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HEADER HYDROLASE 13-NOV-08 3F8S
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 31-766;
COMPND 5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION
COMPND 6 ANTIGEN CD26, TP103, ADENOSINE DEAMINASE COMPLEXING PROTEIN
COMPND 7 2, ADABP;
COMPND 8 EC: 3.4.14.5;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: DPP4, ADCP2, CD26;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PBAC2
KEYWDS DIPEPTIDYL PEPTIDASE 4, COMPLEX, AMINOPEPTIDASE,
KEYWDS 2 GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE, SECRETED,
KEYWDS 3 SERINE PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.AMMIRATI,S.LIU,D.W.PIOTROWSKI
REVDAT 1 23-JUN-09 3F8S 0
JRNL AUTH M.J.AMMIRATI,K.M.ANDREWS,D.D.BOYER,A.M.BRODEUR,
JRNL AUTH 2 D.E.DANLEY,S.D.DORAN,B.HULIN,S.LIU,R.K.MCPHERSON,
JRNL AUTH 3 S.J.ORENA,J.C.PARKER,J.POLIVKOVA,X.QIU,C.B.SOGLIA,
JRNL AUTH 4 J.L.TREADWAY,M.A.VANVOLKENBURG,D.C.WILDER,
JRNL AUTH 5 D.W.PIOTROWSKI
JRNL TITL (3,3-DIFLUORO-PYRROLIDIN-1-YL)-[(2S,4S)-(4-(4-
JRNL TITL 2 PYRIMIDIN-2-YL-PIPERAZIN-1-YL)-PYRROLIDIN-2-YL]-
JRNL TITL 3 METHANONE: A POTENT, SELECTIVE, ORALLY ACTIVE
JRNL TITL 4 DIPEPTIDYL PEPTIDASE IV INHIBITOR.
JRNL REF BIOORG.MED.CHEM.LETT. V. 19 1991 2009
JRNL REFN ISSN 0960-894X
JRNL PMID 19275964
JRNL DOI 10.1016/J.BMCL.2009.02.041
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
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) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 47.8
REMARK 3 NUMBER OF REFLECTIONS : 32550
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) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1685
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) : 2.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 662
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 13.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 27
REMARK 3 BIN FREE R VALUE : 0.4270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11926
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 206
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.11000
REMARK 3 B22 (A**2) : 18.12000
REMARK 3 B33 (A**2) : -10.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.569
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.277
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.392
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12502 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 10679 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17025 ; 1.330 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 24841 ; 0.755 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1454 ; 6.862 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 616 ;34.231 ;23.961
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1994 ;18.521 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;16.678 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1814 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13780 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2680 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2689 ; 0.244 ; 0.600
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 11069 ; 0.242 ; 0.600
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5979 ; 0.204 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 6763 ; 0.100 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 518 ; 0.203 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 11 ; 0.081 ; 0.500
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): 29 ; 0.444 ; 0.600
REMARK 3 SYMMETRY VDW OTHERS (A): 69 ; 0.435 ; 0.600
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.092 ; 0.500
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): 9275 ; 0.555 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2942 ; 0.080 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11766 ; 0.653 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6457 ; 0.935 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5259 ; 1.503 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 39 A 766 1
REMARK 3 1 B 39 B 766 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 11216 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 11216 ; 0.10 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 39 A 766
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9036 15.6087 27.5595
REMARK 3 T TENSOR
REMARK 3 T11: -0.0753 T22: -0.1705
REMARK 3 T33: -0.0196 T12: -0.0795
