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HEADER HYDROLASE/HYDROLASE INHIBITOR 10-JUL-12 4G1F
TITLE CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH A
TITLE 2 PYRIDOPYRIMIDINEDIONE ANALOGUE
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: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,
COMPND 6 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,
COMPND 7 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV
COMPND 8 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL
COMPND 9 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
KEYWDS PROTEASE, 8-BLADED BETA-PROPELLER DOMAIN, AMINOPEPTIDASE, CELL
KEYWDS 2 MEMBRANE, GLYCOPROTEIN, HYDROLASE, SECRETED, SERINE PROTEASE,
KEYWDS 3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.SKENE,S.L.GWALTNEY
REVDAT 1 27-FEB-13 4G1F 0
JRNL AUTH B.LAM,Z.ZHANG,J.A.STAFFORD,R.J.SKENE,L.SHI,S.L.GWALTNEY
JRNL TITL STRUCTURE-BASED DESIGN OF PYRIDOPYRIMIDINEDIONES AS
JRNL TITL 2 DIPEPTIDYL PEPTIDASE IV INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 6628 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 23025999
JRNL DOI 10.1016/J.BMCL.2012.08.110
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0025
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 77247
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4065
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3949
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 185
REMARK 3 BIN FREE R VALUE : 0.3890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23642
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 404
REMARK 3 SOLVENT ATOMS : 391
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.73000
REMARK 3 B22 (A**2) : 0.46000
REMARK 3 B33 (A**2) : 1.71000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.52000
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): 0.435
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.324
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.890
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.854
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24780 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 33741 ; 1.028 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2877 ; 4.328 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1215 ;31.657 ;23.951
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3952 ;14.156 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 117 ;14.350 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3585 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19127 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 41 A 766
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5842 -0.9083 18.8015
REMARK 3 T TENSOR
REMARK 3 T11: 0.0357 T22: 0.0542
REMARK 3 T33: 0.0806 T12: 0.0140
REMARK 3 T13: -0.0200 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 1.3756 L22: 0.8821
REMARK 3 L33: 0.7560 L12: 0.0757
REMARK 3 L13: -0.0884 L23: 0.0464
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: -0.1226 S13: -0.2033
REMARK 3 S21: 0.0913 S22: -0.0023 S23: -0.2217
REMARK 3 S31: 0.0216 S32: 0.1803 S33: 0.0049
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 38 B 766
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3025 -7.6443 20.4737
REMARK 3 T TENSOR
REMARK 3 T11: 0.0415 T22: 0.0247
REMARK 3 T33: 0.0855 T12: 0.0089
REMARK 3 T13: 0.0105 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 1.4202 L22: 0.5187
REMARK 3 L33: 0.6582 L12: 0.1418
REMARK 3 L13: -0.0924 L23: -0.0199
REMARK 3 S TENSOR
REMARK 3 S11: -0.0583 S12: -0.0803 S13: -0.1713
REMARK 3 S21: 0.0229 S22: 0.0511 S23: 0.1118
REMARK 3 S31: 0.0032 S32: -0.0821 S33: 0.0073
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 41 C 766
REMARK 3 ORIGIN FOR THE GROUP (A): -35.8944 -0.5216 -33.5778
REMARK 3 T TENSOR
REMARK 3 T11: 0.1435 T22: 0.1763
REMARK 3 T33: 0.0452 T12: -0.0511
REMARK 3 T13: 0.0338 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 2.0304 L22: 0.5760
REMARK 3 L33: 0.5162 L12: 0.0139
REMARK 3 L13: 0.4100 L23: 0.0957
REMARK 3 S TENSOR
REMARK 3 S11: 0.0625 S12: 0.1636 S13: 0.1953
REMARK 3 S21: -0.0434 S22: -0.0205 S23: -0.0952
REMARK 3 S31: -0.1240 S32: 0.2864 S33: -0.0420
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 41 D 766
