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HEADER HYDROLASE 21-SEP-09 3JYH
TITLE HUMAN DIPEPTIDYL PEPTIDASE DPP7
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
COMPND 6 AMINOPEPTIDASE II, QUIESCENT CELL PROLINE DIPEPTIDASE,
COMPND 7 DIPEPTIDYL PEPTIDASE 7;
COMPND 8 EC: 3.4.14.2;
COMPND 9 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_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9 INSECT CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PFHMSP-LIC-N
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 AMINOPEPTIDASE, CLEAVAGE ON PAIR OF BASIC RESIDUES,
KEYWDS 3 CYTOPLASMIC VESICLE, GLYCOPROTEIN, HYDROLASE, LYSOSOME,
KEYWDS 4 POLYMORPHISM, PROTEASE, SERINE PROTEASE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DOBROVETSKY,A.DONG,A.SEITOVA,L.CROMBETT,S.PAGANON,
AUTHOR 2 D.COSSAR,A.M.EDWARDS,C.H.ARROWSMITH,C.BOUNTRA,J.WEIGELT,
AUTHOR 3 A.HASSEL,L.SHEWCHUK,A.BOCHKAREV,STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (SGC)
REVDAT 1 13-OCT-09 3JYH 0
JRNL AUTH E.DOBROVETSKY,A.DONG,A.SEITOVA,L.CROMBETT,
JRNL AUTH 2 S.PAGANON,D.COSSAR,A.M.EDWARDS,C.H.ARROWSMITH,
JRNL AUTH 3 C.BOUNTRA,J.WEIGELT,A.HASSEL,L.SHEWCHUK,A.BOCHKAREV
JRNL TITL HUMAN DIPEPTIDYL PEPTIDASE DPP7
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 127511
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6400
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7870
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 392
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13857
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 341
REMARK 3 SOLVENT ATOMS : 946
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.96000
REMARK 3 B22 (A**2) : -1.36000
REMARK 3 B33 (A**2) : -0.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.43000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.201
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.175
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.714
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14632 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19969 ; 1.346 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1803 ; 5.860 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 679 ;33.572 ;23.108
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1998 ;13.188 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 103 ;18.862 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2168 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11418 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6821 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9977 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1073 ; 0.147 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 47 ; 0.167 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.162 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9137 ; 0.732 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14193 ; 1.271 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6281 ; 1.875 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5775 ; 2.904 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3JYH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB055318.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127772
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11100
REMARK 200 FOR THE DATA SET : 25.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
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 65.10750
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31530 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.9 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 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 ASP A 28 CG OD1 OD2
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 ARG A 203 NE CZ NH1 NH2
