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HEADER HYDROLASE/HYDROLASE INHIBITOR 03-JUN-16 5KBY
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH SYR-472
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ADABP,ADENOSINE DEAMINASE COMPLEXING PROTEIN 2,ADCP-2,
COMPND 5 DIPEPTIDYL PEPTIDASE IV,DPP IV,T-CELL ACTIVATION ANTIGEN CD26,TP103;
COMPND 6 EC: 3.4.14.5;
COMPND 7 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: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS PEPTIDASE, GLP-1, METABOLIC DISEASE, CO-COMPLEX, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.SKENE,A.J.JENNINGS
REVDAT 1 13-JUL-16 5KBY 0
JRNL AUTH C.E.GRIMSHAW,A.JENNINGS,R.KAMRAN,H.UENO,N.NISHIGAKI,
JRNL AUTH 2 T.KOSAKA,A.TANI,H.SANO,Y.KINUGAWA,E.KOUMURA,L.SHI,K.TAKEUCHI
JRNL TITL TRELAGLIPTIN (SYR-472, ZAFATEK), NOVEL ONCE-WEEKLY TREATMENT
JRNL TITL 2 FOR TYPE 2 DIABETES, INHIBITS DIPEPTIDYL PEPTIDASE-4 (DPP-4)
JRNL TITL 3 VIA A NON-COVALENT MECHANISM.
JRNL REF PLOS ONE V. 11 57509 2016
JRNL REFN ESSN 1932-6203
JRNL PMID 27328054
JRNL DOI 10.1371/JOURNAL.PONE.0157509
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0025
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) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 169608
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8950
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) : 2.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9615
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 520
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23764
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 482
REMARK 3 SOLVENT ATOMS : 1597
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.25000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.251
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.143
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.877
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25013 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 22439 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34056 ; 1.246 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 51455 ; 0.742 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2890 ; 6.411 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1228 ;34.006 ;23.901
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3974 ;15.866 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;18.489 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3629 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 28170 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 6128 ; 0.001 ; 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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 40 A 766
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4638 31.9998 18.7043
REMARK 3 T TENSOR
REMARK 3 T11: 0.0515 T22: 0.0575
REMARK 3 T33: 0.0934 T12: 0.0151
REMARK 3 T13: -0.0147 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 0.7121 L22: 0.1516
REMARK 3 L33: 0.2967 L12: 0.1281
REMARK 3 L13: -0.0354 L23: 0.0292
REMARK 3 S TENSOR
REMARK 3 S11: -0.0229 S12: -0.0766 S13: -0.1444
REMARK 3 S21: 0.0125 S22: -0.0025 S23: -0.0494
REMARK 3 S31: -0.0485 S32: 0.0688 S33: 0.0254
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 36 B 766
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4142 25.1979 20.1457
REMARK 3 T TENSOR
REMARK 3 T11: 0.0463 T22: 0.0542
REMARK 3 T33: 0.0895 T12: 0.0211
REMARK 3 T13: 0.0129 T23: 0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 0.9731 L22: 0.0557
REMARK 3 L33: 0.3068 L12: 0.0704
REMARK 3 L13: -0.1832 L23: 0.0197
REMARK 3 S TENSOR
REMARK 3 S11: -0.0440 S12: -0.0695 S13: -0.1415
REMARK 3 S21: -0.0143 S22: 0.0288 S23: 0.0030
REMARK 3 S31: -0.0595 S32: -0.0414 S33: 0.0152
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 40 C 766
REMARK 3 ORIGIN FOR THE GROUP (A): 90.5409 -29.1038 47.1054
REMARK 3 T TENSOR
REMARK 3 T11: 0.1217 T22: 0.1159
REMARK 3 T33: 0.0686 T12: -0.0406
REMARK 3 T13: -0.0173 T23: 0.0717
REMARK 3 L TENSOR
REMARK 3 L11: 1.1667 L22: 0.4700
REMARK 3 L33: 0.2914 L12: 0.3820
REMARK 3 L13: -0.1143 L23: -0.3352
REMARK 3 S TENSOR
REMARK 3 S11: 0.1107 S12: -0.2665 S13: -0.0825
REMARK 3 S21: -0.0027 S22: -0.2114 S23: -0.1301
REMARK 3 S31: -0.0258 S32: 0.1432 S33: 0.1007
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 40 D 766
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8530 -28.5261 33.4098
REMARK 3 T TENSOR
REMARK 3 T11: 0.0855 T22: 0.1284
REMARK 3 T33: 0.0525 T12: 0.0262
REMARK 3 T13: 0.0182 T23: 0.0594
REMARK 3 L TENSOR
REMARK 3 L11: 1.3572 L22: 0.0394
REMARK 3 L33: 0.2477 L12: 0.0639
REMARK 3 L13: 0.2542 L23: -0.0325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0486 S12: -0.0982 S13: 0.1140
REMARK 3 S21: -0.0026 S22: -0.0097 S23: -0.0088
REMARK 3 S31: -0.0152 S32: -0.1498 S33: -0.0389
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 : WITH TLS ADDED
REMARK 4
REMARK 4 5KBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222009.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-07
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 : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 178650
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
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: PHASER
REMARK 200 STARTING MODEL: 3G0B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.2% PEG MME 2000, 0.1M BICINE PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 61.08250
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, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 116990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 57.0 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 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 61.82021
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 61.08250
