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HEADER HYDROLASE 27-JAN-09 3G0G
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH
TITLE 2 A PYRIMIDINONE INHIBITOR 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 39-766;
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION
COMPND 6 ANTIGEN CD26, TP103, ADENOSINE DEAMINASE COMPLEXING PROTEIN
COMPND 7 2, ADABP, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL
COMPND 8 PEPTIDASE IV MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE
COMPND 9 FORM, DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 10 EC: 3.4.14.5;
COMPND 11 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: ADCP2, CD26, DPP4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSXB9
KEYWDS DPP4, PYRIMIDINONE, PYRIMIDINDIONE, AMINOPEPTIDASE, CELL
KEYWDS 2 MEMBRANE, GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE,
KEYWDS 3 SECRETED, SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ZHANG,M.B.WALLACE,J.FENG,J.A.STAFFORD,S.W.KALDOR,L.SHI,
AUTHOR 2 R.J.SKENE,K.AERTGEERTS,B.LEE,A.JENNINGS,R.XU,D.KASSEL,
AUTHOR 3 D.R.WEBB,S.L.GWALTNEY
REVDAT 1 16-FEB-10 3G0G 0
JRNL AUTH Z.ZHANG,M.B.WALLACE,J.FENG,J.A.STAFFORD,S.W.KALDOR,
JRNL AUTH 2 L.SHI,R.J.SKENE,K.AERTGEERTS,B.LEE,A.JENNINGS,R.XU,
JRNL AUTH 3 D.KASSEL,D.R.WEBB,S.L.GWALTNEY
JRNL TITL THE DESIGN AND SYNTHESIS OF PYRIMIDINONE AND
JRNL TITL 2 PYRIMIDINEDIONE INHIBITORS OF DIPEPTIDYL PEPTIDASE
JRNL TITL 3 IV
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 136813
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6854
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) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7723
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 398
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23501
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 544
REMARK 3 SOLVENT ATOMS : 738
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.83000
REMARK 3 B22 (A**2) : 7.10000
REMARK 3 B33 (A**2) : -1.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.477
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.293
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.240
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.451
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24785 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 33752 ; 1.244 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2859 ; 5.152 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1209 ;33.561 ;23.929
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3921 ;16.302 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 116 ;16.850 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3608 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18926 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 10723 ; 0.197 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 16799 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1120 ; 0.142 ; 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): 98 ; 0.138 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.188 ; 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): 14621 ; 1.212 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23174 ; 1.953 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11923 ; 1.075 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10578 ; 1.596 ; 3.000
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 808
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6937 -0.4258 19.3405
REMARK 3 T TENSOR
REMARK 3 T11: 0.0066 T22: -0.1112
REMARK 3 T33: -0.0265 T12: 0.0151
REMARK 3 T13: -0.0046 T23: 0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.8343 L22: 0.3086
REMARK 3 L33: 0.5887 L12: 0.0621
REMARK 3 L13: -0.1248 L23: 0.0860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0518 S12: -0.1413 S13: -0.1402
REMARK 3 S21: 0.0210 S22: 0.0386 S23: -0.0297
REMARK 3 S31: -0.0022 S32: 0.2021 S33: 0.0132
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 35 B 808
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4623 -6.9805 20.7048