REMARK 470 GLN A 212 CG CD OE1 NE2
REMARK 470 LYS A 215 CE NZ
REMARK 470 GLN A 218 CG CD OE1 NE2
REMARK 470 GLU A 252 CG CD OE1 OE2
REMARK 470 LYS A 253 CE NZ
REMARK 470 ARG A 327 NE CZ NH1 NH2
REMARK 470 ARG A 380 CZ NH1 NH2
REMARK 470 ARG A 427 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 439 CD OE1 NE2
REMARK 470 LYS A 463 CD CE NZ
REMARK 470 GLU A 471 CD OE1 OE2
REMARK 470 LYS A 474 CG CD CE NZ
REMARK 470 ARG A 477 CZ NH1 NH2
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 GLU B 97 CD OE1 OE2
REMARK 470 ARG B 98 CD NE CZ NH1 NH2
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 GLU B 252 CG CD OE1 OE2
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 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 66 NE CZ NH1 NH2
REMARK 470 GLU C 68 CG CD OE1 OE2
REMARK 470 ALA C 89 CB
REMARK 470 GLU C 97 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 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 ASP D 28 CG OD1 OD2
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 LYS D 112 CD CE NZ
REMARK 470 GLN D 119 CG CD OE1 NE2
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 653 O HOH A 1230 2.12
REMARK 500 O HOH B 628 O HOH B 667 2.12
REMARK 500 NE2 GLN D 247 OD1 ASP D 324 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 66 -10.40 -49.15
REMARK 500 ASN A 77 -142.92 -107.92
REMARK 500 TYR A 109 -1.40 77.11
REMARK 500 SER A 113 73.54 -104.42
REMARK 500 ALA A 151 48.11 -149.54
REMARK 500 SER A 162 -136.41 66.62
REMARK 500 SER A 213 108.73 -164.00
REMARK 500 SER A 250 -23.87 -156.86
REMARK 500 PHE A 280 -76.57 -92.17
REMARK 500 ASN A 315 45.51 -146.69
REMARK 500 THR A 353 -66.69 -128.93
REMARK 500 VAL A 364 -58.00 -120.76
REMARK 500 TRP A 400 -8.11 85.61
REMARK 500 ALA A 442 -133.95 -95.00
REMARK 500 HIS A 444 53.39 33.24
REMARK 500 ASN B 77 -146.86 -106.36
REMARK 500 TYR B 109 -0.72 76.27
REMARK 500 SER B 162 -138.33 71.72
REMARK 500 SER B 213 115.38 -166.63
REMARK 500 SER B 250 -32.17 -149.79
REMARK 500 ASP B 279 64.68 -152.91
REMARK 500 PHE B 280 -75.29 -95.33
REMARK 500 ASN B 315 40.47 -142.52
REMARK 500 THR B 353 -68.44 -134.19
REMARK 500 TRP B 400 -1.86 87.04
REMARK 500 ALA B 442 -134.46 -92.05
REMARK 500 HIS B 444 53.33 36.15
REMARK 500 ARG C 66 -4.99 -54.73
REMARK 500 ASN C 77 -141.85 -110.11
REMARK 500 GLU C 78 45.01 -84.48
REMARK 500 SER C 88 50.19 -101.31
REMARK 500 TYR C 109 -1.52 80.45
REMARK 500 SER C 113 75.31 -104.48
REMARK 500 ALA C 151 56.14 -69.84
REMARK 500 SER C 162 -132.10 70.42
REMARK 500 SER C 250 -39.21 -145.04
REMARK 500 ASP C 279 63.78 -151.66
REMARK 500 PHE C 280 -72.86 -90.15
REMARK 500 ASN C 315 45.31 -144.37
REMARK 500 THR C 353 -65.33 -127.94
REMARK 500 TRP C 400 -8.90 81.13
REMARK 500 ALA C 442 -137.22 -92.48
REMARK 500 HIS C 444 60.39 28.84
REMARK 500 ARG D 62 -39.92 -35.64
REMARK 500 ARG D 66 -1.14 -48.08
REMARK 500 ASN D 77 -147.77 -116.81
REMARK 500 GLU D 78 46.84 -73.37
REMARK 500 SER D 88 53.36 -112.05
REMARK 500 TYR D 109 -3.08 74.61
REMARK 500 SER D 162 -135.61 68.47
REMARK 500 ALA D 235 55.85 -94.04
REMARK 500 MET D 272 35.98 -93.41
REMARK 500 PHE D 280 -66.32 -92.89
REMARK 500 ASN D 315 47.43 -151.35
REMARK 500 THR D 353 -67.23 -129.62
REMARK 500 VAL D 364 -53.01 -120.66
REMARK 500 TRP D 400 -9.15 84.46
REMARK 500 ALA D 442 -138.62 -80.44
REMARK 500 HIS D 444 68.33 22.93
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 D1140 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH D1204 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH B 953 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH B1018 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH B1058 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH B1212 DISTANCE = 7.11 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 493