REMARK 3 T13: -0.0186 T23: 0.0637
REMARK 3 L TENSOR
REMARK 3 L11: 0.6411 L22: 0.4405
REMARK 3 L33: 1.4098 L12: -0.1158
REMARK 3 L13: -0.2336 L23: -0.2663
REMARK 3 S TENSOR
REMARK 3 S11: 0.0384 S12: 0.0583 S13: 0.0852
REMARK 3 S21: -0.0656 S22: -0.0075 S23: -0.0086
REMARK 3 S31: 0.0546 S32: 0.0303 S33: -0.0309
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 39 B 766
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0575 -4.0446 77.8037
REMARK 3 T TENSOR
REMARK 3 T11: -0.0909 T22: -0.2078
REMARK 3 T33: -0.0351 T12: -0.0256
REMARK 3 T13: 0.0268 T23: 0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 0.5854 L22: 0.4755
REMARK 3 L33: 1.1932 L12: 0.0262
REMARK 3 L13: -0.1412 L23: -0.2495
REMARK 3 S TENSOR
REMARK 3 S11: -0.0824 S12: -0.0056 S13: -0.0041
REMARK 3 S21: 0.0043 S22: 0.0834 S23: 0.0105
REMARK 3 S31: 0.0937 S32: -0.0798 S33: -0.0010
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3F8S COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050289.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
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 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34242
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 75.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 32.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.32500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.2.0003
REMARK 200 STARTING MODEL: PDB ENTRY 2QJR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 32.71450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 210.76450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.57050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 210.76450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.71450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.57050
REMARK 290 SMTRY3 4 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: MONOMERIC
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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 31
REMARK 465 THR A 32
REMARK 465 ASP A 33
REMARK 465 ASP A 34
REMARK 465 ALA A 35
REMARK 465 THR A 36
REMARK 465 ALA A 37
REMARK 465 ASP A 38
REMARK 465 LEU A 767
REMARK 465 VAL A 768
REMARK 465 PRO A 769
REMARK 465 ARG A 770
REMARK 465 GLY A 771
REMARK 465 SER A 772
REMARK 465 HIS A 773
REMARK 465 HIS A 774
REMARK 465 HIS A 775
REMARK 465 HIS A 776
REMARK 465 HIS A 777
REMARK 465 HIS A 778
REMARK 465 GLY B 31
REMARK 465 THR B 32
REMARK 465 ASP B 33
REMARK 465 ASP B 34
REMARK 465 ALA B 35
REMARK 465 THR B 36
REMARK 465 ALA B 37
REMARK 465 ASP B 38
REMARK 465 LEU B 767
REMARK 465 VAL B 768
REMARK 465 PRO B 769
REMARK 465 ARG B 770
REMARK 465 GLY B 771
REMARK 465 SER B 772
REMARK 465 HIS B 773
REMARK 465 HIS B 774
REMARK 465 HIS B 775
REMARK 465 HIS B 776
REMARK 465 HIS B 777
REMARK 465 HIS B 778
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 ASP B 136 O LYS B 139 1.99
REMARK 500 ND2 ASN A 85 C2 NAG A 794 2.03
REMARK 500 OD1 ASN B 321 C1 NAG B 800 2.04
REMARK 500 O ASP A 136 O LYS A 139 2.07
REMARK 500 OE2 GLU A 347 NZ LYS A 373 2.14
REMARK 500 O ARG B 597 OG1 THR B 600 2.15
REMARK 500 ND2 ASN B 85 C2 NAG B 794 2.17
REMARK 500 CG ASN A 321 C1 NAG A 800 2.18
REMARK 500 ND2 ASN A 229 C2 NAG A 796 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE LYS B 392 OD1 ASN B 506 1545 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 192 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 243 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 310 CD - NE - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG A 310 NE - CZ - NH1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 310 NE - CZ - NH2 ANGL. DEV. = -9.3 DEGREES
REMARK 500 ASP A 515 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 579 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 681 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 729 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP B 96 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP B 243 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 274 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 310 CD - NE - CZ ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG B 310 NE - CZ - NH1 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ARG B 310 NE - CZ - NH2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP B 329 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 556 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 709 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 729 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 40 171.57 86.53
