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HEADER HYDROLASE 22-MAY-22 7ZXS
TITLE CRYSTAL STRUCTURE OF DPP9 IN COMPLEX WITH A 4-OXO-B-LACTAM BASED
TITLE 2 INHIBITOR, A295
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 9;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: EXTCOLOR{RED}{>FRAGMENT<};
COMPND 5 SYNONYM: DP9,DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 2,DPRP-2,
COMPND 6 DIPEPTIDYL PEPTIDASE IX,DPP IX,DIPEPTIDYL PEPTIDASE-LIKE PROTEIN 9,
COMPND 7 DPLP9;
COMPND 8 EC: 3.4.14.5;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: DIPEPTIDYL PEPTIDASE 9;
COMPND 12 CHAIN: B, D;
COMPND 13 SYNONYM: DP9,DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 2,DPRP-2,
COMPND 14 DIPEPTIDYL PEPTIDASE IX,DPP IX,DIPEPTIDYL PEPTIDASE-LIKE PROTEIN 9,
COMPND 15 DPLP9;
COMPND 16 EC: 3.4.14.5;
COMPND 17 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: DPP9, DPRP2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: DPP9, DPRP2;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS DIPEPTIDYL PEPTIDASE, DPP9, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.ROSS,R.HUBER
REVDAT 1 28-SEP-22 7ZXS 0
JRNL AUTH L.A.R.CARVALHO,B.ROSS,L.FEHR,O.BOLGI,S.WOHRLE,K.M.LUM,
JRNL AUTH 2 D.PODLESAINSKI,A.C.VIEIRA,R.KIEFERSAUER,R.FELIX,T.RODRIGUES,
JRNL AUTH 3 S.D.LUCAS,O.GROSS,R.GEISS-FRIEDLANDER,B.F.CRAVATT,R.HUBER,
JRNL AUTH 4 M.KAISER,R.MOREIRA
JRNL TITL CHEMOPROTEOMICS-ENABLED IDENTIFICATION OF 4-OXO-BETA-LACTAMS
JRNL TITL 2 AS INHIBITORS OF DIPEPTIDYL PEPTIDASES 8 AND 9.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2022
JRNL REFN ESSN 1521-3773
JRNL PMID 36089535
JRNL DOI 10.1002/ANIE.202210498
REMARK 2
REMARK 2 RESOLUTION. 1.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 106.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 64.6
REMARK 3 NUMBER OF REFLECTIONS : 219248
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1707
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1059
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 4.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE SET COUNT : 10
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 27210
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 321
REMARK 3 SOLVENT ATOMS : 1653
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.07000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : -0.06000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.193
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.678
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 27958 ; 0.005 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 25440 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 37983 ; 1.357 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 58559 ; 1.191 ; 1.573
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3417 ; 7.188 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1439 ;31.955 ;22.147
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4295 ;12.978 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 147 ;19.179 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3454 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 31833 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 6645 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 22 865 B 22 865 9791 0.030 0.050
REMARK 3 2 A 22 865 C 22 865 9765 0.030 0.050
REMARK 3 3 A 22 865 D 22 865 9696 0.030 0.050
REMARK 3 4 B 21 865 C 21 865 9845 0.030 0.050
REMARK 3 5 B 22 864 D 22 864 9790 0.030 0.050
REMARK 3 6 C 22 865 D 22 865 9817 0.020 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7ZXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1292123050.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-22
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 : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : X-GEN
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 220955
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.807
REMARK 200 RESOLUTION RANGE LOW (A) : 106.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 64.6
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 FOR THE DATA SET : 5.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 15.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.45900
REMARK 200 R SYM FOR SHELL (I) : 0.45900
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6EOR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE CRYSTAL IS GROWN IN A CONDITION
REMARK 280 CONTAINING PEG 2K MME BUFFERED BY TRIS PH 7, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 APPLY THE FOLLOWING TO CHAINS: A, C
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 APPLY THE FOLLOWING TO CHAINS: B, 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 PRO A 20
REMARK 465 ALA A 21
REMARK 465 HIS A 866
REMARK 465 HIS A 867
REMARK 465 HIS A 868
REMARK 465 HIS A 869
REMARK 465 TYR B 44
REMARK 465 SER B 45
REMARK 465 GLY B 46
REMARK 465 LEU B 47
REMARK 465 ILE B 48
REMARK 465 VAL B 49
REMARK 465 ASN B 50
REMARK 465 HIS B 866
REMARK 465 HIS B 867
REMARK 465 HIS B 868
REMARK 465 HIS B 869
REMARK 465 PRO C 20
REMARK 465 GLY C 119
REMARK 465 VAL C 120
REMARK 465 HIS C 866
REMARK 465 HIS C 867
REMARK 465 HIS C 868
REMARK 465 HIS C 869
REMARK 465 PRO D 20
REMARK 465 ALA D 21
REMARK 465 TYR D 44
REMARK 465 SER D 45
REMARK 465 GLY D 46
REMARK 465 LEU D 47
REMARK 465 ILE D 48
REMARK 465 VAL D 49
REMARK 465 HIS D 866
REMARK 465 HIS D 867
REMARK 465 HIS D 868
REMARK 465 HIS D 869
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 28 CE NZ
REMARK 480 LYS A 43 NZ
REMARK 480 ASN A 50 CG OD1 ND2
REMARK 480 LYS A 51 CG CD CE NZ
REMARK 480 THR A 62 OG1 CG2
REMARK 480 TYR A 79 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 ARG A 82 CD NE CZ NH1 NH2
REMARK 480 ILE A 91 CD1
REMARK 480 LYS A 93 NZ
REMARK 480 LYS A 94 CD CE NZ
REMARK 480 ARG A 96 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 97 CG CD CE NZ
REMARK 480 GLU A 98 CG CD OE1 OE2
REMARK 480 GLN A 113 CD OE1 NE2
REMARK 480 HIS A 117 CG ND1 CD2 CE1 NE2
REMARK 480 LYS A 132 NZ
REMARK 480 ILE A 139 CD1
REMARK 480 GLU A 147 CD OE1 OE2
REMARK 480 LYS A 167 CD CE NZ