REMARK 3 ORIGIN FOR THE GROUP (A): -31.1787 -61.8266 47.0615
REMARK 3 T TENSOR
REMARK 3 T11: 0.1325 T22: 0.1597
REMARK 3 T33: 0.1295 T12: -0.0512
REMARK 3 T13: -0.0491 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 1.5635 L22: 1.0016
REMARK 3 L33: 1.0117 L12: 0.3462
REMARK 3 L13: -0.0390 L23: -0.2362
REMARK 3 S TENSOR
REMARK 3 S11: 0.0817 S12: -0.3155 S13: -0.0341
REMARK 3 S21: 0.0801 S22: -0.1623 S23: -0.3245
REMARK 3 S31: -0.0335 S32: 0.3104 S33: 0.0806
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G1F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073616.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-04
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84273
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3G0G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG 200MME, 0.1M BICINE PH 7.8
REMARK 280 , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 60.68100
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, 7
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 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 -121.62200
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 60.68100
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 115790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 61.91867
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 130.22319
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -59.70333
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 60.68100
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 130.22319
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 HIS B 35
REMARK 465 HIS B 36
REMARK 465 HIS B 37
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 TYR C 83
REMARK 465 GLY C 84
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 GLU D 73
REMARK 465 ASN D 74
REMARK 465 GLU D 82
REMARK 465 TYR D 83
REMARK 465 GLY D 84
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS B 38 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 40 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 123 -101.43 -104.24
REMARK 500 TRP A 124 -156.77 -91.31
REMARK 500 HIS A 162 39.20 -142.36
REMARK 500 ASP A 192 -7.33 66.28
REMARK 500 VAL A 207 -60.33 -100.24
REMARK 500 PRO A 218 -34.41 -39.96
REMARK 500 SER A 242 -158.32 57.31
REMARK 500 THR A 307 -157.97 -133.17
REMARK 500 GLN A 320 41.36 -83.20
REMARK 500 GLU A 332 -74.14 -78.13
REMARK 500 LYS A 423 19.17 59.37
REMARK 500 ASN A 450 79.33 -156.25
REMARK 500 GLN A 455 -1.92 -143.77
REMARK 500 GLU A 495 118.82 -160.56
REMARK 500 TYR A 547 -58.95 -130.11
REMARK 500 ALA A 548 10.33 54.16
REMARK 500 ARG A 596 13.35 54.45
REMARK 500 ARG A 597 47.90 -141.68
REMARK 500 THR A 600 -87.40 -126.71
REMARK 500 SER A 630 -113.56 59.82
REMARK 500 ASP A 678 -95.71 -122.29
REMARK 500 ASN A 710 -72.69 -81.16
REMARK 500 MET A 733 119.32 -167.38
REMARK 500 ASP A 739 -158.61 -91.20
REMARK 500 SER B 64 -157.43 -113.40
REMARK 500 HIS B 66 11.19 -151.70
REMARK 500 LEU B 90 111.15 -162.82
REMARK 500 GLN B 123 -106.71 -112.49
REMARK 500 TRP B 124 -153.94 -89.34
REMARK 500 HIS B 162 35.55 -140.02
REMARK 500 ILE B 193 -61.37 -130.97
REMARK 500 ASP B 200 -160.74 -79.73
REMARK 500 SER B 242 -164.33 58.04
REMARK 500 ALA B 259 116.03 -35.45
REMARK 500 THR B 307 -168.01 -128.38
REMARK 500 GLN B 320 42.99 -84.20
REMARK 500 GLU B 378 -8.55 -57.23
REMARK 500 THR B 411 -167.54 -108.11
REMARK 500 ASN B 450 89.70 -152.27
REMARK 500 ALA B 465 19.70 59.81
REMARK 500 LEU B 491 -66.91 -98.16
REMARK 500 GLN B 508 83.07 -68.65
REMARK 500 THR B 600 -97.12 -112.13
REMARK 500 SER B 630 -114.63 59.24
REMARK 500 ASP B 678 -85.39 -133.65
REMARK 500 ASN B 679 24.92 -150.95
REMARK 500 ASN B 710 -79.95 -86.50
REMARK 500 ASP B 739 -156.85 -98.23
REMARK 500 ILE B 742 60.32 38.40
REMARK 500 ASN C 51 52.95 71.34
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0WG 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 0WG 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 0WG C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0WG D 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 804
DBREF 4G1F A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4G1F B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4G1F C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4G1F D 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQADV 4G1F ALA A 27 UNP P27487 EXPRESSION TAG