REMARK 3 T TENSOR
REMARK 3 T11: -0.0294 T22: -0.1537
REMARK 3 T33: -0.0077 T12: 0.0259
REMARK 3 T13: 0.0297 T23: 0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 1.2037 L22: 0.1930
REMARK 3 L33: 0.4715 L12: 0.0247
REMARK 3 L13: -0.1749 L23: 0.1043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0510 S12: -0.1081 S13: -0.1890
REMARK 3 S21: -0.0172 S22: 0.0369 S23: 0.0183
REMARK 3 S31: -0.0543 S32: -0.1190 S33: 0.0141
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 808
REMARK 3 ORIGIN FOR THE GROUP (A): -36.2465 -0.1329 -34.0615
REMARK 3 T TENSOR
REMARK 3 T11: 0.0065 T22: -0.0422
REMARK 3 T33: -0.0930 T12: -0.0236
REMARK 3 T13: 0.0042 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.6685 L22: 0.1969
REMARK 3 L33: 0.4963 L12: -0.1572
REMARK 3 L13: 0.2454 L23: 0.1448
REMARK 3 S TENSOR
REMARK 3 S11: 0.1064 S12: 0.2686 S13: 0.1064
REMARK 3 S21: 0.0163 S22: -0.0638 S23: 0.0054
REMARK 3 S31: -0.0487 S32: 0.2674 S33: -0.0426
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 808
REMARK 3 ORIGIN FOR THE GROUP (A): -32.1887 -61.5936 48.4635
REMARK 3 T TENSOR
REMARK 3 T11: 0.0242 T22: 0.1492
REMARK 3 T33: 0.0837 T12: -0.1229
REMARK 3 T13: -0.0914 T23: 0.1832
REMARK 3 L TENSOR
REMARK 3 L11: 1.3119 L22: 0.6370
REMARK 3 L33: 0.4917 L12: 0.6607
REMARK 3 L13: -0.3143 L23: -0.2825
REMARK 3 S TENSOR
REMARK 3 S11: 0.2533 S12: -0.5857 S13: -0.2360
REMARK 3 S21: 0.0380 S22: -0.3759 S23: -0.2807
REMARK 3 S31: -0.1535 S32: 0.3225 S33: 0.1226
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 3G0G COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051266.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
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) : 1.0000
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 : 136864
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
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 (%) : 95.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.6670
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39500
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: PDB ENTRY 3G0B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG MME 200, 0.1M BICINE PH
REMARK 280 7.8, VAPOR DIFFUSION, 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 61.46050
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, 4, 5, 6
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: 4370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.8 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: 4380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -122.90600
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 61.46050
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ARG A 40
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 HIS B 34
REMARK 465 GLU B 73
REMARK 465 ASN B 74
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 ARG C 40
REMARK 465 GLU C 73
REMARK 465 ASN C 74
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 ARG D 40
REMARK 465 LYS D 71
REMARK 465 GLN D 72
REMARK 465 GLU D 73
REMARK 465 ASN D 74
REMARK 465 ASN D 75
REMARK 465 ILE D 76
REMARK 465 LEU D 77
REMARK 465 VAL D 78
REMARK 465 PHE D 79
REMARK 465 ASN D 80
REMARK 465 ALA D 81
REMARK 465 GLU D 82
REMARK 465 TYR D 83
REMARK 465 GLY D 84
REMARK 465 ASN D 85
REMARK 465 SER D 86
REMARK 465 SER D 87
REMARK 465 VAL D 88
REMARK 465 PHE D 89
REMARK 465 LEU D 90
REMARK 465 GLU D 91
REMARK 465 ASN D 92
REMARK 465 SER D 93
REMARK 465 THR D 94
REMARK 465 PHE D 95
REMARK 465 ASP D 96
REMARK 465 GLU D 97
REMARK 465 PHE D 98
REMARK 465 GLY D 99
REMARK 465 HIS D 100
REMARK 465 LEU D 137
REMARK 465 ASN D 138
REMARK 465 LYS D 139
REMARK 465 ARG D 140
REMARK 465 GLN D 141
REMARK 465 LEU D 142
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 B 922 O HOH B 1337 2.09
REMARK 500 OE1 GLU B 403 O HOH B 940 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 SER A 64 -147.44 -137.99
REMARK 500 HIS A 66 12.07 -147.86
REMARK 500 PHE A 95 46.31 -99.02
REMARK 500 GLN A 123 -99.01 -110.80