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 130.69217
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 ALA A 27
REMARK 465 ASP A 28
REMARK 465 PRO A 29
REMARK 465 GLY A 30
REMARK 465 GLY A 31
REMARK 465 SER A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 HIS A 37
REMARK 465 HIS A 38
REMARK 465 SER A 39
REMARK 465 GLU A 73
REMARK 465 ASN A 74
REMARK 465 ALA B 27
REMARK 465 ASP B 28
REMARK 465 PRO B 29
REMARK 465 GLY B 30
REMARK 465 GLY B 31
REMARK 465 SER B 32
REMARK 465 HIS B 33
REMARK 465 ALA C 27
REMARK 465 ASP C 28
REMARK 465 PRO C 29
REMARK 465 GLY C 30
REMARK 465 GLY C 31
REMARK 465 SER C 32
REMARK 465 HIS C 33
REMARK 465 HIS C 34
REMARK 465 HIS C 35
REMARK 465 HIS C 36
REMARK 465 HIS C 37
REMARK 465 HIS C 38
REMARK 465 SER C 39
REMARK 465 LYS C 71
REMARK 465 GLN C 72
REMARK 465 GLU C 73
REMARK 465 ASN C 74
REMARK 465 ASN C 75
REMARK 465 GLY C 84
REMARK 465 ASN C 85
REMARK 465 SER C 86
REMARK 465 SER C 87
REMARK 465 SER C 93
REMARK 465 ALA D 27
REMARK 465 ASP D 28
REMARK 465 PRO D 29
REMARK 465 GLY D 30
REMARK 465 GLY D 31
REMARK 465 SER D 32
REMARK 465 HIS D 33
REMARK 465 HIS D 34
REMARK 465 HIS D 35
REMARK 465 HIS D 36
REMARK 465 HIS D 37
REMARK 465 HIS D 38
REMARK 465 SER D 39
REMARK 465 GLU D 73
REMARK 465 ASN D 74
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 40 CG CD NE CZ NH1 NH2
REMARK 470 TYR D 70 N
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 OG SER D 552 O HOH D 1601 2.03
REMARK 500 O4 NAG C 1503 O HOH C 1601 2.15
REMARK 500 OG SER A 212 O HOH A 1601 2.17
REMARK 500 O HOH A 1904 O HOH A 1919 2.19
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 HIS A 66 14.30 -151.61
REMARK 500 PHE A 95 40.97 -101.24
REMARK 500 GLN A 123 -104.73 -100.06
REMARK 500 TRP A 124 -146.21 -91.25
REMARK 500 HIS A 162 30.61 -148.61
REMARK 500 ILE A 193 -56.62 -129.27
REMARK 500 SER A 242 -163.17 65.91
REMARK 500 GLN A 320 41.35 -87.62
REMARK 500 ASN A 450 78.17 -154.94
REMARK 500 GLN A 508 88.09 -68.59
REMARK 500 TYR A 547 -76.29 -116.16
REMARK 500 ARG A 597 44.53 -142.88
REMARK 500 THR A 600 -91.47 -121.61
REMARK 500 SER A 630 -124.95 67.79
REMARK 500 ASP A 678 -97.34 -118.09
REMARK 500 ASN A 710 -69.57 -102.30
REMARK 500 GLN A 714 -47.94 -28.75
REMARK 500 ASP A 739 -162.61 -106.24
REMARK 500 ILE A 742 55.29 38.58
REMARK 500 HIS B 37 21.68 49.80
REMARK 500 ASN B 74 -3.37 64.12
REMARK 500 GLN B 123 -95.48 -112.06
REMARK 500 TRP B 124 -143.79 -98.18
REMARK 500 HIS B 162 34.24 -149.89
REMARK 500 ILE B 193 -62.02 -124.69
REMARK 500 SER B 242 -166.81 68.73
REMARK 500 GLN B 320 43.50 -92.81
REMARK 500 ASN B 450 66.25 -165.67
REMARK 500 TYR B 547 -75.69 -117.21
REMARK 500 ARG B 597 47.15 -147.13
REMARK 500 THR B 600 -91.81 -120.20
REMARK 500 SER B 630 -122.16 64.93
REMARK 500 ASP B 678 -92.64 -109.89
REMARK 500 ASN B 710 -74.13 -94.92
REMARK 500 ASP B 739 -157.06 -104.03
REMARK 500 ILE B 742 55.94 33.00
REMARK 500 TRP C 62 99.91 -65.06
REMARK 500 PHE C 89 -24.79 -170.95
REMARK 500 GLU C 91 -58.63 -126.86
REMARK 500 GLN C 123 -100.23 -105.58
REMARK 500 TRP C 124 -146.00 -96.15
REMARK 500 ARG C 140 54.38 36.18
REMARK 500 ILE C 193 -58.96 -132.56
REMARK 500 SER C 242 -168.37 71.38
REMARK 500 SER C 275 39.90 -91.74
REMARK 500 THR C 307 -162.20 -129.92
REMARK 500 GLN C 320 40.62 -88.49
REMARK 500 ASN C 450 85.01 -158.79
REMARK 500 PRO C 531 152.94 -47.51
REMARK 500 TYR C 547 -75.62 -118.46
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2022 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH C1900 DISTANCE = 5.88 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6RL A 1510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6RL B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6RL C 1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6RL D 1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1509
REMARK 800 bound to ASN A 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 1501 through NAG A 1502 bound to ASN A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1503
REMARK 800 bound to ASN A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 1504 through NAG A 1505 bound to ASN A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 1506 through NAG A 1507 bound to ASN A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1508
REMARK 800 bound to ASN A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 801 bound
REMARK 800 to ASN B 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 802 bound
REMARK 800 to ASN B 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 807 bound
REMARK 800 to ASN B 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 803 through NAG B 804 bound to ASN B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 805 bound
REMARK 800 to ASN B 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 806 bound
REMARK 800 to ASN B 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1501
REMARK 800 bound to ASN C 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 1502 through NAG C 1503 bound to ASN C 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1504
REMARK 800 bound to ASN C 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 1501
REMARK 800 bound to ASN D 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 1502
REMARK 800 bound to ASN D 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 1503 through NAG D 1504 bound to ASN D 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 1505
REMARK 800 bound to ASN D 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 1506
REMARK 800 bound to ASN D 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5AX C 1505 and ASN C
REMARK 800 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5AX C 1505 and ASN C
REMARK 800 321
DBREF 5KBY A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 5KBY B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 5KBY C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 5KBY D 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 5KBY ALA A 27 UNP P27487 EXPRESSION TAG