SEQADV 4G1F ASP A 28 UNP P27487 EXPRESSION TAG
SEQADV 4G1F PRO A 29 UNP P27487 EXPRESSION TAG
SEQADV 4G1F GLY A 30 UNP P27487 EXPRESSION TAG
SEQADV 4G1F GLY A 31 UNP P27487 EXPRESSION TAG
SEQADV 4G1F SER A 32 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS A 33 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS A 34 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS A 35 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS A 36 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS A 37 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS A 38 UNP P27487 EXPRESSION TAG
SEQADV 4G1F ALA B 27 UNP P27487 EXPRESSION TAG
SEQADV 4G1F ASP B 28 UNP P27487 EXPRESSION TAG
SEQADV 4G1F PRO B 29 UNP P27487 EXPRESSION TAG
SEQADV 4G1F GLY B 30 UNP P27487 EXPRESSION TAG
SEQADV 4G1F GLY B 31 UNP P27487 EXPRESSION TAG
SEQADV 4G1F SER B 32 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS B 33 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS B 34 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS B 35 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS B 36 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS B 37 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS B 38 UNP P27487 EXPRESSION TAG
SEQADV 4G1F ALA C 27 UNP P27487 EXPRESSION TAG
SEQADV 4G1F ASP C 28 UNP P27487 EXPRESSION TAG
SEQADV 4G1F PRO C 29 UNP P27487 EXPRESSION TAG
SEQADV 4G1F GLY C 30 UNP P27487 EXPRESSION TAG
SEQADV 4G1F GLY C 31 UNP P27487 EXPRESSION TAG
SEQADV 4G1F SER C 32 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS C 33 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS C 34 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS C 35 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS C 36 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS C 37 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS C 38 UNP P27487 EXPRESSION TAG
SEQADV 4G1F ALA D 27 UNP P27487 EXPRESSION TAG
SEQADV 4G1F ASP D 28 UNP P27487 EXPRESSION TAG
SEQADV 4G1F PRO D 29 UNP P27487 EXPRESSION TAG
SEQADV 4G1F GLY D 30 UNP P27487 EXPRESSION TAG
SEQADV 4G1F GLY D 31 UNP P27487 EXPRESSION TAG
SEQADV 4G1F SER D 32 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS D 33 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS D 34 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS D 35 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS D 36 UNP P27487 EXPRESSION TAG
SEQADV 4G1F HIS D 37 UNP P27487 EXPRESSION TAG
SEQADV 4G1F 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 4G1F ASN A 229 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN B 229 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN D 229 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN C 229 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN C 219 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN B 281 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN A 219 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN B 150 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN A 321 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN C 150 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN A 281 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN D 150 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN A 85 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN B 219 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN A 150 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN B 85 ASN GLYCOSYLATION SITE
MODRES 4G1F ASN D 281 ASN GLYCOSYLATION SITE
HET 0WG 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 0WG 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 0WG C 800 24
HET NAG C 801 14
HET NAG C 802 14
HET NAG C 803 14
HET NAG C 804 14
HET 0WG D 800 24
HET NAG D 801 14
HET NAG D 802 14
HET NAG D 803 14
HET NAG D 804 14
HETNAM 0WG 7-AMINO-6-(AMINOMETHYL)-5-(2-BROMOPHENYL)-1,3-
HETNAM 2 0WG DIMETHYLPYRIDO[2,3-D]PYRIMIDINE-2,4(1H,3H)-DIONE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 5 0WG 4(C16 H16 BR N5 O2)
FORMUL 6 NAG 22(C8 H15 N O6)
FORMUL 26 HOH *391(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 ASP A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 LEU A 340 GLN A 344 5 5