REMARK 500 TRP A 124 -146.79 -89.61
REMARK 500 HIS A 162 25.01 -146.04
REMARK 500 ILE A 193 -58.39 -131.22
REMARK 500 SER A 242 -158.00 60.30
REMARK 500 GLN A 320 36.81 -75.04
REMARK 500 SER A 333 39.78 -77.51
REMARK 500 SER A 334 -28.13 -166.79
REMARK 500 ASN A 450 76.04 -158.69
REMARK 500 ASN A 487 12.04 -146.05
REMARK 500 ASP A 488 -5.21 60.25
REMARK 500 TYR A 547 -72.98 -109.75
REMARK 500 TYR A 585 17.56 55.07
REMARK 500 ARG A 597 41.27 -141.60
REMARK 500 THR A 600 -95.25 -128.87
REMARK 500 SER A 630 -134.19 54.21
REMARK 500 ASP A 678 -93.48 -119.95
REMARK 500 ASN A 710 -70.04 -93.35
REMARK 500 ASP A 739 -164.77 -104.74
REMARK 500 ILE A 742 51.55 38.48
REMARK 500 ILE B 63 -38.27 -130.71
REMARK 500 SER B 64 -162.04 -120.91
REMARK 500 PHE B 98 -62.54 -146.33
REMARK 500 GLN B 123 -99.10 -117.73
REMARK 500 TRP B 124 -153.59 -95.16
REMARK 500 HIS B 162 41.03 -147.05
REMARK 500 ILE B 193 -57.28 -120.80
REMARK 500 SER B 242 -165.28 65.15
REMARK 500 GLU B 244 -27.36 -39.00
REMARK 500 GLN B 320 37.42 -83.37
REMARK 500 LYS B 423 16.15 59.70
REMARK 500 ASP B 488 76.60 52.29
REMARK 500 GLU B 521 13.31 52.78
REMARK 500 TYR B 547 -74.82 -114.86
REMARK 500 GLN B 586 30.70 -142.96
REMARK 500 THR B 600 -87.72 -120.71
REMARK 500 SER B 630 -120.86 58.76
REMARK 500 ASP B 678 -91.11 -109.79
REMARK 500 ASN B 679 25.43 -140.84
REMARK 500 PHE B 695 0.47 -62.30
REMARK 500 ASN B 710 -80.98 -82.04
REMARK 500 ASP B 739 -157.42 -102.05
REMARK 500 ILE B 742 48.75 35.64
REMARK 500 TYR C 58 72.81 -151.68
REMARK 500 SER C 64 -145.26 -143.15
REMARK 500 HIS C 66 13.97 -148.19
REMARK 500 TYR C 83 -65.16 -125.14
REMARK 500
REMARK 500 THIS ENTRY HAS 95 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 B 841 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH B 860 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH B 863 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH B1305 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH B1350 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH B1379 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B1393 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH B1395 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH B1400 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B1463 DISTANCE = 5.05 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG D 801
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUM A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUM B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUM C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUM D 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 808
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3G0B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH TAK-322
REMARK 900 RELATED ID: 3G0C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH A PYRIMIDINEDIONE INHIBITOR 1
REMARK 900 RELATED ID: 3G0D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX
REMARK 900 WITH A PYRIMIDINEDIONE INHIBITOR 2
DBREF 3G0G A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3G0G B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3G0G C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 3G0G D 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 3G0G ALA A 27 UNP P27487 EXPRESSION TAG
SEQADV 3G0G ASP A 28 UNP P27487 EXPRESSION TAG
SEQADV 3G0G PRO A 29 UNP P27487 EXPRESSION TAG
SEQADV 3G0G GLY A 30 UNP P27487 EXPRESSION TAG
SEQADV 3G0G GLY A 31 UNP P27487 EXPRESSION TAG
SEQADV 3G0G SER A 32 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS A 33 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS A 34 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS A 35 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS A 36 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS A 37 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS A 38 UNP P27487 EXPRESSION TAG
SEQADV 3G0G ALA B 27 UNP P27487 EXPRESSION TAG
SEQADV 3G0G ASP B 28 UNP P27487 EXPRESSION TAG
SEQADV 3G0G PRO B 29 UNP P27487 EXPRESSION TAG
SEQADV 3G0G GLY B 30 UNP P27487 EXPRESSION TAG