SEQADV 5KBY ASP A 28 UNP P27487 EXPRESSION TAG
SEQADV 5KBY PRO A 29 UNP P27487 EXPRESSION TAG
SEQADV 5KBY GLY A 30 UNP P27487 EXPRESSION TAG
SEQADV 5KBY GLY A 31 UNP P27487 EXPRESSION TAG
SEQADV 5KBY SER A 32 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS A 33 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS A 34 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS A 35 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS A 36 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS A 37 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS A 38 UNP P27487 EXPRESSION TAG
SEQADV 5KBY ALA B 27 UNP P27487 EXPRESSION TAG
SEQADV 5KBY ASP B 28 UNP P27487 EXPRESSION TAG
SEQADV 5KBY PRO B 29 UNP P27487 EXPRESSION TAG
SEQADV 5KBY GLY B 30 UNP P27487 EXPRESSION TAG
SEQADV 5KBY GLY B 31 UNP P27487 EXPRESSION TAG
SEQADV 5KBY SER B 32 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS B 33 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS B 34 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS B 35 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS B 36 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS B 37 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS B 38 UNP P27487 EXPRESSION TAG
SEQADV 5KBY ALA C 27 UNP P27487 EXPRESSION TAG
SEQADV 5KBY ASP C 28 UNP P27487 EXPRESSION TAG
SEQADV 5KBY PRO C 29 UNP P27487 EXPRESSION TAG
SEQADV 5KBY GLY C 30 UNP P27487 EXPRESSION TAG
SEQADV 5KBY GLY C 31 UNP P27487 EXPRESSION TAG
SEQADV 5KBY SER C 32 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS C 33 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS C 34 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS C 35 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS C 36 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS C 37 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS C 38 UNP P27487 EXPRESSION TAG
SEQADV 5KBY ALA D 27 UNP P27487 EXPRESSION TAG
SEQADV 5KBY ASP D 28 UNP P27487 EXPRESSION TAG
SEQADV 5KBY PRO D 29 UNP P27487 EXPRESSION TAG
SEQADV 5KBY GLY D 30 UNP P27487 EXPRESSION TAG
SEQADV 5KBY GLY D 31 UNP P27487 EXPRESSION TAG
SEQADV 5KBY SER D 32 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS D 33 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS D 34 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS D 35 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS D 36 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS D 37 UNP P27487 EXPRESSION TAG
SEQADV 5KBY HIS D 38 UNP P27487 EXPRESSION TAG
SEQRES 1 A 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 A 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 A 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 A 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 A 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 A 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 A 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 A 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 A 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 A 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 A 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 A 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 A 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 A 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 A 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 A 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 A 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 A 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 A 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 A 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 A 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 A 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 A 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 A 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 A 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 A 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 A 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 A 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 A 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 A 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 A 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 A 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 A 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 A 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 A 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 A 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 A 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 A 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 A 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 A 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 A 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 A 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 A 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 A 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 A 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 A 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 A 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 A 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 A 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 A 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 A 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 A 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 A 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 A 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 A 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 A 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 