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 494
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 498
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 495
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 496
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 497
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 493
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 494
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 497
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 495
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 496
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C 1
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 493
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 498
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 494
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 495
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 496
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 497
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 493
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 494
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 495
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 496
DBREF 3JYH A 28 492 UNP Q9UHL4 DPP2_HUMAN 28 492
DBREF 3JYH B 28 492 UNP Q9UHL4 DPP2_HUMAN 28 492
DBREF 3JYH C 28 492 UNP Q9UHL4 DPP2_HUMAN 28 492
DBREF 3JYH D 28 492 UNP Q9UHL4 DPP2_HUMAN 28 492
SEQADV 3JYH GLY A 24 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH ALA A 25 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH MET A 26 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH ASP A 27 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH GLY B 24 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH ALA B 25 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH MET B 26 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH ASP B 27 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH GLY C 24 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH ALA C 25 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH MET C 26 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH ASP C 27 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH GLY D 24 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH ALA D 25 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH MET D 26 UNP Q9UHL4 EXPRESSION TAG
SEQADV 3JYH 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
MODRES 3JYH ASN A 50 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN A 86 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN A 315 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN A 363 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN B 86 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN B 315 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN B 363 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN C 50 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN C 86 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN C 315 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN C 363 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN D 86 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN D 315 ASN GLYCOSYLATION SITE
MODRES 3JYH ASN D 363 ASN GLYCOSYLATION SITE
HET NAG A 1 14
HET BMA A 493 11
HET NAG A 494 14
HET NAG A 498 14
HET NAG A 495 14
HET NAG A 496 14
HET NAG A 497 14
HET NAG B 1 14
HET BMA B 493 11
HET NAG B 494 14
HET NAG B 497 14
HET NAG B 495 14
HET NAG B 496 14
HET BMA C 1 11
HET NAG C 493 14
HET NAG C 498 14
HET NAG C 494 14
HET NAG C 495 14
HET NAG C 496 14
HET NAG C 497 14
HET NAG D 1 14
HET NAG D 493 14
HET NAG D 494 14
HET NAG D 495 14