REMARK 480 ASN A 168 CG OD1 ND2
REMARK 480 MET A 175 CE
REMARK 480 LYS A 176 CD CE NZ
REMARK 480 LEU A 178 CD1 CD2
REMARK 480 LYS A 181 CD CE NZ
REMARK 480 SER A 267 OG
REMARK 480 GLU A 268 CD OE1 OE2
REMARK 480 LYS A 299 NZ
REMARK 480 LYS A 311 NZ
REMARK 480 SER A 326 OG
REMARK 480 GLN A 327 CD OE1 NE2
REMARK 480 LYS A 329 CE NZ
REMARK 480 ILE A 330 CD1
REMARK 480 LYS A 348 NZ
REMARK 480 LYS A 362 CE NZ
REMARK 480 GLU A 391 CG CD OE1 OE2
REMARK 480 GLU A 394 CG CD OE1 OE2
REMARK 480 ILE A 426 CD1
REMARK 480 LYS A 462 CG CD CE NZ
REMARK 480 GLU A 470 CD OE1 OE2
REMARK 480 PHE A 472 CG CD1 CD2 CE1 CE2 CZ
REMARK 480 SER A 473 OG
REMARK 480 GLU A 476 CG CD OE1 OE2
REMARK 480 LYS A 480 NZ
REMARK 480 LYS A 503 NZ
REMARK 480 GLU A 509 CD OE1 OE2
REMARK 480 GLU A 533 CD OE1 OE2
REMARK 480 MET A 558 CE
REMARK 480 LYS A 576 CE NZ
REMARK 480 GLN A 588 CD OE1 NE2
REMARK 480 ARG A 590 CZ NH1 NH2
REMARK 480 SER A 600 OG
REMARK 480 ASP A 618 CG OD1 OD2
REMARK 480 GLN A 632 CD OE1 NE2
REMARK 480 LYS A 635 NZ
REMARK 480 LYS A 660 NZ
REMARK 480 LYS A 748 CE NZ
REMARK 480 GLN A 778 CD OE1 NE2
REMARK 480 LYS B 43 CE NZ
REMARK 480 LYS B 51 CD CE NZ
REMARK 480 GLU B 64 CG CD OE1 OE2
REMARK 480 TYR B 79 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 ARG B 82 CD NE CZ NH1 NH2
REMARK 480 LYS B 94 CD CE NZ
REMARK 480 ARG B 96 CD NE CZ NH1 NH2
REMARK 480 LYS B 97 CD CE NZ
REMARK 480 GLU B 98 CG CD OE1 OE2
REMARK 480 LEU B 100 CD1 CD2
REMARK 480 LEU B 102 CD1 CD2
REMARK 480 LYS B 106 CE NZ
REMARK 480 GLN B 113 CD OE1 NE2
REMARK 480 HIS B 117 CG ND1 CD2 CE1 NE2
REMARK 480 HIS B 118 CG ND1 CD2 CE1 NE2
REMARK 480 GLU B 147 CD OE1 OE2
REMARK 480 LYS B 167 CD CE NZ
REMARK 480 ASN B 168 CG OD1 ND2
REMARK 480 MET B 175 CE
REMARK 480 LYS B 176 CD CE NZ
REMARK 480 LYS B 181 CD CE NZ
REMARK 480 ILE B 214 CD1
REMARK 480 SER B 267 OG
REMARK 480 GLU B 268 CD OE1 OE2
REMARK 480 GLU B 297 CD OE1 OE2
REMARK 480 LYS B 299 NZ
REMARK 480 LYS B 314 NZ
REMARK 480 SER B 326 OG
REMARK 480 GLN B 327 CG CD OE1 NE2
REMARK 480 LYS B 329 NZ
REMARK 480 LYS B 348 CE NZ
REMARK 480 GLU B 391 CD OE1 OE2
REMARK 480 GLU B 393 CD OE1 OE2
REMARK 480 LYS B 462 CD CE NZ
REMARK 480 GLU B 470 CD OE1 OE2
REMARK 480 GLU B 476 CG CD OE1 OE2
REMARK 480 LYS B 484 NZ
REMARK 480 LYS B 503 CE NZ
REMARK 480 GLU B 509 CD OE1 OE2
REMARK 480 LYS B 576 NZ
REMARK 480 ARG B 590 CZ NH1 NH2
REMARK 480 SER B 600 OG
REMARK 480 LYS B 660 CE NZ
REMARK 480 ARG B 688 CD NE CZ NH1 NH2
REMARK 480 GLU B 791 CD OE1 OE2
REMARK 480 LYS B 792 NZ
REMARK 480 LYS C 28 NZ
REMARK 480 LYS C 43 CD CE NZ
REMARK 480 TYR C 44 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 SER C 45 OG
REMARK 480 LEU C 47 CD1 CD2
REMARK 480 ILE C 48 CD1
REMARK 480 VAL C 49 CG1 CG2
REMARK 480 ASN C 50 CG OD1 ND2
REMARK 480 LYS C 51 CG CD CE NZ
REMARK 480 GLU C 64 CD OE1 OE2
REMARK 480 ARG C 82 CG CD NE CZ NH1 NH2
REMARK 480 LYS C 94 CE NZ
REMARK 480 ARG C 96 CD NE CZ NH1 NH2
REMARK 480 LYS C 97 CG CD CE NZ
REMARK 480 GLU C 98 CG CD OE1 OE2
REMARK 480 ASP C 110 CG OD1 OD2
REMARK 480 HIS C 111 CG ND1 CD2 CE1 NE2
REMARK 480 GLN C 113 CD OE1 NE2
REMARK 480 HIS C 117 CG ND1 CD2 CE1 NE2
REMARK 480 HIS C 118 CG ND1 CD2 CE1 NE2
REMARK 480 GLU C 124 CD OE1 OE2
REMARK 480 LYS C 132 NZ
REMARK 480 ARG C 133 CG CD NE CZ NH1 NH2
REMARK 480 VAL C 136 CG1 CG2
REMARK 480 GLU C 147 CD OE1 OE2
REMARK 480 SER C 156 OG
REMARK 480 LYS C 167 CG CD CE NZ
REMARK 480 ASN C 168 CG OD1 ND2
REMARK 480 SER C 173 OG
REMARK 480 LYS C 176 CG CD CE NZ
REMARK 480 LYS C 181 CE NZ
REMARK 480 ILE C 214 CD1
REMARK 480 LYS C 237 NZ
REMARK 480 SER C 267 OG
REMARK 480 LYS C 299 NZ
REMARK 480 LYS C 311 NZ
REMARK 480 GLN C 327 CD OE1 NE2
REMARK 480 LYS C 348 NZ
REMARK 480 GLU C 394 CD OE1 OE2
REMARK 480 GLU C 434 CG CD OE1 OE2
REMARK 480 GLU C 476 CG CD OE1 OE2
REMARK 480 LYS C 480 NZ
REMARK 480 GLU C 509 CD OE1 OE2
REMARK 480 GLU C 533 CG CD OE1 OE2
REMARK 480 LYS C 576 NZ
REMARK 480 ARG C 590 CD NE CZ NH1 NH2
REMARK 480 SER C 600 OG
REMARK 480 LYS C 660 NZ
REMARK 480 ARG C 688 CD NE CZ NH1 NH2
REMARK 480 GLN C 745 CD OE1 NE2
REMARK 480 MET C 760 CE
REMARK 480 GLU C 775 CD OE1 OE2
REMARK 480 LYS C 792 NZ
REMARK 480 GLU C 809 CD OE1 OE2
REMARK 480 ARG C 843 NE CZ NH1 NH2
REMARK 480 LYS D 43 NZ
REMARK 480 ASN D 50 CG OD1 ND2
REMARK 480 LYS D 51 CD CE NZ
REMARK 480 GLU D 64 CD OE1 OE2
REMARK 480 ARG D 82 CD NE CZ NH1 NH2
REMARK 480 LYS D 94 CE NZ
REMARK 480 ARG D 96 NE CZ NH1 NH2
REMARK 480 LYS D 97 CG CD CE NZ
REMARK 480 GLU D 98 CG CD OE1 OE2
REMARK 480 ASP D 110 CG OD1 OD2
REMARK 480 GLN D 113 CG CD OE1 NE2
REMARK 480 HIS D 117 CG ND1 CD2 CE1 NE2
REMARK 480 HIS D 118 CG ND1 CD2 CE1 NE2
REMARK 480 VAL D 120 CG1 CG2
REMARK 480 ARG D 129 CZ NH1 NH2
REMARK 480 LYS D 132 NZ
REMARK 480 LEU D 134 CG CD1 CD2
REMARK 480 VAL D 136 CG1 CG2
REMARK 480 PHE D 137 CG CD1 CD2 CE1 CE2 CZ
REMARK 480 LYS D 167 CG CD CE NZ
REMARK 480 MET D 175 CE
REMARK 480 LYS D 176 NZ
REMARK 480 LYS D 181 CE NZ
REMARK 480 GLU D 268 CG CD OE1 OE2
REMARK 480 LYS D 299 NZ
REMARK 480 LYS D 311 NZ
REMARK 480 GLU D 393 CD OE1 OE2
REMARK 480 GLU D 394 CG CD OE1 OE2
REMARK 480 GLN D 395 CD OE1 NE2
REMARK 480 ARG D 401 CZ NH1 NH2
REMARK 480 GLN D 464 CG CD OE1 NE2
REMARK 480 GLU D 470 CD OE1 OE2
REMARK 480 GLU D 476 CG CD OE1 OE2
REMARK 480 LYS D 480 CE NZ
REMARK 480 LYS D 576 NZ
REMARK 480 SER D 600 OG
REMARK 480 GLN D 632 CD OE1 NE2
REMARK 480 LYS D 635 NZ
REMARK 480 ARG D 688 CZ NH1 NH2
REMARK 480 MET D 760 SD CE
REMARK 480 GLN D 778 CD OE1 NE2
REMARK 480 LYS D 792 NZ
REMARK 480 ARG D 843 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 98 54.64 -102.51
REMARK 500 HIS A 111 73.19 30.11
REMARK 500 ALA A 155 139.98 -170.66
REMARK 500 VAL A 419 -99.42 -97.13
REMARK 500 THR A 521 144.22 -173.85
REMARK 500 TYR A 644 -72.10 -110.41
REMARK 500 GLN A 696 39.06 -144.89
REMARK 500 SER A 730 -114.67 68.16
REMARK 500 ALA A 754 57.06 37.66
REMARK 500 ASP A 772 -176.70 66.64
REMARK 500 ASN A 777 50.74 -150.28
REMARK 500 ASN A 810 -67.95 -107.23
REMARK 500 ARG A 839 -133.39 -81.53
REMARK 500 THR B 62 52.94 -118.12
REMARK 500 GLU B 98 42.21 -99.41