B 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 B 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 B 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 B 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 B 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 B 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 B 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 B 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 B 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 B 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 B 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 B 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 B 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 B 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 B 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 B 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 B 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 B 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 B 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 B 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 B 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 B 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 B 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 B 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 B 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 B 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 B 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 B 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 B 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 B 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 B 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 B 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 B 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 B 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 B 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 B 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 B 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 B 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 B 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 B 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 B 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 B 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 B 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 B 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 B 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 B 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 B 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 B 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 B 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 B 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 B 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 B 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 B 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 B 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 B 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 B 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 C 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 C 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 C 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 C 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 C 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 C 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 C 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 C 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 C 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 C 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 C 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 C 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 C 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 C 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 C 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 C 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 C 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 C 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 C 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 C 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 C 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 C 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 C 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 C 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 C 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 C 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 C 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 C 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 C 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 C 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 C 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 C 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 C 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 C 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 C 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 C 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 C 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 C 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 C 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 C 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 C 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 C 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 C 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 C 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 C 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 C 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 C 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 C 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 C 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 C 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 C 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 C 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 C 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 C 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 C 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 C 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 740 ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER
SEQRES 2 D 740 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 3 D 740 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 4 D 740 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 5 D 740 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 6 D 740 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 7 D 740 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 8 D 740 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 9 D 740 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 10 D 740 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 11 D 740 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 12 D 740 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 13 D 740 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 14 D 740 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 15 D 740 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 16 D 740 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 17 D 740 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 18 D 740 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 19 D 740 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 20 D 740 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 21 D 740 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 22 D 740 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 23 D 740 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 24 D 740 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 25 D 740 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 26 D 740 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 27 D 740 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 28 D 740 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 29 D 740 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 30 D 740 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 31 D 740 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 32 D 740 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 33 D 740 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 34 D 740 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 35 D 740 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 36 D 740 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 37 D 740 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 38 D 740 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 39 D 740 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 40 D 740 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 41 D 740 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 42 D 740 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 43 D 740 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 44 D 740 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 45 D 740 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 46 D 740 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 47 D 740 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 48 D 740 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 49 D 740 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 50 D 740 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 51 D 740 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 52 D 740 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 53 D 740 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 54 D 740 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 55 D 740 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 56 D 740 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 57 D 740 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET NAG A1501 14
HET NAG A1502 14
HET NAG A1503 14
HET NAG A1504 14
HET NAG A1505 14
HET NAG A1506 14
HET NAG A1507 14
HET NAG A1508 14
HET NAG A1509 14
HET 6RL A1510 26
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 805 14
HET NAG B 806 14
HET NAG B 807 14
HET 6RL B 808 26
HET NAG C1501 14
HET NAG C1502 14
HET NAG C1503 14
HET NAG C1504 14
HET 5AX C1505 14
HET 6RL C1506 26
HET NAG D1501 14
HET NAG D1502 14
HET NAG D1503 14
HET NAG D1504 14
HET NAG D1505 14
HET NAG D1506 14
HET 6RL D1507 26
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 6RL 2-[[6-[(3~{R})-3-AZANYLPIPERIDIN-1-YL]-3-METHYL-2,4-
HETNAM 2 6RL BIS(OXIDANYLIDENE)PYRIMIDIN-1-YL]METHYL]-4-FLUORANYL-
HETNAM 3 6RL BENZENECARBONITRILE
HETNAM 5AX 2-(ACETYLAMINO)-1,5-ANHYDRO-2-DEOXY-D-GLUCITOL
HETSYN 6RL SYR-472
FORMUL 5 NAG 26(C8 H15 N O6)
FORMUL 11 6RL 4(C18 H20 F N5 O2)
FORMUL 22 5AX C8 H15 N O5
FORMUL 30 HOH *1597(H2 O)
HELIX 1 AA1 THR A 44 ASN A 51 1 8
HELIX 2 AA2 ASP A 200 VAL A 207 1 8
HELIX 3 AA3 PRO A 290 ILE A 295 1 6
HELIX 4 AA4 VAL A 341 GLN A 344 5 4
HELIX 5 AA5 GLU A 421 MET A 425 5 5
HELIX 6 AA6 ASN A 497 ASN A 506 1 10
HELIX 7 AA7 ASN A 562 ASN A 572 1 11
HELIX 8 AA8 GLY A 587 HIS A 592 1 6
HELIX 9 AA9 ALA A 593 ASN A 595 5 3
HELIX 10 AB1 THR A 600 LYS A 615 1 16
HELIX 11 AB2 SER A 630 GLY A 641 1 12
HELIX 12 AB3 ARG A 658 TYR A 662 5 5
HELIX 13 AB4 ASP A 663 GLY A 672 1 10
HELIX 14 AB5 ASN A 679 SER A 686 1 8
HELIX 15 AB6 VAL A 688 VAL A 698 5 11
HELIX 16 AB7 HIS A 712 VAL A 726 1 15
HELIX 17 AB8 SER A 744 PHE A 763 1 20
HELIX 18 AB9 THR B 44 ASN B 51 1 8
HELIX 19 AC1 ASP B 200 VAL B 207 1 8
HELIX 20 AC2 ASP B 274 LEU B 276 5 3
HELIX 21 AC3 PRO B 290 ILE B 295 1 6
HELIX 22 AC4 VAL B 341 GLN B 344 5 4