HET NAG D 496 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETSYN NAG NAG
FORMUL 5 NAG 22(C8 H15 N O6)
FORMUL 6 BMA 3(C6 H12 O6)
FORMUL 19 HOH *946(H2 O)
HELIX 1 1 ASP A 80 SER A 88 1 9
HELIX 2 2 SER A 88 GLY A 99 1 12
HELIX 3 3 PHE A 116 GLN A 122 5 7
HELIX 4 4 THR A 130 LEU A 149 1 20
HELIX 5 5 SER A 162 TYR A 175 1 14
HELIX 6 6 LEU A 190 GLY A 194 5 5
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 ASP A 324 TYR A 329 1 6
HELIX 14 14 GLY A 341 CYS A 352 1 12
HELIX 15 15 THR A 374 GLY A 387 1 14
HELIX 16 16 ASP A 393 TRP A 400 1 8
HELIX 17 17 ASP A 418 GLY A 424 5 7
HELIX 18 18 HIS A 444 ARG A 448 5 5
HELIX 19 19 PRO A 455 GLU A 479 1 25
HELIX 20 20 ASP B 80 SER B 88 1 9
HELIX 21 21 SER B 88 GLY B 99 1 12
HELIX 22 22 PHE B 116 GLN B 122 5 7
HELIX 23 23 THR B 130 LEU B 149 1 20
HELIX 24 24 SER B 162 TYR B 175 1 14
HELIX 25 25 LEU B 190 GLY B 194 5 5
HELIX 26 26 ASN B 199 SER B 213 1 15
HELIX 27 27 SER B 213 GLN B 233 1 21
HELIX 28 28 ALA B 235 GLY B 244 1 10
HELIX 29 29 ASP B 251 MET B 272 1 22
HELIX 30 30 ASN B 287 SER B 298 1 12
HELIX 31 31 GLN B 301 ASN B 315 1 15
HELIX 32 32 ASP B 324 TYR B 329 1 6
HELIX 33 33 GLY B 341 CYS B 352 1 12
HELIX 34 34 THR B 374 GLY B 387 1 14
HELIX 35 35 ASP B 393 TRP B 400 1 8
HELIX 36 36 TRP B 420 GLY B 424 5 5
HELIX 37 37 HIS B 444 ARG B 448 5 5
HELIX 38 38 PRO B 455 GLU B 479 1 25
HELIX 39 39 ASP C 80 SER C 88 1 9
HELIX 40 40 SER C 88 GLY C 99 1 12
HELIX 41 41 PHE C 116 GLN C 122 5 7
HELIX 42 42 HIS C 125 LEU C 129 5 5
HELIX 43 43 THR C 130 LEU C 149 1 20
HELIX 44 44 SER C 162 TYR C 175 1 14
HELIX 45 45 LEU C 190 GLY C 194 5 5
HELIX 46 46 ASN C 199 SER C 213 1 15
HELIX 47 47 SER C 213 GLN C 233 1 21
HELIX 48 48 ALA C 235 GLY C 244 1 10
HELIX 49 49 ASP C 251 MET C 272 1 22
HELIX 50 50 ASN C 287 LEU C 297 1 11
HELIX 51 51 GLN C 301 ASN C 315 1 15
HELIX 52 52 GLY C 341 CYS C 352 1 12
HELIX 53 53 THR C 374 GLY C 387 1 14
HELIX 54 54 ASP C 393 TRP C 400 1 8
HELIX 55 55 TRP C 420 GLY C 424 5 5
HELIX 56 56 HIS C 444 ARG C 448 5 5
HELIX 57 57 PRO C 455 ARG C 477 1 23
HELIX 58 58 ASP D 80 SER D 88 1 9
HELIX 59 59 SER D 88 GLY D 99 1 12
HELIX 60 60 PHE D 116 GLN D 122 5 7
HELIX 61 61 THR D 130 GLY D 150 1 21
HELIX 62 62 SER D 162 TYR D 175 1 14
HELIX 63 63 PRO D 188 ALA D 193 1 6
HELIX 64 64 ASN D 199 SER D 213 1 15
HELIX 65 65 SER D 213 GLN D 233 1 21
HELIX 66 66 ALA D 235 GLY D 244 1 10
HELIX 67 67 ASP D 251 MET D 272 1 22
HELIX 68 68 ASN D 287 SER D 298 1 12
HELIX 69 69 GLN D 301 ASN D 315 1 15
HELIX 70 70 ASP D 324 TYR D 329 1 6
HELIX 71 71 GLY D 341 CYS D 352 1 12
HELIX 72 72 THR D 374 GLY D 387 1 14
HELIX 73 73 ASP D 393 TRP D 400 1 8
HELIX 74 74 ASP D 418 GLY D 424 5 7
HELIX 75 75 HIS D 444 ARG D 448 5 5
HELIX 76 76 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 53 N GLN A 38
SHEET 3 A 8 LEU A 101 ALA A 105 -1 O PHE A 104 N LEU A 58
SHEET 4 A 8 ILE A 71 THR A 75 1 N PHE A 72 O LEU A 101
SHEET 5 A 8 ALA A 156 GLY A 161 1 O ILE A 157 N PHE A 73
SHEET 6 A 8 GLY A 181 ALA A 185 1 O ALA A 185 N GLY A 160
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 PHE B 53 N GLN B 38
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 ILE B 157 N PHE B 73
SHEET 6 C 8 GLY B 181 ALA B 185 1 O LEU B 183 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 PHE C 72 O LEU C 101
SHEET 5 E 8 ALA C 156 GLY C 161 1 O PHE C 159 N THR C 75
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 PHE D 159 N PHE D 73
SHEET 6 G 8 GLY D 181 ALA D 185 1 O ALA D 185 N GLY D 160
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 216 CYS A 293 1555 1555 2.09
SSBOND 2 CYS A 246 CYS A 322 1555 1555 2.08
SSBOND 3 CYS A 332 CYS A 338 1555 1555 2.05
SSBOND 4 CYS A 352 CYS A 382 1555 1555 2.04
SSBOND 5 CYS B 216 CYS B 293 1555 1555 2.07
SSBOND 6 CYS B 246 CYS B 322 1555 1555 2.06