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 VAL A 507 1 11
HELIX 8 8 ASN A 562 THR A 570 1 9
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
HELIX 11 11 THR A 600 LYS A 615 1 16
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 ARG A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 MET A 671 1 9
HELIX 15 15 ASN A 679 SER A 686 1 8
HELIX 16 16 VAL A 688 VAL A 698 5 11
HELIX 17 17 PHE A 713 VAL A 726 1 14
HELIX 18 18 SER A 744 PHE A 763 1 20
HELIX 19 19 THR B 44 LYS B 50 1 7
HELIX 20 20 ASP B 200 VAL B 207 1 8
HELIX 21 21 ASP B 274 LEU B 276 5 3
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 GLU B 421 MET B 425 5 5
HELIX 24 24 ASN B 497 LEU B 504 1 8
HELIX 25 25 GLN B 505 VAL B 507 5 3
HELIX 26 26 ASN B 562 THR B 570 1 9
HELIX 27 27 GLY B 587 HIS B 592 1 6
HELIX 28 28 ALA B 593 ASN B 595 5 3
HELIX 29 29 THR B 600 LYS B 615 1 16
HELIX 30 30 SER B 630 GLY B 641 1 12
HELIX 31 31 ARG B 658 TYR B 662 5 5
HELIX 32 32 ASP B 663 GLY B 672 1 10
HELIX 33 33 ASN B 679 SER B 686 1 8
HELIX 34 34 THR B 687 VAL B 698 5 12
HELIX 35 35 HIS B 712 VAL B 726 1 15
HELIX 36 36 SER B 744 PHE B 763 1 20
HELIX 37 37 THR C 44 ASN C 51 1 8
HELIX 38 38 ASP C 200 GLU C 206 1 7
HELIX 39 39 PRO C 290 ILE C 295 1 6
HELIX 40 40 VAL C 341 GLN C 344 5 4
HELIX 41 41 GLU C 421 MET C 425 5 5
HELIX 42 42 ASN C 497 GLN C 505 1 9
HELIX 43 43 ASN C 562 THR C 570 1 9
HELIX 44 44 GLY C 587 HIS C 592 1 6
HELIX 45 45 ALA C 593 ASN C 595 5 3
HELIX 46 46 THR C 600 LYS C 615 1 16
HELIX 47 47 SER C 630 GLY C 641 1 12
HELIX 48 48 ARG C 658 TYR C 662 5 5
HELIX 49 49 ASP C 663 GLY C 672 1 10
HELIX 50 50 ASN C 679 SER C 686 1 8
HELIX 51 51 VAL C 688 VAL C 698 5 11
HELIX 52 52 HIS C 712 VAL C 726 1 15
HELIX 53 53 SER C 744 PHE C 763 1 20
HELIX 54 54 THR D 44 LYS D 50 1 7
HELIX 55 55 PHE D 95 GLY D 99 5 5
HELIX 56 56 ASP D 200 GLU D 206 1 7
HELIX 57 57 PRO D 290 ILE D 295 1 6
HELIX 58 58 GLU D 421 MET D 425 5 5
HELIX 59 59 ASN D 497 GLN D 505 1 9
HELIX 60 60 ASN D 562 THR D 570 1 9
HELIX 61 61 GLY D 587 HIS D 592 1 6
HELIX 62 62 ALA D 593 ASN D 595 5 3
HELIX 63 63 THR D 600 LYS D 615 1 16
HELIX 64 64 SER D 630 GLY D 641 1 12
HELIX 65 65 ARG D 658 TYR D 662 5 5
HELIX 66 66 ASP D 663 GLY D 672 1 10
HELIX 67 67 ASN D 679 SER D 686 1 8
HELIX 68 68 VAL D 688 GLN D 697 5 10
HELIX 69 69 HIS D 712 VAL D 726 1 15
HELIX 70 70 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 LEU A 77 N TYR A 70
SHEET 4 A 4 SER A 87 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 ASP A 133 N LEU A 116
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 SER A 284 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 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 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 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 K 4 LEU A 479 SER A 484 -1 O HIS A 483 N TYR A 468
SHEET 4 K 4 GLY A 490 GLU A 495 -1 O GLU A 495 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 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 ASP A 620 N TYR A 540
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 ILE A 703 N ALA A 652
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 M 4 ARG B 61 TRP B 62 0
SHEET 2 M 4 GLU B 67 TYR B 70 -1 O LEU B 69 N ARG B 61
SHEET 3 M 4 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 M 4 SER B 87 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 N 4 ILE B 102 ILE B 107 0
SHEET 2 N 4 PHE B 113 LYS B 122 -1 O GLU B 117 N ASN B 103
SHEET 3 N 4 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 4 N 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 O 4 THR B 152 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 LYS B 267 N GLN B 227
SHEET 4 Q 4 ILE B 285 GLN B 286 -1 O ILE B 285 N VAL B 270
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 THR B 307 0
SHEET 2 S 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
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 CYS B 339 -1 O ASN B 338 N ASP B 329
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 ASP B 331 -1 O CYS B 328 N ILE B 311
SHEET 4 T 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
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 ALA B 409