HELIX 23 AC5 GLU B 421 MET B 425 5 5
HELIX 24 AC6 ASN B 497 LEU B 504 1 8
HELIX 25 AC7 ASN B 562 ASN B 572 1 11
HELIX 26 AC8 GLY B 587 HIS B 592 1 6
HELIX 27 AC9 ALA B 593 ASN B 595 5 3
HELIX 28 AD1 THR B 600 MET B 616 1 17
HELIX 29 AD2 SER B 630 GLY B 641 1 12
HELIX 30 AD3 ARG B 658 TYR B 662 5 5
HELIX 31 AD4 ASP B 663 GLY B 672 1 10
HELIX 32 AD5 ASN B 679 SER B 686 1 8
HELIX 33 AD6 VAL B 688 VAL B 698 5 11
HELIX 34 AD7 HIS B 712 VAL B 726 1 15
HELIX 35 AD8 SER B 744 PHE B 763 1 20
HELIX 36 AD9 THR C 44 LYS C 50 1 7
HELIX 37 AE1 ASP C 200 VAL C 207 1 8
HELIX 38 AE2 PRO C 290 ILE C 295 1 6
HELIX 39 AE3 GLU C 421 MET C 425 5 5
HELIX 40 AE4 ASN C 497 GLN C 505 1 9
HELIX 41 AE5 ASN C 562 THR C 570 1 9
HELIX 42 AE6 GLY C 587 HIS C 592 1 6
HELIX 43 AE7 ALA C 593 ASN C 595 5 3
HELIX 44 AE8 THR C 600 MET C 616 1 17
HELIX 45 AE9 SER C 630 GLY C 641 1 12
HELIX 46 AF1 ARG C 658 TYR C 662 5 5
HELIX 47 AF2 ASP C 663 GLY C 672 1 10
HELIX 48 AF3 ASN C 679 SER C 686 1 8
HELIX 49 AF4 VAL C 688 VAL C 698 5 11
HELIX 50 AF5 PHE C 713 VAL C 726 1 14
HELIX 51 AF6 SER C 744 PHE C 763 1 20
HELIX 52 AF7 THR D 44 LYS D 50 1 7
HELIX 53 AF8 ASP D 200 VAL D 207 1 8
HELIX 54 AF9 PRO D 290 ILE D 295 1 6
HELIX 55 AG1 VAL D 341 GLN D 344 5 4
HELIX 56 AG2 GLU D 421 MET D 425 5 5
HELIX 57 AG3 ASN D 497 GLN D 505 1 9
HELIX 58 AG4 ASN D 562 THR D 570 1 9
HELIX 59 AG5 GLY D 587 HIS D 592 1 6
HELIX 60 AG6 ALA D 593 ASN D 595 5 3
HELIX 61 AG7 THR D 600 MET D 616 1 17
HELIX 62 AG8 SER D 630 GLY D 641 1 12
HELIX 63 AG9 ARG D 658 TYR D 662 5 5
HELIX 64 AH1 ASP D 663 GLY D 672 1 10
HELIX 65 AH2 ASN D 679 SER D 686 1 8
HELIX 66 AH3 THR D 687 VAL D 698 5 12
HELIX 67 AH4 HIS D 712 VAL D 726 1 15
HELIX 68 AH5 SER D 744 PHE D 763 1 20
SHEET 1 AA1 2 LYS A 41 THR A 42 0
SHEET 2 AA1 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 AA2 4 LEU A 60 TRP A 62 0
SHEET 2 AA2 4 GLU A 67 TYR A 70 -1 O LEU A 69 N ARG A 61
SHEET 3 AA2 4 ILE A 76 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 AA2 4 VAL A 88 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 AA3 4 ASP A 104 ILE A 107 0
SHEET 2 AA3 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AA3 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
SHEET 4 AA3 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AA4 4 THR A 152 TRP A 157 0
SHEET 2 AA4 4 LEU A 164 TRP A 168 -1 O VAL A 167 N GLN A 153
SHEET 3 AA4 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 AA4 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA5 3 ILE A 194 ASN A 196 0
SHEET 2 AA5 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA6 4 ILE A 194 ASN A 196 0
SHEET 2 AA6 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA6 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 AA6 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 AA7 2 LEU A 235 PHE A 240 0
SHEET 2 AA7 2 LYS A 250 PRO A 255 -1 O VAL A 254 N ILE A 236
SHEET 1 AA8 4 HIS A 298 THR A 307 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA8 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 AA8 4 ARG A 336 CYS A 339 -1 O ARG A 336 N ASP A 331
SHEET 1 AA9 4 HIS A 298 THR A 307 0
SHEET 2 AA9 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA9 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 AA9 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 AB1 4 HIS A 363 PHE A 364 0
SHEET 2 AB1 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AB1 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 AB1 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB2 4 VAL A 404 LEU A 410 0
SHEET 2 AB2 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 AB2 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB2 4 ASP A 438 CYS A 444 -1 O LYS A 441 N GLN A 435
SHEET 1 AB3 4 TYR A 457 PHE A 461 0
SHEET 2 AB3 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 AB3 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AB3 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB4 8 SER A 511 LEU A 519 0
SHEET 2 AB4 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 AB4 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AB4 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 AB4 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB4 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 AB4 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB5 2 LYS B 41 THR B 42 0
SHEET 2 AB5 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 AB6 4 ARG B 61 TRP B 62 0
SHEET 2 AB6 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 AB6 4 ASN B 75 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 AB6 4 SER B 86 LEU B 90 -1 O LEU B 90 N ILE B 76
SHEET 1 AB7 4 ILE B 102 ILE B 107 0
SHEET 2 AB7 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 AB7 4 TYR B 128 ASP B 136 -1 O ASP B 133 N LEU B 116
SHEET 4 AB7 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 AB8 4 TRP B 154 TRP B 157 0
SHEET 2 AB8 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 AB8 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 AB8 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 AB9 3 ILE B 194 ASN B 196 0
SHEET 2 AB9 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB9 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AC1 4 ILE B 194 ASN B 196 0
SHEET 2 AC1 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AC1 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 AC1 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 AC2 2 LEU B 235 PHE B 240 0
SHEET 2 AC2 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AC3 4 HIS B 298 THR B 307 0
SHEET 2 AC3 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 AC3 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 AC3 4 ARG B 336 CYS B 339 -1 O ARG B 336 N ASP B 331
SHEET 1 AC4 4 HIS B 298 THR B 307 0