SSBOND 7 CYS B 332 CYS B 338 1555 1555 2.03
SSBOND 8 CYS B 352 CYS B 382 1555 1555 2.04
SSBOND 9 CYS C 216 CYS C 293 1555 1555 2.08
SSBOND 10 CYS C 246 CYS C 322 1555 1555 2.07
SSBOND 11 CYS C 332 CYS C 338 1555 1555 2.06
SSBOND 12 CYS C 352 CYS C 382 1555 1555 2.08
SSBOND 13 CYS D 216 CYS D 293 1555 1555 2.04
SSBOND 14 CYS D 246 CYS D 322 1555 1555 2.10
SSBOND 15 CYS D 332 CYS D 338 1555 1555 2.02
SSBOND 16 CYS D 352 CYS D 382 1555 1555 2.04
LINK ND2 ASN A 50 C1 NAG A 495 1555 1555 1.45
LINK ND2 ASN A 86 C1 NAG A 1 1555 1555 1.45
LINK ND2 ASN A 315 C1 NAG A 496 1555 1555 1.44
LINK ND2 ASN A 363 C1 NAG A 498 1555 1555 1.45
LINK ND2 ASN B 86 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN B 315 C1 NAG B 495 1555 1555 1.45
LINK ND2 ASN B 363 C1 NAG B 497 1555 1555 1.44
LINK ND2 ASN C 50 C1 NAG C 494 1555 1555 1.45
LINK ND2 ASN C 86 C1 NAG C 495 1555 1555 1.44
LINK ND2 ASN C 315 C1 NAG C 496 1555 1555 1.43
LINK ND2 ASN C 363 C1 NAG C 498 1555 1555 1.46
LINK ND2 ASN D 86 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN D 315 C1 NAG D 495 1555 1555 1.45
LINK ND2 ASN D 363 C1 NAG D 493 1555 1555 1.44
LINK C1 BMA C 1 O4 NAG C 493 1555 1555 1.48
LINK C1 NAG C 493 O4 NAG C 498 1555 1555 1.46
LINK C1 BMA A 493 O4 NAG A 494 1555 1555 1.45
LINK C1 NAG A 494 O4 NAG A 498 1555 1555 1.45
LINK C1 BMA B 493 O4 NAG B 494 1555 1555 1.46
LINK C1 NAG B 494 O4 NAG B 497 1555 1555 1.46
LINK O4 NAG B 495 C1 NAG B 496 1555 1555 1.45
LINK O4 NAG A 496 C1 NAG A 497 1555 1555 1.47
LINK O4 NAG C 496 C1 NAG C 497 1555 1555 1.46
LINK O4 NAG D 493 C1 NAG D 494 1555 1555 1.44
LINK O4 NAG D 495 C1 NAG D 496 1555 1555 1.45
CISPEP 1 ASP D 28 PRO D 29 0 27.57
SITE 1 AC1 3 TRP A 82 ALA A 83 ASN A 86
SITE 1 AC2 1 NAG A 494
SITE 1 AC3 5 ARG A 225 ASP A 229 BMA A 493 NAG A 498
SITE 2 AC3 5 HOH A 676
SITE 1 AC4 6 LYS A 228 ASN A 363 NAG A 494 HOH A 548
SITE 2 AC4 6 HOH A 584 HOH A 608
SITE 1 AC5 4 ASN A 50 HOH A 877 LEU B 383 TRP B 389
SITE 1 AC6 8 ARG A 307 ASN A 315 GLY A 318 GLU A 320
SITE 2 AC6 8 TYR A 323 NAG A 497 HOH A 581 HOH A1246
SITE 1 AC7 3 NAG A 496 HOH A 581 HOH A1119
SITE 1 AC8 3 TRP B 82 ALA B 83 ASN B 86
SITE 1 AC9 1 NAG B 494
SITE 1 BC1 6 ARG B 225 LYS B 228 ASP B 229 BMA B 493
SITE 2 BC1 6 NAG B 497 HOH B 563
SITE 1 BC2 6 ARG B 225 LYS B 228 ASN B 363 NAG B 494
SITE 2 BC2 6 HOH B 557 HOH B 582
SITE 1 BC3 10 ARG B 307 ASN B 315 GLY B 318 GLU B 320
SITE 2 BC3 10 CYS B 322 TYR B 323 NAG B 496 HOH B 516
SITE 3 BC3 10 HOH B 663 HOH B 922
SITE 1 BC4 2 NAG B 495 HOH B 663
SITE 1 BC5 2 ARG C 225 NAG C 493
SITE 1 BC6 6 BMA C 1 ARG C 225 LYS C 228 ASP C 229
SITE 2 BC6 6 NAG C 498 HOH C 586
SITE 1 BC7 7 PHE C 224 ARG C 225 LYS C 228 ASN C 363
SITE 2 BC7 7 NAG C 493 HOH C 540 HOH C 545
SITE 1 BC8 2 ASN C 50 TRP D 389
SITE 1 BC9 5 ASP C 80 TRP C 82 ALA C 83 ASN C 86
SITE 2 BC9 5 HOH C1252
SITE 1 CC1 9 ARG C 307 ASN C 315 GLY C 318 GLU C 320
SITE 2 CC1 9 HIS C 321 CYS C 322 TYR C 323 NAG C 497
SITE 3 CC1 9 HOH C 892
SITE 1 CC2 3 NAG C 496 HOH C 892 HOH C1201
SITE 1 CC3 3 TRP D 82 ASN D 86 HOH D1266
SITE 1 CC4 8 ARG D 221 PHE D 224 ARG D 225 LYS D 228
SITE 2 CC4 8 ASN D 363 NAG D 494 HOH D 497 HOH D 539
SITE 1 CC5 4 ARG D 225 ASP D 229 NAG D 493 HOH D 985
SITE 1 CC6 8 ARG D 307 ASN D 315 GLY D 318 GLU D 320
SITE 2 CC6 8 HIS D 321 CYS D 322 TYR D 323 NAG D 496
SITE 1 CC7 1 NAG D 495
CRYST1 80.216 130.215 124.436 90.00 102.36 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 0.012466 0.000000 0.002732 0.00000
SCALE2 0.000000 0.007680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008227 0.00000
TER 3473 GLU A 479
TER 6945 GLU B 479
TER 10413 ARG C 478
TER 13861 ARG D 477
MASTER 592 0 25 76 40 0 39 615144 4 387 148
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