SEQADV 3G0G GLY B 31 UNP P27487 EXPRESSION TAG
SEQADV 3G0G SER B 32 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS B 33 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS B 34 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS B 35 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS B 36 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS B 37 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS B 38 UNP P27487 EXPRESSION TAG
SEQADV 3G0G ALA C 27 UNP P27487 EXPRESSION TAG
SEQADV 3G0G ASP C 28 UNP P27487 EXPRESSION TAG
SEQADV 3G0G PRO C 29 UNP P27487 EXPRESSION TAG
SEQADV 3G0G GLY C 30 UNP P27487 EXPRESSION TAG
SEQADV 3G0G GLY C 31 UNP P27487 EXPRESSION TAG
SEQADV 3G0G SER C 32 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS C 33 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS C 34 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS C 35 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS C 36 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS C 37 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS C 38 UNP P27487 EXPRESSION TAG
SEQADV 3G0G ALA D 27 UNP P27487 EXPRESSION TAG
SEQADV 3G0G ASP D 28 UNP P27487 EXPRESSION TAG
SEQADV 3G0G PRO D 29 UNP P27487 EXPRESSION TAG
SEQADV 3G0G GLY D 30 UNP P27487 EXPRESSION TAG
SEQADV 3G0G GLY D 31 UNP P27487 EXPRESSION TAG
SEQADV 3G0G SER D 32 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS D 33 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS D 34 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS D 35 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS D 36 UNP P27487 EXPRESSION TAG
SEQADV 3G0G HIS D 37 UNP P27487 EXPRESSION TAG
SEQADV 3G0G 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
MODRES 3G0G ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN A 150 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN A 219 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN A 281 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN A 321 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN B 150 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN B 219 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN B 229 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN B 281 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN B 321 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN C 85 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN C 150 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN C 219 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN C 229 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN C 281 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN C 321 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN D 150 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN D 219 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN D 229 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN D 281 ASN GLYCOSYLATION SITE
MODRES 3G0G ASN D 321 ASN GLYCOSYLATION SITE
HET RUM A 800 24
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET NAG A 807 14
HET NAG A 808 14
HET RUM B 800 24
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG B 805 14
HET NAG B 806 14
HET NAG B 807 14
HET NAG B 808 14
HET RUM C 800 24
HET NAG C 801 14
HET NAG C 802 14
HET NAG C 803 14
HET NAG C 804 14
HET NAG C 805 14
HET NAG C 806 14
HET NAG C 807 14
HET NAG C 808 14
HET RUM D 800 24
HET NAG D 801 14
HET NAG D 802 14
HET NAG D 803 14
HET NAG D 804 14
HET NAG D 805 14
HET NAG D 806 14
HET NAG D 807 14
HET NAG D 808 14
HETNAM RUM 2-({2-[(3R)-3-AMINOPIPERIDIN-1-YL]-5-BROMO-6-
HETNAM 2 RUM OXOPYRIMIDIN-1(6H)-YL}METHYL)BENZONITRILE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 5 RUM 4(C17 H18 BR N5 O)
FORMUL 6 NAG 32(C8 H15 N O6)
FORMUL 33 HOH *738(H2 O)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 PRO A 290 ILE A 295 1 6
HELIX 4 4 GLU A 421 MET A 425 5 5
HELIX 5 5 ASN A 497 ASN A 506 1 10
HELIX 6 6 ASN A 562 THR A 570 1 9
HELIX 7 7 GLY A 587 HIS A 592 1 6