SHEET 2 AC4 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 AC4 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 AC4 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 AC5 4 HIS B 363 PHE B 364 0
SHEET 2 AC5 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC5 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 AC5 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 AC6 4 VAL B 404 LEU B 410 0
SHEET 2 AC6 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 AC6 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC6 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AC7 4 TYR B 457 PHE B 461 0
SHEET 2 AC7 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 AC7 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 AC7 4 LYS B 489 GLU B 495 -1 O LEU B 494 N TYR B 480
SHEET 1 AC8 8 SER B 511 LEU B 519 0
SHEET 2 AC8 8 THR B 522 LEU B 530 -1 O TYR B 526 N ASP B 515
SHEET 3 AC8 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 AC8 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 AC8 8 VAL B 619 TRP B 629 1 O TRP B 627 N LEU B 544
SHEET 6 AC8 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 AC8 8 GLU B 699 GLY B 705 1 O LEU B 701 N GLY B 650
SHEET 8 AC8 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AC9 2 LYS C 41 THR C 42 0
SHEET 2 AC9 2 VAL C 507 GLN C 508 1 O GLN C 508 N LYS C 41
SHEET 1 AD1 2 GLU C 67 LEU C 69 0
SHEET 2 AD1 2 VAL C 78 ASN C 80 -1 O PHE C 79 N TYR C 68
SHEET 1 AD2 4 ASP C 104 ILE C 107 0
SHEET 2 AD2 4 PHE C 113 LYS C 122 -1 O GLU C 117 N ASP C 104
SHEET 3 AD2 4 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 4 AD2 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AD3 4 THR C 152 TRP C 157 0
SHEET 2 AD3 4 LEU C 164 TRP C 168 -1 O VAL C 167 N GLN C 153
SHEET 3 AD3 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AD3 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AD4 3 ILE C 194 ASN C 196 0
SHEET 2 AD4 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD4 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AD5 4 ILE C 194 ASN C 196 0
SHEET 2 AD5 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD5 4 THR C 265 ASN C 272 -1 O PHE C 269 N TYR C 225
SHEET 4 AD5 4 ILE C 285 GLN C 286 -1 O ILE C 285 N VAL C 270
SHEET 1 AD6 2 LEU C 235 PHE C 240 0
SHEET 2 AD6 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AD7 4 HIS C 298 TRP C 305 0
SHEET 2 AD7 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AD7 4 TYR C 322 ASP C 331 -1 O VAL C 324 N TRP C 315
SHEET 4 AD7 4 ARG C 336 CYS C 339 -1 O ARG C 336 N ASP C 331
SHEET 1 AD8 4 HIS C 298 TRP C 305 0
SHEET 2 AD8 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AD8 4 TYR C 322 ASP C 331 -1 O VAL C 324 N TRP C 315
SHEET 4 AD8 4 HIS C 345 MET C 348 -1 O HIS C 345 N MET C 325
SHEET 1 AD9 4 HIS C 363 PHE C 364 0
SHEET 2 AD9 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AD9 4 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AD9 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AE1 4 VAL C 404 LEU C 410 0
SHEET 2 AE1 4 TYR C 414 SER C 419 -1 O ILE C 418 N GLY C 406
SHEET 3 AE1 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AE1 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AE2 4 TYR C 457 PHE C 461 0
SHEET 2 AE2 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AE2 4 LEU C 479 SER C 484 -1 O THR C 481 N LEU C 470
SHEET 4 AE2 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AE3 8 SER C 511 LEU C 519 0
SHEET 2 AE3 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AE3 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AE3 8 TYR C 540 VAL C 546 1 N ASP C 545 O ALA C 576
SHEET 5 AE3 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 542
SHEET 6 AE3 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AE3 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 652
SHEET 8 AE3 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AE4 2 LYS D 41 THR D 42 0
SHEET 2 AE4 2 VAL D 507 GLN D 508 1 O GLN D 508 N LYS D 41
SHEET 1 AE5 3 LEU D 60 TRP D 62 0
SHEET 2 AE5 3 GLU D 67 LEU D 69 -1 O LEU D 69 N ARG D 61
SHEET 3 AE5 3 PHE D 79 ASN D 80 -1 O PHE D 79 N TYR D 68
SHEET 1 AE6 2 ILE D 76 LEU D 77 0
SHEET 2 AE6 2 VAL D 88 LEU D 90 -1 O LEU D 90 N ILE D 76
SHEET 1 AE7 4 ASP D 104 ILE D 107 0
SHEET 2 AE7 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AE7 4 TYR D 128 ASP D 136 -1 O ASP D 133 N LEU D 116
SHEET 4 AE7 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AE8 4 THR D 152 TRP D 157 0
SHEET 2 AE8 4 LEU D 164 TRP D 168 -1 O VAL D 167 N GLN D 153
SHEET 3 AE8 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AE8 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AE9 3 ILE D 194 ASN D 196 0
SHEET 2 AE9 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AE9 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AF1 4 ILE D 194 ASN D 196 0
SHEET 2 AF1 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AF1 4 THR D 265 ASN D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AF1 4 ILE D 285 GLN D 286 -1 O ILE D 285 N VAL D 270
SHEET 1 AF2 2 LEU D 235 PHE D 240 0
SHEET 2 AF2 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 AF3 4 HIS D 298 THR D 307 0
SHEET 2 AF3 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AF3 4 TYR D 322 ASP D 331 -1 O CYS D 328 N ILE D 311
SHEET 4 AF3 4 ARG D 336 CYS D 339 -1 O ASN D 338 N ASP D 329
SHEET 1 AF4 4 HIS D 298 THR D 307 0
SHEET 2 AF4 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AF4 4 TYR D 322 ASP D 331 -1 O CYS D 328 N ILE D 311
SHEET 4 AF4 4 HIS D 345 MET D 348 -1 O HIS D 345 N MET D 325
SHEET 1 AF5 4 HIS D 363 PHE D 364 0
SHEET 2 AF5 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AF5 4 ARG D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AF5 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 AF6 4 VAL D 404 LEU D 410 0
SHEET 2 AF6 4 TYR D 414 SER D 419 -1 O ILE D 418 N ILE D 405
SHEET 3 AF6 4 ASN D 430 GLN D 435 -1 O ILE D 434 N LEU D 415