SHEET 3 V 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 V 4 ASP B 438 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 ARG B 471 N SER B 458
SHEET 3 W 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 W 4 GLY B 490 GLU B 495 -1 O LEU B 491 N LEU B 482
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 SER B 577 N GLN B 527
SHEET 4 X 8 TYR B 540 VAL B 546 1 N ASP B 545 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 ILE B 703 N ALA B 652
SHEET 8 X 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 Y 4 LEU C 60 TRP C 62 0
SHEET 2 Y 4 GLU C 67 TYR C 70 -1 O LEU C 69 N ARG C 61
SHEET 3 Y 4 ILE C 76 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 4 Y 4 SER C 86 LEU C 90 -1 O PHE C 89 N ILE C 76
SHEET 1 Z 4 ASP C 104 ILE C 107 0
SHEET 2 Z 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 Z 4 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 4 Z 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AA 4 TRP C 154 TRP C 157 0
SHEET 2 AA 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AA 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AA 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AB 3 ILE C 194 ASN C 196 0
SHEET 2 AB 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AB 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AC 4 ILE C 194 ASN C 196 0
SHEET 2 AC 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AC 4 THR C 265 ASN C 272 -1 O PHE C 269 N TYR C 225
SHEET 4 AC 4 ILE C 285 ILE C 287 -1 O ILE C 285 N VAL C 270
SHEET 1 AD 2 LEU C 235 PHE C 240 0
SHEET 2 AD 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AE 4 HIS C 298 TRP C 305 0
SHEET 2 AE 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AE 4 TYR C 322 TYR C 330 -1 O VAL C 324 N TRP C 315
SHEET 4 AE 4 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
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 VAL C 324 N TRP C 315
SHEET 4 AF 4 HIS C 345 MET C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AG 4 HIS C 363 PHE C 364 0
SHEET 2 AG 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AG 4 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AG 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AH 4 VAL C 404 LEU C 410 0
SHEET 2 AH 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AH 4 ASN C 430 GLN C 435 -1 O ILE C 434 N LEU C 415
SHEET 4 AH 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AI 4 CYS C 454 PHE C 461 0
SHEET 2 AI 4 TYR C 467 PRO C 475 -1 O ARG C 471 N SER C 458
SHEET 3 AI 4 LEU C 479 SER C 484 -1 O THR C 481 N LEU C 470
SHEET 4 AI 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AJ 8 SER C 511 LEU C 519 0
SHEET 2 AJ 8 THR C 522 LEU C 530 -1 O TYR C 526 N ASP C 515
SHEET 3 AJ 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AJ 8 TYR C 540 VAL C 546 1 N ASP C 545 O ALA C 576
SHEET 5 AJ 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 542
SHEET 6 AJ 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AJ 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AJ 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AK 4 ARG D 61 TRP D 62 0
SHEET 2 AK 4 GLU D 67 TYR D 70 -1 O LEU D 69 N ARG D 61
SHEET 3 AK 4 LEU D 77 ASN D 80 -1 O PHE D 79 N TYR D 68
SHEET 4 AK 4 SER D 86 SER D 87 -1 O SER D 87 N VAL D 78
SHEET 1 AL 3 ASP D 104 ILE D 107 0
SHEET 2 AL 3 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AL 3 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 1 AM 4 TRP D 154 TRP D 157 0
SHEET 2 AM 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
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 PHE D 269 N TYR D 225
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 LEU D 316 N TYR D 299
SHEET 3 AQ 4 TYR D 322 TYR D 330 -1 O ASP D 326 N LEU D 313
SHEET 4 AQ 4 TRP D 337 CYS D 339 -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 LEU D 316 N TYR D 299
SHEET 3 AR 4 TYR D 322 TYR D 330 -1 O ASP D 326 N LEU D 313
SHEET 4 AR 4 HIS D 345 MET D 348 -1 O GLU D 347 N SER D 323
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 PHE D 387 N PHE D 371
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 GLU D 408
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 GLY D 490 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 VAL D 546 1 N LEU D 543 O ILE D 574
SHEET 5 AV 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 544