HELIX 8 8 ALA A 593 ASN A 595 5 3
HELIX 9 9 THR A 600 LYS A 615 1 16
HELIX 10 10 SER A 630 GLY A 641 1 12
HELIX 11 11 ASP A 663 GLY A 672 1 10
HELIX 12 12 ASN A 679 SER A 686 1 8
HELIX 13 13 VAL A 688 VAL A 698 5 11
HELIX 14 14 HIS A 712 GLY A 727 1 16
HELIX 15 15 SER A 744 PHE A 763 1 20
HELIX 16 16 THR B 44 ASN B 51 1 8
HELIX 17 17 ASP B 200 VAL B 207 1 8
HELIX 18 18 PRO B 290 ILE B 295 1 6
HELIX 19 19 VAL B 341 GLN B 344 5 4
HELIX 20 20 GLU B 421 MET B 425 5 5
HELIX 21 21 ASN B 497 GLN B 505 1 9
HELIX 22 22 ASN B 562 THR B 570 1 9
HELIX 23 23 GLY B 587 ALA B 593 1 7
HELIX 24 24 THR B 600 LYS B 615 1 16
HELIX 25 25 SER B 630 GLY B 641 1 12
HELIX 26 26 ASP B 663 GLY B 672 1 10
HELIX 27 27 ASN B 679 SER B 686 1 8
HELIX 28 28 VAL B 688 VAL B 698 5 11
HELIX 29 29 PHE B 713 VAL B 726 1 14
HELIX 30 30 SER B 744 PHE B 763 1 20
HELIX 31 31 THR C 44 ASN C 51 1 8
HELIX 32 32 ASP C 200 VAL C 207 1 8
HELIX 33 33 PRO C 290 ILE C 295 1 6
HELIX 34 34 VAL C 341 GLN C 344 5 4
HELIX 35 35 GLU C 421 MET C 425 5 5
HELIX 36 36 ASN C 497 GLN C 505 1 9
HELIX 37 37 ASN C 562 THR C 570 1 9
HELIX 38 38 GLY C 587 HIS C 592 1 6
HELIX 39 39 ALA C 593 ASN C 595 5 3
HELIX 40 40 THR C 600 MET C 616 1 17
HELIX 41 41 TYR C 631 GLY C 641 1 11
HELIX 42 42 ASP C 663 GLY C 672 1 10
HELIX 43 43 ASN C 679 SER C 686 1 8
HELIX 44 44 VAL C 688 VAL C 698 5 11
HELIX 45 45 HIS C 712 VAL C 726 1 15
HELIX 46 46 SER C 744 PHE C 763 1 20
HELIX 47 47 THR D 44 ASN D 51 1 8
HELIX 48 48 ASP D 200 VAL D 207 1 8
HELIX 49 49 PRO D 290 ILE D 295 1 6
HELIX 50 50 LEU D 340 GLN D 344 5 5
HELIX 51 51 GLU D 421 MET D 425 5 5
HELIX 52 52 ASN D 497 GLN D 505 1 9
HELIX 53 53 ASN D 562 ASN D 572 1 11
HELIX 54 54 GLY D 587 HIS D 592 1 6
HELIX 55 55 ALA D 593 ASN D 595 5 3
HELIX 56 56 THR D 600 MET D 616 1 17
HELIX 57 57 SER D 630 GLY D 641 1 12
HELIX 58 58 ARG D 658 TYR D 662 5 5
HELIX 59 59 ASP D 663 GLY D 672 1 10
HELIX 60 60 ASN D 679 SER D 686 1 8
HELIX 61 61 VAL D 688 VAL D 698 5 11
HELIX 62 62 HIS D 712 VAL D 726 1 15
HELIX 63 63 SER D 744 PHE D 763 1 20
SHEET 1 A 4 ARG A 61 TRP A 62 0
SHEET 2 A 4 GLU A 67 TYR A 70 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ILE A 76 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 A 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 B 4 ASP A 104 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 B 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 C 4 TRP A 154 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 C 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 D 3 ILE A 194 ASN A 196 0
SHEET 2 D 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 D 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 E 4 ILE A 194 ASN A 196 0
SHEET 2 E 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 E 4 ILE A 285 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 G 4 HIS A 298 TRP A 305 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 G 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 G 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 H 4 HIS A 298 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 I 4 HIS A 363 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 CYS A 394 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 J 4 VAL A 404 LEU A 410 0
SHEET 2 J 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 K 4 CYS A 454 PHE A 461 0
SHEET 2 K 4 TYR A 467 PRO A 475 -1 O GLY A 474 N GLN A 455
SHEET 3 K 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 K 4 GLY A 490 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 L 8 SER A 511 LEU A 519 0
SHEET 2 L 8 THR A 522 LEU A 530 -1 O TYR A 526 N ASP A 515
SHEET 3 L 8 ILE A 574 ASP A 579 -1 O VAL A 575 N ILE A 529
SHEET 4 L 8 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 5 L 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
SHEET 6 L 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 L 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 M 2 LYS B 41 THR B 42 0
SHEET 2 M 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 N 4 ARG B 61 TRP B 62 0