REMARK 500 SER A 64 -158.02 -164.61
REMARK 500 GLU A 73 66.04 78.16
REMARK 500 ASN A 74 -70.46 69.63
REMARK 500 ASN A 75 151.49 -28.92
REMARK 500 GLU A 97 52.64 -109.57
REMARK 500 GLN A 123 -98.39 -113.78
REMARK 500 TRP A 124 -157.23 -103.01
REMARK 500 ARG A 140 43.46 -58.23
REMARK 500 PRO A 149 151.78 -46.70
REMARK 500 ASN A 151 37.97 70.02
REMARK 500 ILE A 193 -59.76 -126.02
REMARK 500 ALA A 210 139.05 179.73
REMARK 500 SER A 242 -163.26 65.61
REMARK 500 GLN A 320 47.47 -93.20
REMARK 500 GLU A 332 -66.44 -16.32
REMARK 500 ARG A 336 -168.25 -113.84
REMARK 500 ARG A 358 155.05 169.53
REMARK 500 LYS A 392 -74.39 -64.62
REMARK 500 ASP A 393 -130.02 -90.33
REMARK 500 THR A 401 48.62 -82.59
REMARK 500 GLU A 464 -5.76 64.06
REMARK 500 VAL A 486 -71.83 -40.95
REMARK 500 ASN A 487 73.88 -119.26
REMARK 500 ASP A 488 70.08 -5.91
REMARK 500 ARG A 492 127.55 -177.98
REMARK 500 TYR A 547 -64.00 -122.33
REMARK 500 CYS A 551 29.25 83.08
REMARK 500 GLN A 553 107.23 -163.22
REMARK 500 SER A 583 172.74 -59.74
REMARK 500 TYR A 585 12.38 81.36
REMARK 500 ARG A 597 35.13 -154.71
REMARK 500 THR A 600 -99.86 -81.81
REMARK 500 ARG A 623 75.56 -118.31
REMARK 500 SER A 630 -117.07 69.98
REMARK 500 ALA A 654 58.08 35.16
REMARK 500 ASP A 678 -95.09 -106.17
REMARK 500 LYS A 696 -6.97 -58.29
REMARK 500 ASN A 710 -66.63 -107.07
REMARK 500 ASP A 725 11.27 -67.81
REMARK 500 VAL A 726 -2.98 -143.77
REMARK 500 ASP A 739 -156.29 -98.91
REMARK 500 ILE A 742 64.54 34.70
REMARK 500 ARG B 40 172.60 88.36
REMARK 500 SER B 64 -154.67 -163.30
REMARK 500 GLU B 73 69.69 75.14
REMARK 500 ASN B 74 -68.66 67.29
REMARK 500 ASN B 75 148.79 -31.47
REMARK 500 GLU B 97 52.20 -107.18
REMARK 500 GLN B 123 -95.51 -114.07
REMARK 500 TRP B 124 -155.29 -106.03
REMARK 500 ARG B 140 40.83 -58.15
REMARK 500 PRO B 149 154.72 -44.60
REMARK 500 ILE B 193 -57.83 -127.32
REMARK 500 ALA B 210 139.36 -177.54
REMARK 500 SER B 242 -158.00 64.64
REMARK 500 ALA B 259 123.79 -36.99
REMARK 500 GLN B 320 48.10 -96.26
REMARK 500 GLU B 332 -68.00 -14.48
REMARK 500 ARG B 336 -169.04 -115.06
REMARK 500 ARG B 358 151.82 166.24
REMARK 500 LYS B 392 -73.76 -60.90
REMARK 500 ASP B 393 -128.88 -91.11
REMARK 500 GLN B 455 -2.35 -141.38
REMARK 500 GLU B 464 -5.10 61.45
REMARK 500 VAL B 486 -71.03 -38.79
REMARK 500 ASN B 487 76.67 -119.60
REMARK 500 ASP B 488 72.05 -7.89
REMARK 500 ARG B 492 129.01 -177.49
REMARK 500 TYR B 547 -66.92 -120.96
REMARK 500 GLN B 553 110.96 -163.31
REMARK 500 TYR B 585 10.07 80.88
REMARK 500 ARG B 597 31.42 -153.12
REMARK 500 THR B 600 -101.13 -80.13
REMARK 500 ARG B 623 74.95 -114.34
REMARK 500 SER B 630 -117.98 67.18
REMARK 500 ALA B 654 57.03 37.68
REMARK 500 ASP B 678 -96.19 -103.86
REMARK 500 LYS B 696 -9.79 -58.01
REMARK 500 ASN B 710 -69.95 -109.46
REMARK 500 GLN B 714 -39.72 -38.49
REMARK 500 VAL B 726 -4.25 -148.35
REMARK 500 ASP B 739 -158.73 -101.99
REMARK 500 ILE B 742 62.64 34.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 310 0.07 SIDE_CHAIN
REMARK 500 ARG B 310 0.10 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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 B 800
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 794
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 797
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 796
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 801
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 794
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 797
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 796
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 798
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 799
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PF2 A 900
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PF2 B 900
DBREF 3F8S A 31 766 UNP P27487 DPP4_HUMAN 31 766
DBREF 3F8S B 31 766 UNP P27487 DPP4_HUMAN 31 766
SEQADV 3F8S LEU A 767 UNP P27487 EXPRESSION TAG
SEQADV 3F8S VAL A 768 UNP P27487 EXPRESSION TAG
SEQADV 3F8S PRO A 769 UNP P27487 EXPRESSION TAG
SEQADV 3F8S ARG A 770 UNP P27487 EXPRESSION TAG
SEQADV 3F8S GLY A 771 UNP P27487 EXPRESSION TAG