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 LEU D 701 N ALA D 652
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 2.03
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.04
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.04
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.04
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.04
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.04
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.03
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.04
SSBOND 13 CYS C 444 CYS C 447 1555 1555 2.03
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.04
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.04
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 2.03
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.04
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.04
LINK ND2 ASN A 229 C1 NAG A 804 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG B 804 1555 1555 1.44
LINK ND2 ASN D 229 C1 NAG D 802 1555 1555 1.44
LINK ND2 ASN C 229 C1 NAG C 803 1555 1555 1.44
LINK ND2 ASN C 219 C1 NAG C 802 1555 1555 1.44
LINK O4 NAG A 804 C1 NAG A 805 1555 1555 1.44
LINK ND2 ASN B 281 C1 NAG B 806 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG A 803 1555 1555 1.44
LINK O4 NAG C 803 C1 NAG C 804 1555 1555 1.44
LINK ND2 ASN B 150 C1 NAG B 802 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG A 808 1555 1555 1.44
LINK ND2 ASN C 150 C1 NAG C 801 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG A 806 1555 1555 1.45
LINK O4 NAG A 806 C1 NAG A 807 1555 1555 1.45
LINK ND2 ASN D 150 C1 NAG D 801 1555 1555 1.45
LINK O4 NAG B 804 C1 NAG B 805 1555 1555 1.45
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.45
LINK ND2 ASN B 219 C1 NAG B 803 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A 802 1555 1555 1.45
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.45
LINK O4 NAG D 802 C1 NAG D 803 1555 1555 1.45
LINK ND2 ASN D 281 C1 NAG D 804 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 1.07
CISPEP 2 GLY B 474 PRO B 475 0 3.38
CISPEP 3 GLY C 474 PRO C 475 0 2.41
CISPEP 4 GLY D 474 PRO D 475 0 2.43
SITE 1 AC1 14 ARG A 125 GLU A 205 GLU A 206 TYR A 547
SITE 2 AC1 14 TRP A 629 SER A 630 TYR A 631 VAL A 656
SITE 3 AC1 14 TYR A 662 TYR A 666 ASN A 710 VAL A 711
SITE 4 AC1 14 HIS A 740 HOH A 956
SITE 1 AC2 4 VAL A 78 ASN A 85 SER A 86 SER A 87
SITE 1 AC3 3 ARG A 147 ASN A 150 HOH A 905
SITE 1 AC4 4 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 1 AC5 4 ASN A 229 THR A 231 GLU A 232 NAG A 805
SITE 1 AC6 3 THR A 231 GLU A 232 NAG A 804
SITE 1 AC7 3 TRP A 187 ASN A 281 NAG A 807
SITE 1 AC8 3 TRP A 187 NAG A 806 GLN C 141
SITE 1 AC9 3 ASN A 321 SER A 349 ARG A 596
SITE 1 BC1 12 GLU B 205 GLU B 206 TYR B 547 TRP B 629
SITE 2 BC1 12 SER B 630 TYR B 631 VAL B 656 TYR B 662
SITE 3 BC1 12 TYR B 666 VAL B 711 HIS B 740 HOH B 958
SITE 1 BC2 2 ASN B 85 SER B 87
SITE 1 BC3 1 ASN B 150
SITE 1 BC4 4 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 1 BC5 4 ILE B 194 ASN B 229 THR B 231 NAG B 805
SITE 1 BC6 2 GLU B 232 NAG B 804
SITE 1 BC7 2 TRP B 187 ASN B 281
SITE 1 BC8 14 ARG C 125 GLU C 205 GLU C 206 TYR C 547
SITE 2 BC8 14 TRP C 629 SER C 630 TYR C 631 VAL C 656
SITE 3 BC8 14 TYR C 662 TYR C 666 ASN C 710 VAL C 711
SITE 4 BC8 14 HIS C 740 HOH C 905
SITE 1 BC9 2 ILE C 148 ASN C 150
SITE 1 CC1 4 ASN C 219 THR C 221 GLN C 308 GLU C 309
SITE 1 CC2 5 ILE C 194 GLN C 227 ASN C 229 THR C 231
SITE 2 CC2 5 NAG C 804
SITE 1 CC3 1 NAG C 803
SITE 1 CC4 11 GLU D 205 GLU D 206 TYR D 547 SER D 630
SITE 2 CC4 11 TYR D 631 VAL D 656 TYR D 662 TYR D 666
SITE 3 CC4 11 VAL D 711 HIS D 740 HOH D 901
SITE 1 CC5 3 ARG D 147 ILE D 148 ASN D 150
SITE 1 CC6 5 ILE D 194 ASN D 229 THR D 231 GLU D 232
SITE 2 CC6 5 NAG D 803
SITE 1 CC7 1 NAG D 802
SITE 1 CC8 1 ASN D 281
CRYST1 121.622 121.362 143.257 90.00 114.63 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 0.008222 0.000000 0.003769 0.00000
SCALE2 0.000000 0.008240 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007679 0.00000
TER 5936 PRO A 766
TER 11882 PRO B 766
TER 17796 PRO C 766
TER 23652 PRO D 766
MASTER 618 0 26 70 195 0 38 624437 4 461 228
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