SHEET 2 N 4 GLU B 67 TYR B 70 -1 O LEU B 69 N ARG B 61
SHEET 3 N 4 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 N 4 SER B 86 LEU B 90 -1 O LEU B 90 N ILE B 76
SHEET 1 O 4 ASP B 104 ILE B 107 0
SHEET 2 O 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 O 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 O 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 P 4 TRP B 154 TRP B 157 0
SHEET 2 P 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 P 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 P 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 Q 3 ILE B 194 ASN B 196 0
SHEET 2 Q 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 R 4 ILE B 194 ASN B 196 0
SHEET 2 R 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 R 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 S 2 LEU B 235 PHE B 240 0
SHEET 2 S 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 T 4 HIS B 298 THR B 307 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 T 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 T 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 U 4 HIS B 298 THR B 307 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 U 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 U 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 V 4 HIS B 363 PHE B 364 0
SHEET 2 V 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 V 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 V 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 W 4 VAL B 404 LEU B 410 0
SHEET 2 W 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 W 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 W 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 X 4 TYR B 457 PHE B 461 0
SHEET 2 X 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 X 4 LEU B 479 SER B 484 -1 O THR B 481 N LEU B 470
SHEET 4 X 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Y 8 SER B 511 LEU B 519 0
SHEET 2 Y 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Y 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Y 8 TYR B 540 VAL B 546 1 N ASP B 545 O ALA B 576
SHEET 5 Y 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 Y 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Y 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Y 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 Z 4 ARG C 61 TRP C 62 0
SHEET 2 Z 4 GLU C 67 TYR C 70 -1 O LEU C 69 N ARG C 61
SHEET 3 Z 4 ILE C 76 ASN C 80 -1 O PHE C 79 N TYR C 68
SHEET 4 Z 4 SER C 87 LEU C 90 -1 O PHE C 89 N ILE C 76
SHEET 1 AA 4 ILE C 102 ILE C 107 0
SHEET 2 AA 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AA 4 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 4 AA 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AB 4 TRP C 154 TRP C 157 0
SHEET 2 AB 4 LEU C 164 TRP C 168 -1 O ALA C 165 N THR C 156
SHEET 3 AB 4 ASP C 171 LYS C 175 -1 O TYR C 173 N TYR C 166
SHEET 4 AB 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AC 3 ILE C 194 ASN C 196 0
SHEET 2 AC 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AC 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AD 4 ILE C 194 ASN C 196 0
SHEET 2 AD 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AD 4 THR C 265 ASN C 272 -1 O PHE C 269 N TYR C 225
SHEET 4 AD 4 ILE C 285 ILE C 287 -1 O ILE C 285 N VAL C 270
SHEET 1 AE 2 LEU C 235 PHE C 240 0
SHEET 2 AE 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AF 4 HIS C 298 TRP C 305 0
SHEET 2 AF 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AF 4 TYR C 322 TYR C 330 -1 O CYS C 328 N ILE C 311
SHEET 4 AF 4 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 1 AG 4 HIS C 298 TRP C 305 0
SHEET 2 AG 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AG 4 TYR C 322 TYR C 330 -1 O CYS C 328 N ILE C 311
SHEET 4 AG 4 HIS C 345 MET C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AH 4 HIS C 363 PHE C 364 0
SHEET 2 AH 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AH 4 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AH 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AI 4 VAL C 404 LEU C 410 0