SEQADV 3F8S SER A 772 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS A 773 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS A 774 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS A 775 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS A 776 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS A 777 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS A 778 UNP P27487 EXPRESSION TAG
SEQADV 3F8S LEU B 767 UNP P27487 EXPRESSION TAG
SEQADV 3F8S VAL B 768 UNP P27487 EXPRESSION TAG
SEQADV 3F8S PRO B 769 UNP P27487 EXPRESSION TAG
SEQADV 3F8S ARG B 770 UNP P27487 EXPRESSION TAG
SEQADV 3F8S GLY B 771 UNP P27487 EXPRESSION TAG
SEQADV 3F8S SER B 772 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS B 773 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS B 774 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS B 775 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS B 776 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS B 777 UNP P27487 EXPRESSION TAG
SEQADV 3F8S HIS B 778 UNP P27487 EXPRESSION TAG
SEQRES 1 A 748 GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR
SEQRES 2 A 748 THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS
SEQRES 3 A 748 LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU
SEQRES 4 A 748 TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU
SEQRES 5 A 748 TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER THR PHE
SEQRES 6 A 748 ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER
SEQRES 7 A 748 PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL
SEQRES 8 A 748 LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE
SEQRES 9 A 748 TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG
SEQRES 10 A 748 ILE PRO ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL
SEQRES 11 A 748 GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR
SEQRES 12 A 748 VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR
SEQRES 13 A 748 TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR
SEQRES 14 A 748 ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER
SEQRES 15 A 748 ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR
SEQRES 16 A 748 ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR
SEQRES 17 A 748 SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR
SEQRES 18 A 748 VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO
SEQRES 19 A 748 THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER
SEQRES 20 A 748 SER VAL THR ASN ALA THR SER ILE GLN ILE THR ALA PRO
SEQRES 21 A 748 ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL
SEQRES 22 A 748 THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU
SEQRES 23 A 748 ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP
SEQRES 24 A 748 TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA
SEQRES 25 A 748 ARG GLN HIS ILE GLU MET SER THR THR GLY TRP VAL GLY
SEQRES 26 A 748 ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY
SEQRES 27 A 748 ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR
SEQRES 28 A 748 ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS
SEQRES 29 A 748 THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE
SEQRES 30 A 748 GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN
SEQRES 31 A 748 GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS
SEQRES 32 A 748 ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS LEU SER
SEQRES 33 A 748 CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL
SEQRES 34 A 748 SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS
SEQRES 35 A 748 SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER
SEQRES 36 A 748 VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER
SEQRES 37 A 748 ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER
SEQRES 38 A 748 LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE
SEQRES 39 A 748 TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER
SEQRES 40 A 748 LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO
SEQRES 41 A 748 CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP
SEQRES 42 A 748 ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA
SEQRES 43 A 748 SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS
SEQRES 44 A 748 ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU
SEQRES 45 A 748 VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS
SEQRES 46 A 748 MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY
SEQRES 47 A 748 TRP SER TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY
SEQRES 48 A 748 SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA
SEQRES 49 A 748 PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR
SEQRES 50 A 748 GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU
SEQRES 51 A 748 ASP HIS TYR ARG ASN SER THR VAL MET SER ARG ALA GLU
SEQRES 52 A 748 ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR
SEQRES 53 A 748 ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE
SEQRES 54 A 748 SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA
SEQRES 55 A 748 MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER
SEQRES 56 A 748 THR ALA HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE
SEQRES 57 A 748 ILE LYS GLN CYS PHE SER LEU PRO LEU VAL PRO ARG GLY
SEQRES 58 A 748 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 748 GLY THR ASP ASP ALA THR ALA ASP SER ARG LYS THR TYR
SEQRES 2 B 748 THR LEU THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS
SEQRES 3 B 748 LEU TYR SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU
SEQRES 4 B 748 TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU
SEQRES 5 B 748 TYR GLY ASN SER SER VAL PHE LEU GLU ASN SER THR PHE
SEQRES 6 B 748 ASP GLU PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER
SEQRES 7 B 748 PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL
SEQRES 8 B 748 LYS GLN TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE
SEQRES 9 B 748 TYR ASP LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG
SEQRES 10 B 748 ILE PRO ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL
SEQRES 11 B 748 GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR
SEQRES 12 B 748 VAL LYS ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR
SEQRES 13 B 748 TRP THR GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR
SEQRES 14 B 748 ASP TRP VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER
SEQRES 15 B 748 ALA LEU TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR
SEQRES 16 B 748 ALA GLN PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR
SEQRES 17 B 748 SER PHE TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR
SEQRES 18 B 748 VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO
SEQRES 19 B 748 THR VAL LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER
SEQRES 20 B 748 SER VAL THR ASN ALA THR SER ILE GLN ILE THR ALA PRO
SEQRES 21 B 748 ALA SER MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL
SEQRES 22 B 748 THR TRP ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU
SEQRES 23 B 748 ARG ARG ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP
SEQRES 24 B 748 TYR ASP GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA
SEQRES 25 B 748 ARG GLN HIS ILE GLU MET SER THR THR GLY TRP VAL GLY
SEQRES 26 B 748 ARG PHE ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY
SEQRES 27 B 748 ASN SER PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR
SEQRES 28 B 748 ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS
SEQRES 29 B 748 THR PHE ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE
SEQRES 30 B 748 GLU ALA LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN
SEQRES 31 B 748 GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS
SEQRES 32 B 748 ILE GLN LEU SER ASP TYR THR LYS VAL THR CYS LEU SER
SEQRES 33 B 748 CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL
SEQRES 34 B 748 SER PHE SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS
SEQRES 35 B 748 SER GLY PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER
SEQRES 36 B 748 VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER
SEQRES 37 B 748 ALA LEU ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER
SEQRES 38 B 748 LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE
SEQRES 39 B 748 TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER
SEQRES 40 B 748 LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO
SEQRES 41 B 748 CYS SER GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP
SEQRES 42 B 748 ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA
SEQRES 43 B 748 SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS
SEQRES 44 B 748 ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU
SEQRES 45 B 748 VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS
SEQRES 46 B 748 MET GLY PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY
SEQRES 47 B 748 TRP SER TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY
SEQRES 48 B 748 SER GLY SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA
SEQRES 49 B 748 PRO VAL SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR
SEQRES 50 B 748 GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU
SEQRES 51 B 748 ASP HIS TYR ARG ASN SER THR VAL MET SER ARG ALA GLU
SEQRES 52 B 748 ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR
SEQRES 53 B 748 ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE
SEQRES 54 B 748 SER LYS ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA
SEQRES 55 B 748 MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER
SEQRES 56 B 748 THR ALA HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE
SEQRES 57 B 748 ILE LYS GLN CYS PHE SER LEU PRO LEU VAL PRO ARG GLY
SEQRES 58 B 748 SER HIS HIS HIS HIS HIS HIS
MODRES 3F8S ASN A 85 ASN GLYCOSYLATION SITE
MODRES 3F8S ASN A 229 ASN GLYCOSYLATION SITE
MODRES 3F8S ASN A 321 ASN GLYCOSYLATION SITE
MODRES 3F8S ASN B 85 ASN GLYCOSYLATION SITE
MODRES 3F8S ASN B 219 ASN GLYCOSYLATION SITE
MODRES 3F8S ASN B 229 ASN GLYCOSYLATION SITE
HET NAG A 794 14
HET NAG A 797 14
HET NAG A 796 14
HET NAG A 800 14
HET NAG A 801 14
HET NAG B 794 14
HET NAG B 797 14
HET NAG B 796 14
HET NAG B 798 14
HET NAG B 799 14
HET NAG B 800 14
HET PF2 A 900 26
HET PF2 B 900 26
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PF2 2-(4-{(3S,5S)-5-[(3,3-DIFLUOROPYRROLIDIN-1-YL)
HETNAM 2 PF2 CARBONYL]PYRROLIDIN-3-YL}PIPERAZIN-1-YL)PYRIMIDINE
HETSYN NAG NAG
FORMUL 3 NAG 11(C8 H15 N O6)
FORMUL 10 PF2 2(C17 H24 F2 N6 O)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 GLU A 91 ASP A 96 5 6
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 ASP A 274 LEU A 276 5 3
HELIX 5 5 PRO A 290 ILE A 295 1 6
HELIX 6 6 LEU A 340 GLN A 344 5 5
HELIX 7 7 GLU A 421 MET A 425 5 5
HELIX 8 8 LYS A 463 ALA A 465 5 3
HELIX 9 9 ASN A 497 GLN A 505 1 9
HELIX 10 10 ASN A 562 THR A 570 1 9
HELIX 11 11 GLY A 587 HIS A 592 1 6
HELIX 12 12 ALA A 593 ASN A 595 5 3
HELIX 13 13 THR A 600 MET A 616 1 17
HELIX 14 14 SER A 630 GLY A 641 1 12
HELIX 15 15 ARG A 658 TYR A 662 5 5
HELIX 16 16 ASP A 663 GLY A 672 1 10
HELIX 17 17 ASN A 679 SER A 686 1 8
HELIX 18 18 VAL A 688 SER A 690 5 3
HELIX 19 19 ARG A 691 LYS A 696 1 6
HELIX 20 20 HIS A 712 ASP A 725 1 14
HELIX 21 21 SER A 744 PHE A 763 1 20
HELIX 22 22 THR B 44 LYS B 50 1 7
HELIX 23 23 GLU B 91 ASP B 96 5 6
HELIX 24 24 ASP B 200 VAL B 207 1 8
HELIX 25 25 PRO B 290 ILE B 295 1 6
HELIX 26 26 GLU B 421 MET B 425 5 5
HELIX 27 27 LYS B 463 ALA B 465 5 3
HELIX 28 28 ASN B 497 GLN B 505 1 9
HELIX 29 29 ASN B 562 GLU B 571 1 10
HELIX 30 30 GLY B 587 HIS B 592 1 6
HELIX 31 31 ALA B 593 ASN B 595 5 3
HELIX 32 32 THR B 600 MET B 616 1 17
HELIX 33 33 SER B 630 GLY B 641 1 12
HELIX 34 34 ARG B 658 TYR B 662 5 5
HELIX 35 35 ASP B 663 GLY B 672 1 10
HELIX 36 36 ASN B 679 SER B 686 1 8
HELIX 37 37 VAL B 688 VAL B 698 5 11
HELIX 38 38 HIS B 712 ASP B 725 1 14
HELIX 39 39 SER B 744 PHE B 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 LEU A 77 N TYR A 70
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 ILE A 143 -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 ALA A 165 N THR A 156
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 ILE A 287 -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 LEU A 316 N TYR A 299
SHEET 3 G 4 TYR A 322 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 G 4 ARG A 336 ASN A 338 -1 O ARG A 336 N ASP A 331
SHEET 1 H 4 HIS A 298 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 H 4 TYR A 322 ASP A 331 -1 O CYS A 328 N ILE A 311
SHEET 4 H 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
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 CYS A 385 N LYS A 373
SHEET 4 I 4 THR A 395 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 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 K 4 LEU A 479 SER A 484 -1 O HIS A 483 N TYR A 468
SHEET 4 K 4 LYS A 489 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 LEU A 530 N SER A 511
SHEET 3 L 8 ILE A 574 PHE A 578 -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 ALA A 576
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 4 ARG B 61 TRP B 62 0
SHEET 2 M 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 M 4 ILE B 76 ASN B 80 -1 O LEU B 77 N TYR B 70
SHEET 4 M 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 N 4 ASP B 104 ILE B 107 0
SHEET 2 N 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 N 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 N 4 GLN B 141 ILE B 143 -1 O GLN B 141 N ASP B 136
SHEET 1 O 4 TRP B 154 TRP B 157 0
