.06
SSBOND 2 CYS A 322 CYS A 246 1555 1555 2.04
SSBOND 3 CYS A 338 CYS A 332 1555 1555 2.05
SSBOND 4 CYS A 382 CYS A 352 1555 1555 2.04
SSBOND 5 CYS B 293 CYS B 216 1555 1555 2.04
SSBOND 6 CYS B 322 CYS B 246 1555 1555 2.04
SSBOND 7 CYS B 338 CYS B 332 1555 1555 2.05
SSBOND 8 CYS B 382 CYS B 352 1555 1555 2.04
SSBOND 9 CYS C 293 CYS C 216 1555 1555 2.05
SSBOND 10 CYS C 322 CYS C 246 1555 1555 2.05
SSBOND 11 CYS C 338 CYS C 332 1555 1555 2.06
SSBOND 12 CYS C 382 CYS C 352 1555 1555 2.04
SSBOND 13 CYS D 293 CYS D 216 1555 1555 2.04
SSBOND 14 CYS D 322 CYS D 246 1555 1555 2.05
SSBOND 15 CYS D 338 CYS D 332 1555 1555 2.05
SSBOND 16 CYS D 382 CYS D 352 1555 1555 2.03
SITE 1 AC1 11 GLU A 78 SER A 162 PRO A 188 MET A 271
SITE 2 AC1 11 ASP A 334 THR A 336 GLY A 337 TRP A 347
SITE 3 AC1 11 TRP A 420 HIS A 443 HOH A 545
SITE 1 AC2 10 GLU B 78 SER B 162 TYR B 163 PRO B 188
SITE 2 AC2 10 MET B 271 ASP B 334 THR B 336 GLY B 337
SITE 3 AC2 10 TRP B 347 TRP B 420
SITE 1 AC3 10 GLU C 78 SER C 162 TYR C 163 PRO C 188
SITE 2 AC3 10 MET C 271 ASP C 334 THR C 336 GLY C 337
SITE 3 AC3 10 TRP C 347 TRP C 420
SITE 1 AC4 10 GLU D 78 SER D 162 TYR D 163 PRO D 188
SITE 2 AC4 10 MET D 271 ASP D 334 THR D 336 GLY D 337
SITE 3 AC4 10 TRP D 347 TRP D 420
CRYST1 80.546 130.500 125.075 90.00 102.28 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 0.012415 0.000000 0.002702 0.00000
SCALE2 0.000000 0.007663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008182 0.00000
TER 3487 GLU A 479
TER 6964 GLU B 479
TER 10414 ARG C 478
TER 13837 ARG D 477
MASTER 595 0 4 73 40 0 12 614133 4 84 148
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