REMARK 500 HIS B 111 74.47 30.27
REMARK 500 ALA B 155 141.45 -170.94
REMARK 500 VAL B 419 -100.31 -100.16
REMARK 500 GLU B 493 59.90 -91.24
REMARK 500 THR B 521 142.62 -175.22
REMARK 500 ALA B 534 71.55 -114.43
REMARK 500 TYR B 644 -73.50 -109.55
REMARK 500 GLN B 696 39.44 -143.13
REMARK 500 SER B 730 -114.06 70.80
REMARK 500 ALA B 754 55.72 39.31
REMARK 500 ASP B 772 -175.72 65.86
REMARK 500 ASN B 777 52.68 -152.77
REMARK 500 ASN B 810 -67.53 -107.36
REMARK 500 ARG B 839 -135.10 -82.53
REMARK 500 TYR C 44 45.13 -101.43
REMARK 500 GLU C 98 51.81 -100.95
REMARK 500 HIS C 111 75.71 28.58
REMARK 500 ALA C 155 138.16 -171.32
REMARK 500 VAL C 419 -100.08 -97.51
REMARK 500 ASP C 437 30.21 -98.94
REMARK 500 THR C 521 143.39 -172.81
REMARK 500 ALA C 534 70.18 -110.55
REMARK 500 TYR C 644 -73.00 -110.19
REMARK 500 GLN C 696 40.15 -144.80
REMARK 500 SER C 730 -113.33 69.29
REMARK 500 ASP C 772 -173.39 65.41
REMARK 500 ASN C 777 51.99 -151.43
REMARK 500 ASN C 810 -69.59 -102.04
REMARK 500 ARG C 839 -138.00 -85.11
REMARK 500 ASP D 55 65.19 61.75
REMARK 500 GLU D 98 52.77 -101.53
REMARK 500 HIS D 111 76.24 28.34
REMARK 500 VAL D 419 -100.58 -97.55
REMARK 500 PHE D 479 -0.17 77.76
REMARK 500 GLU D 493 58.81 -90.05
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 KBO A 901
REMARK 615 KBO B 901
REMARK 615 KBO C 901
REMARK 615 KBO D 901
DBREF 7ZXS A 20 863 UNP Q86TI2 DPP9_HUMAN 20 863
DBREF 7ZXS B 20 863 UNP Q86TI2 DPP9_HUMAN 20 863
DBREF 7ZXS C 20 863 UNP Q86TI2 DPP9_HUMAN 20 863
DBREF 7ZXS D 20 863 UNP Q86TI2 DPP9_HUMAN 20 863
SEQADV 7ZXS HIS A 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS A 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS A 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS A 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS A 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS A 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS B 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS B 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS B 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS B 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS B 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS B 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS C 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS C 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS C 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS C 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS C 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS C 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS D 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS D 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS D 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS D 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS D 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 7ZXS HIS D 869 UNP Q86TI2 EXPRESSION TAG
SEQRES 1 A 850 PRO ALA ALA ARG PHE GLN VAL GLN LYS HIS SER TRP ASP
SEQRES 2 A 850 GLY LEU ARG SER ILE ILE HIS GLY SER ARG LYS TYR SER
SEQRES 3 A 850 GLY LEU ILE VAL ASN LYS ALA PRO HIS ASP PHE GLN PHE
SEQRES 4 A 850 VAL GLN LYS THR ASP GLU SER GLY PRO HIS SER HIS ARG
SEQRES 5 A 850 LEU TYR TYR LEU GLY MET PRO TYR GLY SER ARG GLU ASN
SEQRES 6 A 850 SER LEU LEU TYR SER GLU ILE PRO LYS LYS VAL ARG LYS
SEQRES 7 A 850 GLU ALA LEU LEU LEU LEU SER TRP LYS GLN MET LEU ASP
SEQRES 8 A 850 HIS PHE GLN ALA THR PRO HIS HIS GLY VAL TYR SER ARG
SEQRES 9 A 850 GLU GLU GLU LEU LEU ARG GLU ARG LYS ARG LEU GLY VAL
SEQRES 10 A 850 PHE GLY ILE THR SER TYR ASP PHE HIS SER GLU SER GLY
SEQRES 11 A 850 LEU PHE LEU PHE GLN ALA SER ASN SER LEU PHE HIS CYS
SEQRES 12 A 850 ARG ASP GLY GLY LYS ASN GLY PHE MET VAL SER PRO MET
SEQRES 13 A 850 LYS PRO LEU GLU ILE LYS THR GLN CYS SER GLY PRO ARG
SEQRES 14 A 850 MET ASP PRO LYS ILE CYS PRO ALA ASP PRO ALA PHE PHE
SEQRES 15 A 850 SER PHE ILE ASN ASN SER ASP LEU TRP VAL ALA ASN ILE
SEQRES 16 A 850 GLU THR GLY GLU GLU ARG ARG LEU THR PHE CYS HIS GLN
SEQRES 17 A 850 GLY LEU SER ASN VAL LEU ASP ASP PRO LYS SER ALA GLY
SEQRES 18 A 850 VAL ALA THR PHE VAL ILE GLN GLU GLU PHE ASP ARG PHE
SEQRES 19 A 850 THR GLY TYR TRP TRP CYS PRO THR ALA SER TRP GLU GLY
SEQRES 20 A 850 SER GLU GLY LEU LYS THR LEU ARG ILE LEU TYR GLU GLU
SEQRES 21 A 850 VAL ASP GLU SER GLU VAL GLU VAL ILE HIS VAL PRO SER
SEQRES 22 A 850 PRO ALA LEU GLU GLU ARG LYS THR ASP SER TYR ARG TYR
SEQRES 23 A 850 PRO ARG THR GLY SER LYS ASN PRO LYS ILE ALA LEU LYS
SEQRES 24 A 850 LEU ALA GLU PHE GLN THR ASP SER GLN GLY LYS ILE VAL
SEQRES 25 A 850 SER THR GLN GLU LYS GLU LEU VAL GLN PRO PHE SER SER
SEQRES 26 A 850 LEU PHE PRO LYS VAL GLU TYR ILE ALA ARG ALA GLY TRP
SEQRES 27 A 850 THR ARG ASP GLY LYS TYR ALA TRP ALA MET PHE LEU ASP
SEQRES 28 A 850 ARG PRO GLN GLN TRP LEU GLN LEU VAL LEU LEU PRO PRO
SEQRES 29 A 850 ALA LEU PHE ILE PRO SER THR GLU ASN GLU GLU GLN ARG
SEQRES 30 A 850 LEU ALA SER ALA ARG ALA VAL PRO ARG ASN VAL GLN PRO
SEQRES 31 A 850 TYR VAL VAL TYR GLU GLU VAL THR ASN VAL TRP ILE ASN
SEQRES 32 A 850 VAL HIS ASP ILE PHE TYR PRO PHE PRO GLN SER GLU GLY
SEQRES 33 A 850 GLU ASP GLU LEU CYS PHE LEU ARG ALA ASN GLU CYS LYS
SEQRES 34 A 850 THR GLY PHE CYS HIS LEU TYR LYS VAL THR ALA VAL LEU
SEQRES 35 A 850 LYS SER GLN GLY TYR ASP TRP SER GLU PRO PHE SER PRO
SEQRES 36 A 850 GLY GLU ASP GLU PHE LYS CYS PRO ILE LYS GLU GLU ILE
SEQRES 37 A 850 ALA LEU THR SER GLY GLU TRP GLU VAL LEU ALA ARG HIS
SEQRES 38 A 850 GLY SER LYS ILE TRP VAL ASN GLU GLU THR LYS LEU VAL
SEQRES 39 A 850 TYR PHE GLN GLY THR LYS ASP THR PRO LEU GLU HIS HIS
SEQRES 40 A 850 LEU TYR VAL VAL SER TYR GLU ALA ALA GLY GLU ILE VAL
SEQRES 41 A 850 ARG LEU THR THR PRO GLY PHE SER HIS SER CYS SER MET
SEQRES 42 A 850 SER GLN ASN PHE ASP MET PHE VAL SER HIS TYR SER SER
SEQRES 43 A 850 VAL SER THR PRO PRO CYS VAL HIS VAL TYR LYS LEU SER
SEQRES 44 A 850 GLY PRO ASP ASP ASP PRO LEU HIS LYS GLN PRO ARG PHE
SEQRES 45 A 850 TRP ALA SER MET MET GLU ALA ALA SER CYS PRO PRO ASP
SEQRES 46 A 850 TYR VAL PRO PRO GLU ILE PHE HIS PHE HIS THR ARG SER