SHEET 2 O 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 O 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 O 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 P 3 ILE B 194 ASN B 196 0
SHEET 2 P 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 P 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 Q 4 ILE B 194 ASN B 196 0
SHEET 2 Q 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 Q 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 Q 4 ILE B 285 ILE B 287 -1 O ILE B 287 N PHE B 268
SHEET 1 R 2 LEU B 235 PHE B 240 0
SHEET 2 R 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 S 4 HIS B 298 TRP B 305 0
SHEET 2 S 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 S 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 S 4 ARG B 336 ASN B 338 -1 O ARG B 336 N ASP B 331
SHEET 1 T 4 HIS B 298 TRP B 305 0
SHEET 2 T 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 T 4 TYR B 322 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 T 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 U 4 HIS B 363 PHE B 364 0
SHEET 2 U 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 U 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 U 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 V 4 VAL B 404 LEU B 410 0
SHEET 2 V 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 V 4 ASN B 430 GLN B 435 -1 O ILE B 434 N LEU B 415
SHEET 4 V 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 W 4 TYR B 457 PHE B 461 0
SHEET 2 W 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 W 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 W 4 LYS B 489 GLU B 495 -1 O LEU B 494 N TYR B 480
SHEET 1 X 8 SER B 511 LEU B 519 0
SHEET 2 X 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 X 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 X 8 TYR B 540 VAL B 546 1 N LEU B 543 O ALA B 576
SHEET 5 X 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 X 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 X 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 X 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.05
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.03
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.02
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.06
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.06
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.06
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.06
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.05
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.09
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
LINK ND2 ASN A 85 C1 NAG A 794 1555 1555 1.44
LINK ND2 ASN A 229 C1 NAG A 796 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG A 800 1555 1555 1.48
LINK ND2 ASN B 85 C1 NAG B 794 1555 1555 1.45
LINK ND2 ASN B 219 C1 NAG B 799 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG B 796 1555 1555 1.46
LINK O4 NAG A 794 C1 NAG A 797 1555 1555 1.44
LINK O4 NAG A 800 C1 NAG A 801 1555 1555 1.45
LINK O4 NAG B 794 C1 NAG B 797 1555 1555 1.45
LINK O4 NAG B 796 C1 NAG B 798 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 9.23
CISPEP 2 GLY B 474 PRO B 475 0 8.73
SITE 1 AC1 9 VAL A 78 ASN A 80 ASN A 85 SER A 86
SITE 2 AC1 9 SER A 87 TYR A 386 GLN A 388 THR A 395
SITE 3 AC1 9 NAG A 797
SITE 1 AC2 1 NAG A 794
SITE 1 AC3 3 ILE A 194 ASN A 229 THR A 231
SITE 1 AC4 5 ASN A 321 MET A 348 SER A 349 THR A 350
SITE 2 AC4 5 NAG A 801
SITE 1 AC5 1 NAG A 800
SITE 1 AC6 8 VAL B 78 ASN B 85 SER B 86 SER B 87
SITE 2 AC6 8 TYR B 386 GLN B 388 THR B 395 NAG B 797
SITE 1 AC7 2 LYS B 391 NAG B 794
SITE 1 AC8 3 ASN B 229 THR B 231 NAG B 798
SITE 1 AC9 1 NAG B 796
SITE 1 BC1 2 ASN B 219 THR B 221
SITE 1 BC2 5 ILE B 319 ASN B 321 MET B 348 SER B 349
SITE 2 BC2 5 THR B 350
SITE 1 BC3 11 ARG A 125 GLU A 205 GLU A 206 PHE A 357
SITE 2 BC3 11 TYR A 585 SER A 630 TYR A 631 VAL A 656
SITE 3 BC3 11 TYR A 662 TYR A 666 ASN A 710
SITE 1 BC4 10 ARG B 125 GLU B 205 GLU B 206 PHE B 357
SITE 2 BC4 10 SER B 630 TYR B 631 VAL B 656 TYR B 662
SITE 3 BC4 10 TYR B 666 ASN B 710
CRYST1 65.429 67.141 421.529 90.00 90.00 90.00 P 21 21 21 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 0.015284 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002372 0.00000
TER 5964 PRO A 766
TER 11928 PRO B 766
MASTER 579 0 13 39 98 0 22 612132 2 232 116
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