SHEET 2 AI 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AI 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AI 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AJ 4 TYR C 457 PHE C 461 0
SHEET 2 AJ 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AJ 4 LEU C 479 SER C 484 -1 O THR C 481 N LEU C 470
SHEET 4 AJ 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AK 8 SER C 511 LEU C 519 0
SHEET 2 AK 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AK 8 ILE C 574 PHE C 578 -1 O SER C 577 N GLN C 527
SHEET 4 AK 8 TYR C 540 VAL C 546 1 N ASP C 545 O ALA C 576
SHEET 5 AK 8 VAL C 619 SER C 630 1 O ALA C 625 N LEU C 542
SHEET 6 AK 8 CYS C 649 PRO C 655 1 O VAL C 653 N GLY C 628
SHEET 7 AK 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 654
SHEET 8 AK 8 GLN C 731 TYR C 735 1 O GLN C 731 N LEU C 702
SHEET 1 AL 3 ASP D 104 ILE D 107 0
SHEET 2 AL 3 ILE D 114 LYS D 122 -1 O GLU D 117 N ASP D 104
SHEET 3 AL 3 TYR D 128 TYR D 135 -1 O ASP D 133 N LEU D 116
SHEET 1 AM 4 TRP D 154 TRP D 157 0
SHEET 2 AM 4 LEU D 164 TRP D 168 -1 O VAL D 167 N TRP D 154
SHEET 3 AM 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AM 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AN 3 ILE D 194 ASN D 196 0
SHEET 2 AN 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AN 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AO 4 ILE D 194 ASN D 196 0
SHEET 2 AO 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AO 4 THR D 265 ASN D 272 -1 O VAL D 271 N LEU D 223
SHEET 4 AO 4 ILE D 285 ILE D 287 -1 O ILE D 285 N VAL D 270
SHEET 1 AP 2 LEU D 235 PHE D 240 0
SHEET 2 AP 2 LYS D 250 PRO D 255 -1 O VAL D 254 N ILE D 236
SHEET 1 AQ 4 HIS D 298 TRP D 305 0
SHEET 2 AQ 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AQ 4 TYR D 322 TYR D 330 -1 O VAL D 324 N TRP D 315
SHEET 4 AQ 4 TRP D 337 ASN D 338 -1 O ASN D 338 N ASP D 329
SHEET 1 AR 4 HIS D 298 TRP D 305 0
SHEET 2 AR 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AR 4 TYR D 322 TYR D 330 -1 O VAL D 324 N TRP D 315
SHEET 4 AR 4 HIS D 345 MET D 348 -1 O HIS D 345 N MET D 325
SHEET 1 AS 4 HIS D 363 PHE D 364 0
SHEET 2 AS 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AS 4 ARG D 382 GLN D 388 -1 O HIS D 383 N ILE D 375
SHEET 4 AS 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 AT 4 VAL D 404 LEU D 410 0
SHEET 2 AT 4 TYR D 414 SER D 419 -1 O TYR D 416 N ALA D 409
SHEET 3 AT 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AT 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AU 4 TYR D 457 PHE D 461 0
SHEET 2 AU 4 TYR D 467 CYS D 472 -1 O ARG D 471 N SER D 458
SHEET 3 AU 4 LEU D 479 SER D 484 -1 O THR D 481 N LEU D 470
SHEET 4 AU 4 LYS D 489 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AV 8 SER D 511 LEU D 519 0
SHEET 2 AV 8 THR D 522 LEU D 530 -1 O TYR D 526 N ASP D 515
SHEET 3 AV 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AV 8 TYR D 540 ASP D 545 1 N LEU D 543 O ILE D 574
SHEET 5 AV 8 VAL D 619 TRP D 629 1 O ASP D 620 N TYR D 540
SHEET 6 AV 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AV 8 GLU D 699 GLY D 705 1 O GLU D 699 N GLY D 650
SHEET 8 AV 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 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.06
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.04
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.07
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.07
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.06
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.05
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.06
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.05
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.05
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 2.05
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.04
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 2.05
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.05
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A 802 1555 1555 1.46