SEQRES 47 A 850 ASP VAL ARG LEU TYR GLY MET ILE TYR LYS PRO HIS ALA
SEQRES 48 A 850 LEU GLN PRO GLY LYS LYS HIS PRO THR VAL LEU PHE VAL
SEQRES 49 A 850 TYR GLY GLY PRO GLN VAL GLN LEU VAL ASN ASN SER PHE
SEQRES 50 A 850 LYS GLY ILE LYS TYR LEU ARG LEU ASN THR LEU ALA SER
SEQRES 51 A 850 LEU GLY TYR ALA VAL VAL VAL ILE ASP GLY ARG GLY SER
SEQRES 52 A 850 CYS GLN ARG GLY LEU ARG PHE GLU GLY ALA LEU LYS ASN
SEQRES 53 A 850 GLN MET GLY GLN VAL GLU ILE GLU ASP GLN VAL GLU GLY
SEQRES 54 A 850 LEU GLN PHE VAL ALA GLU LYS TYR GLY PHE ILE ASP LEU
SEQRES 55 A 850 SER ARG VAL ALA ILE HIS GLY TRP SER TYR GLY GLY PHE
SEQRES 56 A 850 LEU SER LEU MET GLY LEU ILE HIS LYS PRO GLN VAL PHE
SEQRES 57 A 850 LYS VAL ALA ILE ALA GLY ALA PRO VAL THR VAL TRP MET
SEQRES 58 A 850 ALA TYR ASP THR GLY TYR THR GLU ARG TYR MET ASP VAL
SEQRES 59 A 850 PRO GLU ASN ASN GLN HIS GLY TYR GLU ALA GLY SER VAL
SEQRES 60 A 850 ALA LEU HIS VAL GLU LYS LEU PRO ASN GLU PRO ASN ARG
SEQRES 61 A 850 LEU LEU ILE LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS
SEQRES 62 A 850 PHE PHE HIS THR ASN PHE LEU VAL SER GLN LEU ILE ARG
SEQRES 63 A 850 ALA GLY LYS PRO TYR GLN LEU GLN ILE TYR PRO ASN GLU
SEQRES 64 A 850 ARG HIS SER ILE ARG CSO PRO GLU SER GLY GLU HIS TYR
SEQRES 65 A 850 GLU VAL THR LEU LEU HIS PHE LEU GLN GLU TYR LEU HIS
SEQRES 66 A 850 HIS HIS HIS HIS HIS
SEQRES 1 B 850 PRO ALA ALA ARG PHE GLN VAL GLN LYS HIS SER TRP ASP
SEQRES 2 B 850 GLY LEU ARG SER ILE ILE HIS GLY SER ARG LYS TYR SER
SEQRES 3 B 850 GLY LEU ILE VAL ASN LYS ALA PRO HIS ASP PHE GLN PHE
SEQRES 4 B 850 VAL GLN LYS THR ASP GLU SER GLY PRO HIS SER HIS ARG
SEQRES 5 B 850 LEU TYR TYR LEU GLY MET PRO TYR GLY SER ARG GLU ASN
SEQRES 6 B 850 SER LEU LEU TYR SER GLU ILE PRO LYS LYS VAL ARG LYS
SEQRES 7 B 850 GLU ALA LEU LEU LEU LEU SER TRP LYS GLN MET LEU ASP
SEQRES 8 B 850 HIS PHE GLN ALA THR PRO HIS HIS GLY VAL TYR SER ARG
SEQRES 9 B 850 GLU GLU GLU LEU LEU ARG GLU ARG LYS ARG LEU GLY VAL
SEQRES 10 B 850 PHE GLY ILE THR SER TYR ASP PHE HIS SER GLU SER GLY
SEQRES 11 B 850 LEU PHE LEU PHE GLN ALA SER ASN SER LEU PHE HIS CYS
SEQRES 12 B 850 ARG ASP GLY GLY LYS ASN GLY PHE MET VAL SER PRO MET
SEQRES 13 B 850 LYS PRO LEU GLU ILE LYS THR GLN CYS SER GLY PRO ARG
SEQRES 14 B 850 MET ASP PRO LYS ILE CYS PRO ALA ASP PRO ALA PHE PHE
SEQRES 15 B 850 SER PHE ILE ASN ASN SER ASP LEU TRP VAL ALA ASN ILE
SEQRES 16 B 850 GLU THR GLY GLU GLU ARG ARG LEU THR PHE CYS HIS GLN
SEQRES 17 B 850 GLY LEU SER ASN VAL LEU ASP ASP PRO LYS SER ALA GLY
SEQRES 18 B 850 VAL ALA THR PHE VAL ILE GLN GLU GLU PHE ASP ARG PHE
SEQRES 19 B 850 THR GLY TYR TRP TRP CYS PRO THR ALA SER TRP GLU GLY
SEQRES 20 B 850 SER GLU GLY LEU LYS THR LEU ARG ILE LEU TYR GLU GLU
SEQRES 21 B 850 VAL ASP GLU SER GLU VAL GLU VAL ILE HIS VAL PRO SER
SEQRES 22 B 850 PRO ALA LEU GLU GLU ARG LYS THR ASP SER TYR ARG TYR
SEQRES 23 B 850 PRO ARG THR GLY SER LYS ASN PRO LYS ILE ALA LEU LYS
SEQRES 24 B 850 LEU ALA GLU PHE GLN THR ASP SER GLN GLY LYS ILE VAL
SEQRES 25 B 850 SER THR GLN GLU LYS GLU LEU VAL GLN PRO PHE SER SER
SEQRES 26 B 850 LEU PHE PRO LYS VAL GLU TYR ILE ALA ARG ALA GLY TRP
SEQRES 27 B 850 THR ARG ASP GLY LYS TYR ALA TRP ALA MET PHE LEU ASP
SEQRES 28 B 850 ARG PRO GLN GLN TRP LEU GLN LEU VAL LEU LEU PRO PRO
SEQRES 29 B 850 ALA LEU PHE ILE PRO SER THR GLU ASN GLU GLU GLN ARG
SEQRES 30 B 850 LEU ALA SER ALA ARG ALA VAL PRO ARG ASN VAL GLN PRO
SEQRES 31 B 850 TYR VAL VAL TYR GLU GLU VAL THR ASN VAL TRP ILE ASN
SEQRES 32 B 850 VAL HIS ASP ILE PHE TYR PRO PHE PRO GLN SER GLU GLY
SEQRES 33 B 850 GLU ASP GLU LEU CYS PHE LEU ARG ALA ASN GLU CYS LYS
SEQRES 34 B 850 THR GLY PHE CYS HIS LEU TYR LYS VAL THR ALA VAL LEU
SEQRES 35 B 850 LYS SER GLN GLY TYR ASP TRP SER GLU PRO PHE SER PRO
SEQRES 36 B 850 GLY GLU ASP GLU PHE LYS CYS PRO ILE LYS GLU GLU ILE
SEQRES 37 B 850 ALA LEU THR SER GLY GLU TRP GLU VAL LEU ALA ARG HIS
SEQRES 38 B 850 GLY SER LYS ILE TRP VAL ASN GLU GLU THR LYS LEU VAL
SEQRES 39 B 850 TYR PHE GLN GLY THR LYS ASP THR PRO LEU GLU HIS HIS
SEQRES 40 B 850 LEU TYR VAL VAL SER TYR GLU ALA ALA GLY GLU ILE VAL
SEQRES 41 B 850 ARG LEU THR THR PRO GLY PHE SER HIS SER CYS SER MET
SEQRES 42 B 850 SER GLN ASN PHE ASP MET PHE VAL SER HIS TYR SER SER
SEQRES 43 B 850 VAL SER THR PRO PRO CYS VAL HIS VAL TYR LYS LEU SER
SEQRES 44 B 850 GLY PRO ASP ASP ASP PRO LEU HIS LYS GLN PRO ARG PHE
SEQRES 45 B 850 TRP ALA SER MET MET GLU ALA ALA SER CYS PRO PRO ASP
SEQRES 46 B 850 TYR VAL PRO PRO GLU ILE PHE HIS PHE HIS THR ARG SER
SEQRES 47 B 850 ASP VAL ARG LEU TYR GLY MET ILE TYR LYS PRO HIS ALA
SEQRES 48 B 850 LEU GLN PRO GLY LYS LYS HIS PRO THR VAL LEU PHE VAL
SEQRES 49 B 850 TYR GLY GLY PRO GLN VAL GLN LEU VAL ASN ASN SER PHE
SEQRES 50 B 850 LYS GLY ILE LYS TYR LEU ARG LEU ASN THR LEU ALA SER
SEQRES 51 B 850 LEU GLY TYR ALA VAL VAL VAL ILE ASP GLY ARG GLY SER
SEQRES 52 B 850 CYS GLN ARG GLY LEU ARG PHE GLU GLY ALA LEU LYS ASN
SEQRES 53 B 850 GLN MET GLY GLN VAL GLU ILE GLU ASP GLN VAL GLU GLY
SEQRES 54 B 850 LEU GLN PHE VAL ALA GLU LYS TYR GLY PHE ILE ASP LEU
SEQRES 55 B 850 SER ARG VAL ALA ILE HIS GLY TRP SER TYR GLY GLY PHE
SEQRES 56 B 850 LEU SER LEU MET GLY LEU ILE HIS LYS PRO GLN VAL PHE
SEQRES 57 B 850 LYS VAL ALA ILE ALA GLY ALA PRO VAL THR VAL TRP MET
SEQRES 58 B 850 ALA TYR ASP THR GLY TYR THR GLU ARG TYR MET ASP VAL
SEQRES 59 B 850 PRO GLU ASN ASN GLN HIS GLY TYR GLU ALA GLY SER VAL
SEQRES 60 B 850 ALA LEU HIS VAL GLU LYS LEU PRO ASN GLU PRO ASN ARG
SEQRES 61 B 850 LEU LEU ILE LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS
SEQRES 62 B 850 PHE PHE HIS THR ASN PHE LEU VAL SER GLN LEU ILE ARG
SEQRES 63 B 850 ALA GLY LYS PRO TYR GLN LEU GLN ILE TYR PRO ASN GLU
SEQRES 64 B 850 ARG HIS SER ILE ARG CYS PRO GLU SER GLY GLU HIS TYR
SEQRES 65 B 850 GLU VAL THR LEU LEU HIS PHE LEU GLN GLU TYR LEU HIS
SEQRES 66 B 850 HIS HIS HIS HIS HIS
SEQRES 1 C 850 PRO ALA ALA ARG PHE GLN VAL GLN LYS HIS SER TRP ASP
SEQRES 2 C 850 GLY LEU ARG SER ILE ILE HIS GLY SER ARG LYS TYR SER
SEQRES 3 C 850 GLY LEU ILE VAL ASN LYS ALA PRO HIS ASP PHE GLN PHE
SEQRES 4 C 850 VAL GLN LYS THR ASP GLU SER GLY PRO HIS SER HIS ARG