SHEET 4 AF6 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AF7 4 TYR D 457 PHE D 461 0
SHEET 2 AF7 4 TYR D 467 CYS D 472 -1 O ARG D 471 N SER D 458
SHEET 3 AF7 4 LEU D 479 SER D 484 -1 O THR D 481 N LEU D 470
SHEET 4 AF7 4 LYS D 489 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AF8 8 SER D 511 LEU D 519 0
SHEET 2 AF8 8 THR D 522 LEU D 530 -1 O LEU D 530 N SER D 511
SHEET 3 AF8 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AF8 8 TYR D 540 VAL D 546 1 N ASP D 545 O ALA D 576
SHEET 5 AF8 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 542
SHEET 6 AF8 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AF8 8 GLU D 699 GLY D 705 1 O LEU D 701 N ALA D 652
SHEET 8 AF8 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.06
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.05
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.09
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.08
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.07
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.06
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.02
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.09
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.07
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.05
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.04
SSBOND 13 CYS C 444 CYS C 447 1555 1555 2.03
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.07
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.08
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.05
SSBOND 17 CYS D 385 CYS D 394 1555 1555 2.04
SSBOND 18 CYS D 444 CYS D 447 1555 1555 2.04
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.08
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.07
LINK ND2 ASN A 85 C1 NAG A1509 1555 1555 1.46
LINK ND2 ASN A 150 C1 NAG A1501 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG A1503 1555 1555 1.46
LINK ND2 ASN A 229 C1 NAG A1504 1555 1555 1.45
LINK ND2 ASN A 281 C1 NAG A1506 1555 1555 1.45
LINK ND2 ASN A 321 C1 NAG A1508 1555 1555 1.45
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.46
LINK ND2 ASN B 150 C1 NAG B 802 1555 1555 1.46
LINK ND2 ASN B 219 C1 NAG B 807 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG B 803 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG B 805 1555 1555 1.46
LINK ND2 ASN B 321 C1 NAG B 806 1555 1555 1.46
LINK ND2 ASN C 150 C1 NAG C1501 1555 1555 1.46
LINK ND2 ASN C 229 C1 NAG C1502 1555 1555 1.44
LINK ND2 ASN C 281 C1 NAG C1504 1555 1555 1.46
LINK ND2 ASN C 321 C1 5AX C1505 1555 1555 1.43
LINK ND2 ASN C 321 C2 5AX C1505 1555 1555 1.34
LINK ND2 ASN D 150 C1 NAG D1501 1555 1555 1.43
LINK ND2 ASN D 219 C1 NAG D1502 1555 1555 1.44
LINK ND2 ASN D 229 C1 NAG D1503 1555 1555 1.46
LINK ND2 ASN D 281 C1 NAG D1505 1555 1555 1.46
LINK ND2 ASN D 321 C1 NAG D1506 1555 1555 1.46
LINK O4 NAG A1501 C1 NAG A1502 1555 1555 1.45
LINK O4 NAG A1504 C1 NAG A1505 1555 1555 1.44
LINK O4 NAG A1506 C1 NAG A1507 1555 1555 1.44
LINK O4 NAG B 803 C1 NAG B 804 1555 1555 1.45
LINK O4 NAG C1502 C1 NAG C1503 1555 1555 1.44
LINK O4 NAG D1503 C1 NAG D1504 1555 1555 1.44
CISPEP 1 GLY A 474 PRO A 475 0 8.72
CISPEP 2 GLY B 474 PRO B 475 0 8.36
CISPEP 3 GLY C 474 PRO C 475 0 9.98
CISPEP 4 GLY D 474 PRO D 475 0 7.33
SITE 1 AC1 13 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC1 13 SER A 630 TYR A 631 VAL A 656 TRP A 659
SITE 3 AC1 13 TYR A 662 TYR A 666 VAL A 711 HOH A1674
SITE 4 AC1 13 HOH A1906
SITE 1 AC2 13 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 AC2 13 SER B 630 TYR B 631 VAL B 656 TRP B 659
SITE 3 AC2 13 TYR B 662 TYR B 666 ASN B 710 VAL B 711
SITE 4 AC2 13 HOH B1001
SITE 1 AC3 12 ARG C 125 GLU C 205 GLU C 206 TYR C 547
SITE 2 AC3 12 SER C 630 TYR C 631 VAL C 656 TRP C 659
SITE 3 AC3 12 TYR C 662 TYR C 666 VAL C 711 HOH C1632
SITE 1 AC4 14 ARG D 125 GLU D 205 GLU D 206 TYR D 547
SITE 2 AC4 14 SER D 630 TYR D 631 VAL D 656 TRP D 659
SITE 3 AC4 14 TYR D 662 TYR D 666 ASN D 710 VAL D 711
SITE 4 AC4 14 HOH D1720 HOH D1862
SITE 1 AC5 3 ASN A 85 SER A 86 SER A 87
SITE 1 AC6 4 ARG A 147 ASN A 150 HOH A1720 HOH A1844
SITE 1 AC7 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC8 4 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 1 AC9 4 TRP A 187 VAL A 279 ASN A 281 HOH A1609
SITE 1 AD1 5 ILE A 319 ASN A 321 SER A 349 THR A 350
SITE 2 AD1 5 ARG A 596
SITE 1 AD2 6 TYR B 83 ASN B 85 SER B 86 SER B 87
SITE 2 AD2 6 HOH B 949 HOH B1152
SITE 1 AD3 2 ASN B 150 HOH B 958
SITE 1 AD4 6 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 AD4 6 HOH B 901 HOH B1036
SITE 1 AD5 5 ILE B 194 ASN B 229 THR B 231 GLU B 232
SITE 2 AD5 5 HOH B1037
SITE 1 AD6 2 VAL B 279 ASN B 281
SITE 1 AD7 7 ILE B 319 ASN B 321 MET B 348 SER B 349
SITE 2 AD7 7 THR B 350 ARG B 596 HOH B 939
SITE 1 AD8 3 ILE C 148 ASN C 150 HOH C1799
SITE 1 AD9 4 ASN C 229 THR C 231 GLU C 232 HOH C1601
SITE 1 AE1 1 ASN C 281
SITE 1 AE2 4 ARG D 147 ASN D 150 HOH D1775 HOH D1824
SITE 1 AE3 5 ASN D 219 THR D 221 GLN D 308 GLU D 309
SITE 2 AE3 5 HOH D1618
SITE 1 AE4 7 ASN D 229 THR D 231 GLU D 232 LYS D 267
SITE 2 AE4 7 HOH D1687 HOH D1723 HOH D1828
SITE 1 AE5 3 VAL D 279 ASN D 281 HOH D1718
SITE 1 AE6 4 ILE D 319 ASN D 321 SER D 349 ARG D 596
SITE 1 AE7 7 ILE C 319 GLN C 320 TYR C 322 MET C 348
SITE 2 AE7 7 SER C 349 GLY C 352 ARG C 596
SITE 1 AE8 7 ILE C 319 GLN C 320 TYR C 322 MET C 348
SITE 2 AE8 7 SER C 349 GLY C 352 ARG C 596
CRYST1 121.573 122.165 143.704 90.00 114.57 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 0.008226 0.000000 0.003760 0.00000
SCALE2 0.000000 0.008186 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007651 0.00000
TER 5937 PRO A 766
TER 11962 PRO B 766
TER 17845 PRO C 766
TER 23792 PRO D 766
MASTER 628 0 31 68 203 0 46 625843 4 543 228
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