LINK ND2 ASN A 219 C1 NAG A 803 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG A 804 1555 1555 1.45
LINK ND2 ASN A 281 C1 NAG A 806 1555 1555 1.46
LINK ND2 ASN A 321 C1 NAG A 808 1555 1555 1.44
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.45
LINK ND2 ASN B 150 C1 NAG B 802 1555 1555 1.45
LINK ND2 ASN B 219 C1 NAG B 803 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG B 804 1555 1555 1.44
LINK ND2 ASN B 281 C1 NAG B 806 1555 1555 1.45
LINK ND2 ASN B 321 C1 NAG B 808 1555 1555 1.45
LINK ND2 ASN C 85 C1 NAG C 801 1555 1555 1.45
LINK ND2 ASN C 150 C1 NAG C 802 1555 1555 1.45
LINK ND2 ASN C 219 C1 NAG C 803 1555 1555 1.45
LINK ND2 ASN C 229 C1 NAG C 804 1555 1555 1.44
LINK ND2 ASN C 281 C1 NAG C 806 1555 1555 1.45
LINK ND2 ASN C 321 C1 NAG C 808 1555 1555 1.45
LINK ND2 ASN D 150 C1 NAG D 802 1555 1555 1.46
LINK ND2 ASN D 219 C1 NAG D 803 1555 1555 1.44
LINK ND2 ASN D 229 C1 NAG D 804 1555 1555 1.44
LINK ND2 ASN D 281 C1 NAG D 806 1555 1555 1.45
LINK ND2 ASN D 321 C1 NAG D 808 1555 1555 1.45
LINK O4 NAG A 804 C1 NAG A 805 1555 1555 1.45
LINK O4 NAG A 806 C1 NAG A 807 1555 1555 1.45
LINK O4 NAG B 804 C1 NAG B 805 1555 1555 1.45
LINK O4 NAG B 806 C1 NAG B 807 1555 1555 1.45
LINK O4 NAG C 804 C1 NAG C 805 1555 1555 1.45
LINK O4 NAG C 806 C1 NAG C 807 1555 1555 1.45
LINK O4 NAG D 804 C1 NAG D 805 1555 1555 1.45
LINK O4 NAG D 806 C1 NAG D 807 1555 1555 1.46
CISPEP 1 GLY A 474 PRO A 475 0 8.00
CISPEP 2 GLY B 474 PRO B 475 0 8.90
CISPEP 3 GLY C 474 PRO C 475 0 5.90
SITE 1 AC1 14 HOH A 2 ARG A 125 GLU A 205 GLU A 206
SITE 2 AC1 14 TYR A 547 TRP A 629 SER A 630 TYR A 631
SITE 3 AC1 14 VAL A 656 TYR A 662 TYR A 666 ASN A 710
SITE 4 AC1 14 HOH B1116 HOH B1336
SITE 1 AC2 3 ASN A 85 SER A 86 SER A 87
SITE 1 AC3 1 ASN A 150
SITE 1 AC4 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC5 5 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 2 AC5 5 NAG A 805
SITE 1 AC6 2 NAG A 804 HOH B 775
SITE 1 AC7 3 TRP A 187 ASN A 281 NAG A 807
SITE 1 AC8 1 NAG A 806
SITE 1 AC9 4 ILE A 319 ASN A 321 SER A 349 ARG A 596
SITE 1 BC1 15 ARG B 125 GLU B 205 GLU B 206 TYR B 547
SITE 2 BC1 15 TRP B 629 SER B 630 TYR B 631 VAL B 656
SITE 3 BC1 15 TYR B 662 TYR B 666 ASN B 710 VAL B 711
SITE 4 BC1 15 HOH B1042 HOH B1202 HOH B1203
SITE 1 BC2 2 ASN B 85 SER B 87
SITE 1 BC3 1 ASN B 150
SITE 1 BC4 5 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 2 BC4 5 HOH B1402
SITE 1 BC5 4 ASN B 229 THR B 231 NAG B 805 HOH B1273
SITE 1 BC6 1 NAG B 804
SITE 1 BC7 4 ASN B 281 NAG B 807 HOH B1274 HOH B1275
SITE 1 BC8 1 NAG B 806
SITE 1 BC9 3 ILE B 319 ASN B 321 SER B 349
SITE 1 CC1 14 HOH B1115 HOH B1278 ARG C 125 GLU C 205
SITE 2 CC1 14 GLU C 206 TYR C 547 TRP C 629 SER C 630
SITE 3 CC1 14 TYR C 631 VAL C 656 TYR C 662 TYR C 666
SITE 4 CC1 14 ASN C 710 VAL C 711
SITE 1 CC2 2 ASN C 85 SER C 87
SITE 1 CC3 1 ASN C 150
SITE 1 CC4 3 ASN C 219 THR C 221 GLN C 308
SITE 1 CC5 6 ILE C 194 ASN C 229 THR C 231 GLU C 232
SITE 2 CC5 6 LYS C 267 NAG C 805
SITE 1 CC6 1 NAG C 804
SITE 1 CC7 2 ASN C 281 NAG C 807
SITE 1 CC8 2 TRP C 187 NAG C 806
SITE 1 CC9 2 ASN C 321 SER C 349
SITE 1 DC1 11 HOH B1277 ARG D 125 GLU D 205 GLU D 206
SITE 2 DC1 11 TYR D 547 SER D 630 TYR D 631 VAL D 656
SITE 3 DC1 11 TYR D 662 TYR D 666 VAL D 711
SITE 1 DC2 2 ILE D 148 ASN D 150
SITE 1 DC3 6 HOH B1254 ASN D 219 GLY D 220 THR D 221
SITE 2 DC3 6 ASP D 274 GLN D 308
SITE 1 DC4 6 ILE D 194 GLN D 227 ASN D 229 THR D 231
SITE 2 DC4 6 GLU D 232 NAG D 805
SITE 1 DC5 2 THR D 231 NAG D 804
SITE 1 DC6 2 ASN D 281 NAG D 807
SITE 1 DC7 1 NAG D 806
SITE 1 DC8 4 ARG D 317 ILE D 319 ASN D 321 TYR D 322
CRYST1 122.906 122.921 145.092 90.00 114.77 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 0.008136 0.000000 0.003754 0.00000
SCALE2 0.000000 0.008135 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007590 0.00000
TER 5934 PRO A 766
TER 11925 PRO B 766
TER 17855 PRO C 766
TER 23505 PRO D 766
MASTER 704 0 36 63 193 0 51 624783 4 607 228
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