SEQRES 5 C 850 LEU TYR TYR LEU GLY MET PRO TYR GLY SER ARG GLU ASN
SEQRES 6 C 850 SER LEU LEU TYR SER GLU ILE PRO LYS LYS VAL ARG LYS
SEQRES 7 C 850 GLU ALA LEU LEU LEU LEU SER TRP LYS GLN MET LEU ASP
SEQRES 8 C 850 HIS PHE GLN ALA THR PRO HIS HIS GLY VAL TYR SER ARG
SEQRES 9 C 850 GLU GLU GLU LEU LEU ARG GLU ARG LYS ARG LEU GLY VAL
SEQRES 10 C 850 PHE GLY ILE THR SER TYR ASP PHE HIS SER GLU SER GLY
SEQRES 11 C 850 LEU PHE LEU PHE GLN ALA SER ASN SER LEU PHE HIS CYS
SEQRES 12 C 850 ARG ASP GLY GLY LYS ASN GLY PHE MET VAL SER PRO MET
SEQRES 13 C 850 LYS PRO LEU GLU ILE LYS THR GLN CYS SER GLY PRO ARG
SEQRES 14 C 850 MET ASP PRO LYS ILE CYS PRO ALA ASP PRO ALA PHE PHE
SEQRES 15 C 850 SER PHE ILE ASN ASN SER ASP LEU TRP VAL ALA ASN ILE
SEQRES 16 C 850 GLU THR GLY GLU GLU ARG ARG LEU THR PHE CYS HIS GLN
SEQRES 17 C 850 GLY LEU SER ASN VAL LEU ASP ASP PRO LYS SER ALA GLY
SEQRES 18 C 850 VAL ALA THR PHE VAL ILE GLN GLU GLU PHE ASP ARG PHE
SEQRES 19 C 850 THR GLY TYR TRP TRP CYS PRO THR ALA SER TRP GLU GLY
SEQRES 20 C 850 SER GLU GLY LEU LYS THR LEU ARG ILE LEU TYR GLU GLU
SEQRES 21 C 850 VAL ASP GLU SER GLU VAL GLU VAL ILE HIS VAL PRO SER
SEQRES 22 C 850 PRO ALA LEU GLU GLU ARG LYS THR ASP SER TYR ARG TYR
SEQRES 23 C 850 PRO ARG THR GLY SER LYS ASN PRO LYS ILE ALA LEU LYS
SEQRES 24 C 850 LEU ALA GLU PHE GLN THR ASP SER GLN GLY LYS ILE VAL
SEQRES 25 C 850 SER THR GLN GLU LYS GLU LEU VAL GLN PRO PHE SER SER
SEQRES 26 C 850 LEU PHE PRO LYS VAL GLU TYR ILE ALA ARG ALA GLY TRP
SEQRES 27 C 850 THR ARG ASP GLY LYS TYR ALA TRP ALA MET PHE LEU ASP
SEQRES 28 C 850 ARG PRO GLN GLN TRP LEU GLN LEU VAL LEU LEU PRO PRO
SEQRES 29 C 850 ALA LEU PHE ILE PRO SER THR GLU ASN GLU GLU GLN ARG
SEQRES 30 C 850 LEU ALA SER ALA ARG ALA VAL PRO ARG ASN VAL GLN PRO
SEQRES 31 C 850 TYR VAL VAL TYR GLU GLU VAL THR ASN VAL TRP ILE ASN
SEQRES 32 C 850 VAL HIS ASP ILE PHE TYR PRO PHE PRO GLN SER GLU GLY
SEQRES 33 C 850 GLU ASP GLU LEU CYS PHE LEU ARG ALA ASN GLU CYS LYS
SEQRES 34 C 850 THR GLY PHE CYS HIS LEU TYR LYS VAL THR ALA VAL LEU
SEQRES 35 C 850 LYS SER GLN GLY TYR ASP TRP SER GLU PRO PHE SER PRO
SEQRES 36 C 850 GLY GLU ASP GLU PHE LYS CYS PRO ILE LYS GLU GLU ILE
SEQRES 37 C 850 ALA LEU THR SER GLY GLU TRP GLU VAL LEU ALA ARG HIS
SEQRES 38 C 850 GLY SER LYS ILE TRP VAL ASN GLU GLU THR LYS LEU VAL
SEQRES 39 C 850 TYR PHE GLN GLY THR LYS ASP THR PRO LEU GLU HIS HIS
SEQRES 40 C 850 LEU TYR VAL VAL SER TYR GLU ALA ALA GLY GLU ILE VAL
SEQRES 41 C 850 ARG LEU THR THR PRO GLY PHE SER HIS SER CYS SER MET
SEQRES 42 C 850 SER GLN ASN PHE ASP MET PHE VAL SER HIS TYR SER SER
SEQRES 43 C 850 VAL SER THR PRO PRO CYS VAL HIS VAL TYR LYS LEU SER
SEQRES 44 C 850 GLY PRO ASP ASP ASP PRO LEU HIS LYS GLN PRO ARG PHE
SEQRES 45 C 850 TRP ALA SER MET MET GLU ALA ALA SER CYS PRO PRO ASP
SEQRES 46 C 850 TYR VAL PRO PRO GLU ILE PHE HIS PHE HIS THR ARG SER
SEQRES 47 C 850 ASP VAL ARG LEU TYR GLY MET ILE TYR LYS PRO HIS ALA
SEQRES 48 C 850 LEU GLN PRO GLY LYS LYS HIS PRO THR VAL LEU PHE VAL
SEQRES 49 C 850 TYR GLY GLY PRO GLN VAL GLN LEU VAL ASN ASN SER PHE
SEQRES 50 C 850 LYS GLY ILE LYS TYR LEU ARG LEU ASN THR LEU ALA SER
SEQRES 51 C 850 LEU GLY TYR ALA VAL VAL VAL ILE ASP GLY ARG GLY SER
SEQRES 52 C 850 CYS GLN ARG GLY LEU ARG PHE GLU GLY ALA LEU LYS ASN
SEQRES 53 C 850 GLN MET GLY GLN VAL GLU ILE GLU ASP GLN VAL GLU GLY
SEQRES 54 C 850 LEU GLN PHE VAL ALA GLU LYS TYR GLY PHE ILE ASP LEU
SEQRES 55 C 850 SER ARG VAL ALA ILE HIS GLY TRP SER TYR GLY GLY PHE
SEQRES 56 C 850 LEU SER LEU MET GLY LEU ILE HIS LYS PRO GLN VAL PHE
SEQRES 57 C 850 LYS VAL ALA ILE ALA GLY ALA PRO VAL THR VAL TRP MET
SEQRES 58 C 850 ALA TYR ASP THR GLY TYR THR GLU ARG TYR MET ASP VAL
SEQRES 59 C 850 PRO GLU ASN ASN GLN HIS GLY TYR GLU ALA GLY SER VAL
SEQRES 60 C 850 ALA LEU HIS VAL GLU LYS LEU PRO ASN GLU PRO ASN ARG
SEQRES 61 C 850 LEU LEU ILE LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS
SEQRES 62 C 850 PHE PHE HIS THR ASN PHE LEU VAL SER GLN LEU ILE ARG
SEQRES 63 C 850 ALA GLY LYS PRO TYR GLN LEU GLN ILE TYR PRO ASN GLU
SEQRES 64 C 850 ARG HIS SER ILE ARG CSO PRO GLU SER GLY GLU HIS TYR
SEQRES 65 C 850 GLU VAL THR LEU LEU HIS PHE LEU GLN GLU TYR LEU HIS
SEQRES 66 C 850 HIS HIS HIS HIS HIS
SEQRES 1 D 850 PRO ALA ALA ARG PHE GLN VAL GLN LYS HIS SER TRP ASP
SEQRES 2 D 850 GLY LEU ARG SER ILE ILE HIS GLY SER ARG LYS TYR SER
SEQRES 3 D 850 GLY LEU ILE VAL ASN LYS ALA PRO HIS ASP PHE GLN PHE
SEQRES 4 D 850 VAL GLN LYS THR ASP GLU SER GLY PRO HIS SER HIS ARG
SEQRES 5 D 850 LEU TYR TYR LEU GLY MET PRO TYR GLY SER ARG GLU ASN
SEQRES 6 D 850 SER LEU LEU TYR SER GLU ILE PRO LYS LYS VAL ARG LYS
SEQRES 7 D 850 GLU ALA LEU LEU LEU LEU SER TRP LYS GLN MET LEU ASP
SEQRES 8 D 850 HIS PHE GLN ALA THR PRO HIS HIS GLY VAL TYR SER ARG
SEQRES 9 D 850 GLU GLU GLU LEU LEU ARG GLU ARG LYS ARG LEU GLY VAL
SEQRES 10 D 850 PHE GLY ILE THR SER TYR ASP PHE HIS SER GLU SER GLY
SEQRES 11 D 850 LEU PHE LEU PHE GLN ALA SER ASN SER LEU PHE HIS CYS
SEQRES 12 D 850 ARG ASP GLY GLY LYS ASN GLY PHE MET VAL SER PRO MET
SEQRES 13 D 850 LYS PRO LEU GLU ILE LYS THR GLN CYS SER GLY PRO ARG
SEQRES 14 D 850 MET ASP PRO LYS ILE CYS PRO ALA ASP PRO ALA PHE PHE
SEQRES 15 D 850 SER PHE ILE ASN ASN SER ASP LEU TRP VAL ALA ASN ILE
SEQRES 16 D 850 GLU THR GLY GLU GLU ARG ARG LEU THR PHE CYS HIS GLN
SEQRES 17 D 850 GLY LEU SER ASN VAL LEU ASP ASP PRO LYS SER ALA GLY
SEQRES 18 D 850 VAL ALA THR PHE VAL ILE GLN GLU GLU PHE ASP ARG PHE
SEQRES 19 D 850 THR GLY TYR TRP TRP CYS PRO THR ALA SER TRP GLU GLY
SEQRES 20 D 850 SER GLU GLY LEU LYS THR LEU ARG ILE LEU TYR GLU GLU
SEQRES 21 D 850 VAL ASP GLU SER GLU VAL GLU VAL ILE HIS VAL PRO SER
SEQRES 22 D 850 PRO ALA LEU GLU GLU ARG LYS THR ASP SER TYR ARG TYR
SEQRES 23 D 850 PRO ARG THR GLY SER LYS ASN PRO LYS ILE ALA LEU LYS
SEQRES 24 D 850 LEU ALA GLU PHE GLN THR ASP SER GLN GLY LYS ILE VAL
SEQRES 25 D 850 SER THR GLN GLU LYS GLU LEU VAL GLN PRO PHE SER SER
SEQRES 26 D 850 LEU PHE PRO LYS VAL GLU TYR ILE ALA ARG ALA GLY TRP
SEQRES 27 D 850 THR ARG ASP GLY LYS TYR ALA TRP ALA MET PHE LEU ASP
SEQRES 28 D 850 ARG PRO GLN GLN TRP LEU GLN LEU VAL LEU LEU PRO PRO
SEQRES 29 D 850 ALA LEU PHE ILE PRO SER THR GLU ASN GLU GLU GLN ARG
SEQRES 30 D 850 LEU ALA SER ALA ARG ALA VAL PRO ARG ASN VAL GLN PRO
SEQRES 31 D 850 TYR VAL VAL TYR GLU GLU VAL THR ASN VAL TRP ILE ASN
SEQRES 32 D 850 VAL HIS ASP ILE PHE TYR PRO PHE PRO GLN SER GLU GLY
SEQRES 33 D 850 GLU ASP GLU LEU CYS PHE LEU ARG ALA ASN GLU CYS LYS
SEQRES 34 D 850 THR GLY PHE CYS HIS LEU TYR LYS VAL THR ALA VAL LEU
SEQRES 35 D 850 LYS SER GLN GLY TYR ASP TRP SER GLU PRO PHE SER PRO
SEQRES 36 D 850 GLY GLU ASP GLU PHE LYS CYS PRO ILE LYS GLU GLU ILE
SEQRES 37 D 850 ALA LEU THR SER GLY GLU TRP GLU VAL LEU ALA ARG HIS
SEQRES 38 D 850 GLY SER LYS ILE TRP VAL ASN GLU GLU THR LYS LEU VAL
SEQRES 39 D 850 TYR PHE GLN GLY THR LYS ASP THR PRO LEU GLU HIS HIS
SEQRES 40 D 850 LEU TYR VAL VAL SER TYR GLU ALA ALA GLY GLU ILE VAL
SEQRES 41 D 850 ARG LEU THR THR PRO GLY PHE SER HIS SER CYS SER MET
SEQRES 42 D 850 SER GLN ASN PHE ASP MET PHE VAL SER HIS TYR SER SER
SEQRES 43 D 850 VAL SER THR PRO PRO CYS VAL HIS VAL TYR LYS LEU SER
SEQRES 44 D 850 GLY PRO ASP ASP ASP PRO LEU HIS LYS GLN PRO ARG PHE
SEQRES 45 D 850 TRP ALA SER MET MET GLU ALA ALA SER CYS PRO PRO ASP
SEQRES 46 D 850 TYR VAL PRO PRO GLU ILE PHE HIS PHE HIS THR ARG SER
SEQRES 47 D 850 ASP VAL ARG LEU TYR GLY MET ILE TYR LYS PRO HIS ALA
SEQRES 48 D 850 LEU GLN PRO GLY LYS LYS HIS PRO THR VAL LEU PHE VAL
SEQRES 49 D 850 TYR GLY GLY PRO GLN VAL GLN LEU VAL ASN ASN SER PHE
SEQRES 50 D 850 LYS GLY ILE LYS TYR LEU ARG LEU ASN THR LEU ALA SER
SEQRES 51 D 850 LEU GLY TYR ALA VAL VAL VAL ILE ASP GLY ARG GLY SER
SEQRES 52 D 850 CYS GLN ARG GLY LEU ARG PHE GLU GLY ALA LEU LYS ASN
SEQRES 53 D 850 GLN MET GLY GLN VAL GLU ILE GLU ASP GLN VAL GLU GLY
SEQRES 54 D 850 LEU GLN PHE VAL ALA GLU LYS TYR GLY PHE ILE ASP LEU
SEQRES 55 D 850 SER ARG VAL ALA ILE HIS GLY TRP SER TYR GLY GLY PHE
SEQRES 56 D 850 LEU SER LEU MET GLY LEU ILE HIS LYS PRO GLN VAL PHE
SEQRES 57 D 850 LYS VAL ALA ILE ALA GLY ALA PRO VAL THR VAL TRP MET
SEQRES 58 D 850 ALA TYR ASP THR GLY TYR THR GLU ARG TYR MET ASP VAL
SEQRES 59 D 850 PRO GLU ASN ASN GLN HIS GLY TYR GLU ALA GLY SER VAL
SEQRES 60 D 850 ALA LEU HIS VAL GLU LYS LEU PRO ASN GLU PRO ASN ARG
SEQRES 61 D 850 LEU LEU ILE LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS
SEQRES 62 D 850 PHE PHE HIS THR ASN PHE LEU VAL SER GLN LEU ILE ARG
SEQRES 63 D 850 ALA GLY LYS PRO TYR GLN LEU GLN ILE TYR PRO ASN GLU
SEQRES 64 D 850 ARG HIS SER ILE ARG CYS PRO GLU SER GLY GLU HIS TYR
SEQRES 65 D 850 GLU VAL THR LEU LEU HIS PHE LEU GLN GLU TYR LEU HIS
SEQRES 66 D 850 HIS HIS HIS HIS HIS
MODRES 7ZXS CSO A 844 CYS MODIFIED RESIDUE
MODRES 7ZXS CSO C 844 CYS MODIFIED RESIDUE
HET CSO A 844 7
HET CSO C 844 7
HET KBO A 901 34
HET EDO A 902 4
HET EDO A 903 4
HET EDO A 904 4
HET EDO A 905 4
HET EDO A 906 4
HET EDO A 907 4
HET EDO A 908 4
HET KBO B 901 34
HET EDO B 902 4
HET EDO B 903 4
HET EDO B 904 4
HET EDO B 905 4
HET EDO B 906 4
HET EDO B 907 4
HET EDO B 908 4
HET EDO B 909 4
HET EDO B 910 4
HET EDO B 911 4
HET EDO B 912 4
HET PEG B 913 7
HET EDO B 914 4
HET KBO C 901 34
HET EDO C 902 4
HET EDO C 903 4
HET EDO C 904 4
HET EDO C 905 4
HET EDO C 906 4
HET EDO C 907 4
HET EDO C 908 4
HET PEG C 909 7
HET EDO C 910 4
HET EDO C 911 4
HET EDO C 912 4
HET KBO D 901 34
HET EDO D 902 4
HET EDO D 903 4
HET EDO D 904 4
HET EDO D 905 4
HET EDO D 906 4
HET EDO D 907 4
HET EDO D 908 4
HET EDO D 909 4
HET EDO D 910 4
HET EDO D 911 4
HET PEG D 912 7
HET EDO D 913 4
HET EDO D 914 4
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM KBO 2-ETHYL-2-METHANOYL-~{N}-[3-[[4-(QUINOLIN-8-YLMETHYL)
HETNAM 2 KBO PIPERAZIN-1-YL]METHYL]PHENYL]BUTANAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 5 KBO 4(C28 H34 N4 O2)
FORMUL 6 EDO 41(C2 H6 O2)
FORMUL 25 PEG 3(C4 H10 O3)
FORMUL 53 HOH *1653(H2 O)
HELIX 1 AA1 SER A 30 VAL A 49 1 20
HELIX 2 AA2 PRO A 116 VAL A 120 5 5
HELIX 3 AA3 SER A 122 LYS A 132 1 11
HELIX 4 AA4 ASN A 231 ASP A 235 5 5
HELIX 5 AA5 THR A 243 ASP A 251 1 9
HELIX 6 AA6 ALA A 294 ARG A 298 5 5
HELIX 7 AA7 PRO A 341 PHE A 346 1 6
HELIX 8 AA8 PRO A 382 ALA A 384 5 3
HELIX 9 AA9 ASN A 392 VAL A 403 1 12
HELIX 10 AB1 ASP A 583 LYS A 587 5 5
HELIX 11 AB2 TYR A 661 LEU A 670 1 10
HELIX 12 AB3 GLY A 686 GLY A 691 1 6
HELIX 13 AB4 ALA A 692 LYS A 694 5 3
HELIX 14 AB5 VAL A 700 GLY A 717 1 18
HELIX 15 AB6 SER A 730 LYS A 743 1 14
HELIX 16 AB7 VAL A 758 TYR A 762 5 5
HELIX 17 AB8 ASP A 763 ASP A 772 1 10
HELIX 18 AB9 VAL A 773 ASN A 776 5 4
HELIX 19 AC1 ASN A 777 SER A 785 1 9
HELIX 20 AC2 VAL A 786 LEU A 793 5 8
HELIX 21 AC3 PHE A 813 ALA A 826 1 14
HELIX 22 AC4 CSO A 844 LEU A 863 1 20
HELIX 23 AC5 SER B 30 ARG B 42 1 13
HELIX 24 AC6 PRO B 116 VAL B 120 5 5
HELIX 25 AC7 SER B 122 LYS B 132 1 11
HELIX 26 AC8 ASN B 231 ASP B 235 5 5
HELIX 27 AC9 THR B 243 ASP B 251 1 9
HELIX 28 AD1 ALA B 294 ARG B 298 5 5
HELIX 29 AD2 PRO B 341 PHE B 346 1 6
HELIX 30 AD3 PRO B 382 ALA B 384 5 3
HELIX 31 AD4 ASN B 392 ALA B 402 1 11
HELIX 32 AD5 ASP B 583 LYS B 587 5 5
HELIX 33 AD6 TYR B 661 LEU B 670 1 10
HELIX 34 AD7 GLY B 686 GLY B 691 1 6
HELIX 35 AD8 ALA B 692 LYS B 694 5 3
HELIX 36 AD9 VAL B 700 GLY B 717 1 18
HELIX 37 AE1 SER B 730 LYS B 743 1 14
HELIX 38 AE2 VAL B 758 TYR B 762 5 5
HELIX 39 AE3 ASP B 763 ASP B 772 1 10
HELIX 40 AE4 VAL B 773 ASN B 776 5 4
HELIX 41 AE5 ASN B 777 SER B 785 1 9
HELIX 42 AE6 VAL B 786 LEU B 793 5 8
HELIX 43 AE7 PHE B 813 ALA B 826 1 14
HELIX 44 AE8 CYS B 844 LEU B 863 1 20
HELIX 45 AE9 SER C 30 TYR C 44 1 15
HELIX 46 AF1 SER C 122 LYS C 132 1 11
HELIX 47 AF2 ASN C 231 ASP C 235 5 5
HELIX 48 AF3 THR C 243 ASP C 251 1 9
HELIX 49 AF4 ALA C 294 ARG C 298 5 5
HELIX 50 AF5 PRO C 341 PHE C 346 1 6
HELIX 51 AF6 PRO C 382 ALA C 384 5 3
HELIX 52 AF7 ASN C 392 ALA C 402 1 11
HELIX 53 AF8 ASP C 583 LYS C 587 5 5
HELIX 54 AF9 TYR C 661 LEU C 670 1 10
HELIX 55 AG1 GLY C 686 GLY C 691 1 6
HELIX 56 AG2 ALA C 692 LYS C 694 5 3
HELIX 57 AG3 VAL C 700 GLY C 717 1 18
HELIX 58 AG4 SER C 730 LYS C 743 1 14
HELIX 59 AG5 VAL C 758 TYR C 762 5 5
HELIX 60 AG6 ASP C 763 ASP C 772 1 10
HELIX 61 AG7 VAL C 773 ASN C 776 5 4
HELIX 62 AG8 ASN C 777 SER C 785 1 9
HELIX 63 AG9 VAL C 786 LEU C 793 5 8
HELIX 64 AH1 PHE C 813 ALA C 826 1 14
HELIX 65 AH2 CSO C 844 LEU C 863 1 20
HELIX 66 AH3 SER D 30 LYS D 43 1 14
HELIX 67 AH4 PRO D 116 VAL D 120 5 5
HELIX 68 AH5 SER D 122 LYS D 132 1 11
HELIX 69 AH6 ASN D 231 ASP D 235 5 5
HELIX 70 AH7 THR D 243 ASP D 251 1 9
HELIX 71 AH8 ALA D 294 ARG D 298 5 5
HELIX 72 AH9 PRO D 341 PHE D 346 1 6
HELIX 73 AI1 PRO D 382 ALA D 384 5 3
HELIX 74 AI2 ASN D 392 ALA D 402 1 11
HELIX 75 AI3 ASP D 583 LYS D 587 5 5
HELIX 76 AI4 TYR D 661 LEU D 670 1 10
HELIX 77 AI5 GLY D 686 GLY D 691 1 6
HELIX 78 AI6 ALA D 692 LYS D 694 5 3
HELIX 79 AI7 VAL D 700 GLY D 717 1 18
HELIX 80 AI8 SER D 730 LYS D 743 1 14
HELIX 81 AI9 VAL D 758 TYR D 762 5 5
HELIX 82 AJ1 ASP D 763 ASP D 772 1 10
HELIX 83 AJ2 VAL D 773 ASN D 776 5 4
HELIX 84 AJ3 ASN D 777 SER D 785 1 9
HELIX 85 AJ4 VAL D 786 LEU D 793 5 8
HELIX 86 AJ5 PHE D 813 ALA D 826 1 14
HELIX 87 AJ6 CYS D 844 LEU D 863 1 20
SHEET 1 AA1 4 HIS A 54 GLN A 60 0
SHEET 2 AA1 4 HIS A 68 GLY A 76 -1 O LEU A 75 N HIS A 54
SHEET 3 AA1 4 SER A 85 PRO A 92 -1 O LEU A 87 N TYR A 74
SHEET 4 AA1 4 LYS A 106 GLN A 107 -1 O LYS A 106 N TYR A 88
SHEET 1 AA2 4 ASP A 143 HIS A 145 0
SHEET 2 AA2 4 LEU A 150 ALA A 155 -1 O LEU A 152 N ASP A 143
SHEET 3 AA2 4 SER A 158 ARG A 163 -1 O CYS A 162 N PHE A 151
SHEET 4 AA2 4 LEU A 178 GLU A 179 -1 O LEU A 178 N HIS A 161
SHEET 1 AA3 4 MET A 189 ILE A 193 0
SHEET 2 AA3 4 PHE A 200 ASN A 205 -1 O ILE A 204 N MET A 189
SHEET 3 AA3 4 ASP A 208 ASN A 213 -1 O TRP A 210 N PHE A 203
SHEET 4 AA3 4 GLU A 219 ARG A 221 -1 O ARG A 220 N VAL A 211
SHEET 1 AA4 3 LYS A 237 ALA A 239 0
SHEET 2 AA4 3 LYS A 271 ASP A 281 -1 O VAL A 280 N SER A 238
SHEET 3 AA4 3 TYR A 256 TRP A 258 -1 N TRP A 257 O LEU A 276
SHEET 1 AA5 5 LYS A 237 ALA A 239 0
SHEET 2 AA5 5 LYS A 271 ASP A 281 -1 O VAL A 280 N SER A 238
SHEET 3 AA5 5 LYS A 314 THR A 324 -1 O ALA A 320 N ILE A 275
SHEET 4 AA5 5 ILE A 330 LEU A 338 -1 O LYS A 336 N LEU A 319
SHEET 5 AA5 5 PHE A 386 PRO A 388 -1 O ILE A 387 N GLU A 337
SHEET 1 AA6 2 VAL A 287 PRO A 291 0
SHEET 2 AA6 2 THR A 300 ARG A 304 -1 O ASP A 301 N VAL A 290
SHEET 1 AA7 4 TYR A 351 TRP A 357 0
SHEET 2 AA7 4 ALA A 364 LEU A 369 -1 O MET A 367 N ARG A 354
SHEET 3 AA7 4 TRP A 375 LEU A 381 -1 O LEU A 381 N ALA A 364
SHEET 4 AA7 4 TYR A 410 VAL A 416 -1 O GLU A 415 N LEU A 376
SHEET 1 AA8 4 PHE A 427 PRO A 429 0
SHEET 2 AA8 4 GLU A 438 ASN A 445 -1 O LEU A 442 N TYR A 428
SHEET 3 AA8 4 HIS A 453 VAL A 460 -1 O VAL A 457 N PHE A 441
SHEET 4 AA8 4 ILE A 483 ALA A 488 -1 O ILE A 487 N LYS A 456
SHEET 1 AA9 4 TRP A 505 ASN A 507 0
SHEET 2 AA9 4 LEU A 512 GLY A 517 -1 O TYR A 514 N TRP A 505
SHEET 3 AA9 4 HIS A 526 SER A 531 -1 O TYR A 528 N PHE A 515
SHEET 4 AA9 4 VAL A 539 ARG A 540 -1 O VAL A 539 N VAL A 529
SHEET 1 AB1 4 SER A 547 MET A 552 0
SHEET 2 AB1 4 MET A 558 SER A 564 -1 O HIS A 562 N SER A 549
SHEET 3 AB1 4 CYS A 571 SER A 578 -1 O TYR A 575 N PHE A 559
SHEET 4 AB1 4 GLN A 588 MET A 596 -1 O GLN A 588 N SER A 578
SHEET 1 AB2 8 GLU A 609 HIS A 614 0
SHEET 2 AB2 8 ARG A 620 TYR A 626 -1 O ILE A 625 N GLU A 609
SHEET 3 AB2 8 ALA A 673 ASP A 678 -1 O VAL A 674 N TYR A 626
SHEET 4 AB2 8 HIS A 637 PHE A 642 1 N VAL A 640 O ALA A 673
SHEET 5 AB2 8 ILE A 719 TRP A 729 1 O ALA A 725 N LEU A 641
SHEET 6 AB2 8 VAL A 749 GLY A 753 1 O GLY A 753 N GLY A 728
SHEET 7 AB2 8 LEU A 800 GLY A 805 1 O LEU A 801 N ALA A 752
SHEET 8 AB2 8 GLN A 831 TYR A 835 1 O GLN A 833 N ILE A 802
SHEET 1 AB3 5 ALA B 22 ARG B 23 0
SHEET 2 AB3 5 LYS B 635 PHE B 642 1 O LYS B 636 N ALA B 22
SHEET 3 AB3 5 ALA B 673 ASP B 678 1 O ALA B 673 N VAL B 640
SHEET 4 AB3 5 ARG B 620 TYR B 626 -1 N TYR B 626 O VAL B 674
SHEET 5 AB3 5 GLU B 609 HIS B 614 -1 N GLU B 609 O ILE B 625
SHEET 1 AB4 6 ALA B 22 ARG B 23 0
SHEET 2 AB4 6 LYS B 635 PHE B 642 1 O LYS B 636 N ALA B 22
SHEET 3 AB4 6 ILE B 719 TRP B 729 1 O ALA B 725 N LEU B 641
SHEET 4 AB4 6 VAL B 749 GLY B 753 1 O GLY B 753 N GLY B 728
SHEET 5 AB4 6 LEU B 800 GLY B 805 1 O LEU B 801 N ALA B 752
SHEET 6 AB4 6 GLN B 831 TYR B 835 1 O GLN B 831 N ILE B 802
SHEET 1 AB5 4 HIS B 54 GLN B 60 0
SHEET 2 AB5 4 HIS B 68 GLY B 76 -1 O LEU B 75 N HIS B 54
SHEET 3 AB5 4 SER B 85 PRO B 92 -1 O LEU B 87 N TYR B 74
SHEET 4 AB5 4 LYS B 106 GLN B 107 -1 O LYS B 106 N TYR B 88
SHEET 1 AB6 4 ASP B 143 HIS B 145 0
SHEET 2 AB6 4 LEU B 150 ALA B 155 -1 O LEU B 152 N ASP B 143
SHEET 3 AB6 4 SER B 158 ARG B 163 -1 O CYS B 162 N PHE B 151
SHEET 4 AB6 4 LEU B 178 GLU B 179 -1 O LEU B 178 N HIS B 161
SHEET 1 AB7 4 MET B 189 ILE B 193 0
SHEET 2 AB7 4 PHE B 200 ASN B 205 -1 O ILE B 204 N MET B 189
SHEET 3 AB7 4 ASP B 208 ASN B 213 -1 O TRP B 210 N PHE B 203
SHEET 4 AB7 4 GLU B 219 ARG B 221 -1 O ARG B 220 N VAL B 211
SHEET 1 AB8 3 LYS B 237 ALA B 239 0
SHEET 2 AB8 3 LYS B 271 ASP B 281 -1 O VAL B 280 N SER B 238
SHEET 3 AB8 3 TYR B 256 TRP B 258 -1 N TRP B 257 O LEU B 276
SHEET 1 AB9 5 LYS B 237 ALA B 239 0
SHEET 2 AB9 5 LYS B 271 ASP B 281 -1 O VAL B 280 N SER B 238
SHEET 3 AB9 5 LYS B 314 THR B 324 -1 O ALA B 320 N ILE B 275
SHEET 4 AB9 5 ILE B 330 LEU B 338 -1 O LYS B 336 N LEU B 319
SHEET 5 AB9 5 PHE B 386 PRO B 388 -1 O ILE B 387 N GLU B 337
SHEET 1 AC1 2 VAL B 287 PRO B 291 0
SHEET 2 AC1 2 THR B 300 ARG B 304 -1 O ASP B 301 N VAL B 290
SHEET 1 AC2 4 TYR B 351 TRP B 357 0
SHEET 2 AC2 4 ALA B 364 LEU B 369 -1 O MET B 367 N ARG B 354
SHEET 3 AC2 4 TRP B 375 LEU B 381 -1 O LEU B 381 N ALA B 364
SHEET 4 AC2 4 TYR B 410 VAL B 416 -1 O GLU B 415 N LEU B 376
SHEET 1 AC3 4 PHE B 427 PRO B 429 0
SHEET 2 AC3 4 GLU B 438 ASN B 445 -1 O LEU B 442 N TYR B 428
SHEET 3 AC3 4 HIS B 453 VAL B 460 -1 O VAL B 457 N PHE B 441
SHEET 4 AC3 4 ILE B 483 ALA B 488 -1 O GLU B 485 N THR B 458
SHEET 1 AC4 4 TRP B 505 ASN B 507 0
SHEET 2 AC4 4 LEU B 512 GLY B 517 -1 O TYR B 514 N TRP B 505
SHEET 3 AC4 4 HIS B 526 SER B 531 -1 O TYR B 528 N PHE B 515
SHEET 4 AC4 4 VAL B 539 ARG B 540 -1 O VAL B 539 N VAL B 529
SHEET 1 AC5 4 SER B 547 MET B 552 0
SHEET 2 AC5 4 MET B 558 SER B 564 -1 O HIS B 562 N SER B 549
SHEET 3 AC5 4 CYS B 571 SER B 578 -1 O TYR B 575 N PHE B 559
SHEET 4 AC5 4 GLN B 588 MET B 596 -1 O ARG B 590 N LYS B 576
SHEET 1 AC6 5 ALA C 22 ARG C 23 0
SHEET 2 AC6 5 LYS C 635 PHE C 642 1 O LYS C 636 N ALA C 22
SHEET 3 AC6 5 ALA C 673 ASP C 678 1 O ALA C 673 N VAL C 640
SHEET 4 AC6 5 ARG C 620 TYR C 626 -1 N TYR C 626 O VAL C 674
SHEET 5 AC6 5 GLU C 609 HIS C 614 -1 N GLU C 609 O ILE C 625
SHEET 1 AC7 6 ALA C 22 ARG C 23 0
SHEET 2 AC7 6 LYS C 635 PHE C 642 1 O LYS C 636 N ALA C 22
SHEET 3 AC7 6 ILE C 719 TRP C 729 1 O ALA C 725 N LEU C 641
SHEET 4 AC7 6 VAL C 749 GLY C 753 1 O GLY C 753 N GLY C 728
SHEET 5 AC7 6 LEU C 800 GLY C 805 1 O LEU C 801 N ALA C 752
SHEET 6 AC7 6 GLN C 831 TYR C 835 1 O GLN C 831 N ILE C 802
SHEET 1 AC8 4 HIS C 54 GLN C 60 0
SHEET 2 AC8 4 HIS C 68 GLY C 76 -1 O LEU C 75 N HIS C 54
SHEET 3 AC8 4 SER C 85 PRO C 92 -1 O LEU C 87 N TYR C 74
SHEET 4 AC8 4 LYS C 106 GLN C 107 -1 O LYS C 106 N TYR C 88
SHEET 1 AC9 4 ASP C 143 HIS C 145 0
SHEET 2 AC9 4 LEU C 150 ALA C 155 -1 O LEU C 152 N ASP C 143
SHEET 3 AC9 4 SER C 158 ARG C 163 -1 O CYS C 162 N PHE C 151
SHEET 4 AC9 4 LEU C 178 GLU C 179 -1 O LEU C 178 N HIS C 161
SHEET 1 AD1 4 MET C 189 ILE C 193 0
SHEET 2 AD1 4 PHE C 200 ASN C 205 -1 O ILE C 204 N MET C 189
SHEET 3 AD1 4 ASP C 208 ASN C 213 -1 O TRP C 210 N PHE C 203
SHEET 4 AD1 4 GLU C 219 ARG C 221 -1 O ARG C 220 N VAL C 211
SHEET 1 AD2 3 LYS C 237 ALA C 239 0
SHEET 2 AD2 3 LYS C 271 ASP C 281 -1 O VAL C 280 N SER C 238
SHEET 3 AD2 3 TYR C 256 TRP C 258 -1 N TRP C 257 O LEU C 276
SHEET 1 AD3 5 LYS C 237 ALA C 239 0
SHEET 2 AD3 5 LYS C 271 ASP C 281 -1 O VAL C 280 N SER C 238
SHEET 3 AD3 5 LYS C 314 THR C 324 -1 O ALA C 320 N ILE C 275
SHEET 4 AD3 5 ILE C 330 LEU C 338 -1 O LYS C 336 N LEU C 319
SHEET 5 AD3 5 PHE C 386 PRO C 388 -1 O ILE C 387 N GLU C 337
SHEET 1 AD4 2 VAL C 287 PRO C 291 0
SHEET 2 AD4 2 THR C 300 ARG C 304 -1 O ASP C 301 N VAL C 290
SHEET 1 AD5 4 TYR C 351 TRP C 357 0
SHEET 2 AD5 4 ALA C 364 LEU C 369 -1 O MET C 367 N ARG C 354
SHEET 3 AD5 4 TRP C 375 LEU C 381 -1 O GLN C 377 N PHE C 368
SHEET 4 AD5 4 TYR C 410 VAL C 416 -1 O GLU C 415 N LEU C 376
SHEET 1 AD6 4 PHE C 427 PRO C 429 0
SHEET 2 AD6 4 GLU C 438 ASN C 445 -1 O LEU C 442 N TYR C 428
SHEET 3 AD6 4 HIS C 453 VAL C 460 -1 O VAL C 457 N PHE C 441
SHEET 4 AD6 4 ILE C 483 ALA C 488 -1 O GLU C 485 N THR C 458
SHEET 1 AD7 4 TRP C 505 ASN C 507 0
SHEET 2 AD7 4 LEU C 512 GLY C 517 -1 O TYR C 514 N TRP C 505
SHEET 3 AD7 4 HIS C 526 SER C 531 -1 O TYR C 528 N PHE C 515
SHEET 4 AD7 4 VAL C 539 ARG C 540 -1 O VAL C 539 N VAL C 529
SHEET 1 AD8 4 SER C 547 MET C 552 0
SHEET 2 AD8 4 MET C 558 SER C 565 -1 O HIS C 562 N SER C 549
SHEET 3 AD8 4 THR C 568 SER C 578 -1 O TYR C 575 N PHE C 559
SHEET 4 AD8 4 GLN C 588 MET C 596 -1 O GLN C 588 N SER C 578
SHEET 1 AD9 4 HIS D 54 GLN D 60 0
SHEET 2 AD9 4 HIS D 68 GLY D 76 -1 O LEU D 75 N HIS D 54
SHEET 3 AD9 4 SER D 85 PRO D 92 -1 O LEU D 87 N TYR D 74
SHEET 4 AD9 4 LYS D 106 GLN D 107 -1 O LYS D 106 N TYR D 88
SHEET 1 AE1 4 ASP D 143 HIS D 145 0
SHEET 2 AE1 4 LEU D 150 ALA D 155 -1 O LEU D 152 N ASP D 143
SHEET 3 AE1 4 SER D 158 ARG D 163 -1 O CYS D 162 N PHE D 151
SHEET 4 AE1 4 LEU D 178 GLU D 179 -1 O LEU D 178 N HIS D 161
SHEET 1 AE2 4 MET D 189 ILE D 193 0
SHEET 2 AE2 4 PHE D 200 ASN D 205 -1 O ILE D 204 N MET D 189
SHEET 3 AE2 4 ASP D 208 ASN D 213 -1 O TRP D 210 N PHE D 203
SHEET 4 AE2 4 GLU D 219 ARG D 221 -1 O ARG D 220 N VAL D 211
SHEET 1 AE3 3 LYS D 237 ALA D 239 0
SHEET 2 AE3 3 LYS D 271 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE3 3 TYR D 256 TRP D 258 -1 N TRP D 257 O LEU D 276
SHEET 1 AE4 5 LYS D 237 ALA D 239 0
SHEET 2 AE4 5 LYS D 271 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE4 5 LYS D 314 THR D 324 -1 O ALA D 320 N ILE D 275
SHEET 4 AE4 5 ILE D 330 LEU D 338 -1 O LYS D 336 N LEU D 319
SHEET 5 AE4 5 PHE D 386 PRO D 388 -1 O ILE D 387 N GLU D 337
SHEET 1 AE5 2 VAL D 287 PRO D 291 0
SHEET 2 AE5 2 THR D 300 ARG D 304 -1 O ASP D 301 N VAL D 290
SHEET 1 AE6 4 TYR D 351 TRP D 357 0
SHEET 2 AE6 4 ALA D 364 LEU D 369 -1 O MET D 367 N ARG D 354
SHEET 3 AE6 4 TRP D 375 LEU D 381 -1 O GLN D 377 N PHE D 368
SHEET 4 AE6 4 TYR D 410 VAL D 416 -1 O GLU D 415 N LEU D 376
SHEET 1 AE7 4 PHE D 427 PRO D 429 0
SHEET 2 AE7 4 GLU D 438 ASN D 445 -1 O LEU D 442 N TYR D 428
SHEET 3 AE7 4 HIS D 453 VAL D 460 -1 O VAL D 457 N PHE D 441
SHEET 4 AE7 4 ILE D 483 ALA D 488 -1 O GLU D 485 N THR D 458
SHEET 1 AE8 4 TRP D 505 ASN D 507 0
SHEET 2 AE8 4 LEU D 512 GLY D 517 -1 O TYR D 514 N TRP D 505
SHEET 3 AE8 4 HIS D 526 SER D 531 -1 O TYR D 528 N PHE D 515
SHEET 4 AE8 4 VAL D 539 ARG D 540 -1 O VAL D 539 N VAL D 529
SHEET 1 AE9 4 SER D 547 MET D 552 0
SHEET 2 AE9 4 MET D 558 SER D 565 -1 O HIS D 562 N SER D 549
SHEET 3 AE9 4 THR D 568 SER D 578 -1 O TYR D 575 N PHE D 559
SHEET 4 AE9 4 GLN D 588 MET D 596 -1 O GLN D 588 N SER D 578
SHEET 1 AF1 8 GLU D 609 HIS D 614 0
SHEET 2 AF1 8 ARG D 620 TYR D 626 -1 O ILE D 625 N GLU D 609
SHEET 3 AF1 8 ALA D 673 ASP D 678 -1 O VAL D 674 N TYR D 626
SHEET 4 AF1 8 HIS D 637 PHE D 642 1 N VAL D 640 O ALA D 673
SHEET 5 AF1 8 ILE D 719 TRP D 729 1 O ALA D 725 N LEU D 641
SHEET 6 AF1 8 VAL D 749 GLY D 753 1 O GLY D 753 N GLY D 728
SHEET 7 AF1 8 LEU D 800 GLY D 805 1 O LEU D 801 N ALA D 752
SHEET 8 AF1 8 GLN D 831 TYR D 835 1 O GLN D 831 N ILE D 802
LINK OG SER A 730 C KBO A 901 1555 1555 1.45
LINK C ARG A 843 N CSO A 844 1555 1555 1.34
LINK C CSO A 844 N PRO A 845 1555 1555 1.35
LINK OG SER B 730 C KBO B 901 1555 1555 1.45
LINK OG SER C 730 C KBO C 901 1555 1555 1.46
LINK C ARG C 843 N CSO C 844 1555 1555 1.34
LINK C CSO C 844 N PRO C 845 1555 1555 1.36
LINK OG SER D 730 C KBO D 901 1555 1555 1.44
CRYST1 88.350 106.176 121.127 65.25 70.43 75.86 P 1 2
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 0.011319 -0.002850 -0.003199 0.00000
SCALE2 0.000000 0.009712 -0.003852 0.00000
SCALE3 0.000000 0.000000 0.009426 0.00000
TER 6855 HIS A 865
TER 13711 HIS B 865
TER 20593 HIS C 865
TER 27424 HIS D 865
MASTER 569 0 50 87 190 0 0 629184 4 343 264
END |