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HEADER HYDROLASE/PROTEIN BINDING 19-MAR-19 6OAZ
TITLE APO STRUCTURE OF WT LIPOPROTEIN LIPASE IN COMPLEX WITH GPIHBP1 MUTANT
TITLE 2 N78D N82D PRODUCED IN HEK293-F CELLS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPROTEIN LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: LPL;
COMPND 5 EC: 3.1.1.34;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED HIGH DENSITY
COMPND 9 LIPOPROTEIN-BINDING PROTEIN 1;
COMPND 10 CHAIN: E, F, G, H;
COMPND 11 FRAGMENT: RESIDUES 21-151;
COMPND 12 SYNONYM: GPI-ANCHORED HDL-BINDING PROTEIN 1,HIGH DENSITY LIPOPROTEIN-
COMPND 13 BINDING PROTEIN 1;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GPIHBP1, HBP1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293-F;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: GPIHBP1, HBP1;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293-F
KEYWDS LIPASE, HYDROLASE-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ARORA,P.A.HORTON,T.E.BENSON,M.J.ROMANOWSKI
REVDAT 1 08-MAY-19 6OAZ 0
JRNL AUTH R.ARORA,A.NIMONKAR,D.BAIRD,C.WANG,C.-H.CHIU,P.A.HORTON,
JRNL AUTH 2 S.HANRAHAN,R.CUBBON,S.WELDON,W.TSCHANTZ,S.MUELLER,R.BRUNNER,
JRNL AUTH 3 P.LEHR,P.MEIER,J.OTTL,A.VOZNESENSKY,P.PANDEY,T.SMITH,
JRNL AUTH 4 A.STOJANOVIC,A.FLYER,T.E.BENSON,M.J.ROMANOWSKI,J.TRAUGER
JRNL TITL STRUCTURE OF LIPOPROTEIN LIPASE IN COMPLEX WITH GPIHBP1
JRNL REF PROC.NATL.ACAD.SCI.USA 2019
JRNL REFN ESSN 1091-6490
JRNL DOI 10.1073/PNAS.1820171116
REMARK 2
REMARK 2 RESOLUTION. 3.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 121.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 54997
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 2738
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.06
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.86
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1100
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2469
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1048
REMARK 3 BIN R VALUE (WORKING SET) : 0.2441
REMARK 3 BIN FREE R VALUE : 0.3013
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.73
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 52
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15670
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 152
REMARK 3 SOLVENT ATOMS : 21
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 113.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.70070
REMARK 3 B22 (A**2) : -0.88810
REMARK 3 B33 (A**2) : 10.58880
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.450
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.393
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 16230 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 22012 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5590 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 2706 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 16230 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 2148 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 17732 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.82
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.09
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4758 -14.9133 93.4710
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: -0.5561
REMARK 3 T33: -0.6079 T12: 0.0788
REMARK 3 T13: 0.0669 T23: -0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 1.1410 L22: 1.8118
REMARK 3 L33: 6.3289 L12: -0.5478
REMARK 3 L13: -1.7054 L23: 0.7331
REMARK 3 S TENSOR
REMARK 3 S11: -0.1637 S12: -0.0782 S13: -0.0626
REMARK 3 S21: -0.2890 S22: 0.0623 S23: -0.1654
REMARK 3 S31: 0.1864 S32: 0.0591 S33: 0.1013
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9579 20.9743 55.3524
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: -0.5949
REMARK 3 T33: -0.6079 T12: -0.0115
REMARK 3 T13: -0.1635 T23: -0.0993
REMARK 3 L TENSOR
REMARK 3 L11: 0.9703 L22: 3.8082
REMARK 3 L33: 10.1035 L12: 0.2721
REMARK 3 L13: 1.0967 L23: -0.9127
REMARK 3 S TENSOR
REMARK 3 S11: -0.2370 S12: -0.0662 S13: 0.1877
REMARK 3 S21: 0.6253 S22: -0.0696 S23: -0.3187
REMARK 3 S31: -1.0885 S32: 0.2408 S33: 0.3066
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 58.9763 15.9909 84.5933
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: -0.6079
REMARK 3 T33: -0.6079 T12: 0.0996
REMARK 3 T13: -0.1440 T23: 0.0718
REMARK 3 L TENSOR
REMARK 3 L11: 0.8926 L22: 1.7178
REMARK 3 L33: 5.4158 L12: -0.4479
REMARK 3 L13: 0.8869 L23: -0.2410
REMARK 3 S TENSOR
REMARK 3 S11: -0.1499 S12: -0.0360 S13: 0.1318
REMARK 3 S21: -0.2827 S22: -0.0121 S23: 0.2269
REMARK 3 S31: -0.4939 S32: -0.2925 S33: 0.1620
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5849 -20.2297 46.5742
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: -0.5546
REMARK 3 T33: -0.5823 T12: 0.0407
REMARK 3 T13: 0.0368 T23: 0.1015
REMARK 3 L TENSOR
REMARK 3 L11: 0.6914 L22: 1.8432
REMARK 3 L33: 5.8583 L12: 0.3097
REMARK 3 L13: -1.0305 L23: -0.5256
REMARK 3 S TENSOR
REMARK 3 S11: -0.1999 S12: -0.0424 S13: -0.0685
REMARK 3 S21: 0.0292 S22: 0.1439 S23: -0.0026
REMARK 3 S31: 0.3217 S32: 0.1019 S33: 0.0560
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6341 -38.5929 63.1811
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: -0.6079
REMARK 3 T33: -0.6052 T12: -0.1174
REMARK 3 T13: 0.2175 T23: -0.1775
REMARK 3 L TENSOR
REMARK 3 L11: 6.2793 L22: 10.6579
REMARK 3 L33: 5.0861 L12: -0.7114
REMARK 3 L13: -1.1267 L23: 2.1033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0442 S12: 0.1075 S13: -0.8412
REMARK 3 S21: -0.8125 S22: -0.4142 S23: 0.1750
REMARK 3 S31: 0.8665 S32: -0.8049 S33: 0.4584
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { F|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0112 46.0836 86.5418
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: -0.6079
REMARK 3 T33: -0.6079 T12: -0.0111
REMARK 3 T13: -0.0565 T23: -0.3040
REMARK 3 L TENSOR
REMARK 3 L11: 6.0463 L22: 13.0512
REMARK 3 L33: 7.5077 L12: 0.1067
REMARK 3 L13: 1.9626 L23: 5.8208
REMARK 3 S TENSOR
REMARK 3 S11: -0.1017 S12: 0.3795 S13: 1.0032
REMARK 3 S21: 0.8828 S22: 0.0892 S23: -0.5404
REMARK 3 S31: -0.7621 S32: 0.6713 S33: 0.0126
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { G|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1545 40.1067 53.9767
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: -0.6079
REMARK 3 T33: -0.6079 T12: 0.2296
REMARK 3 T13: -0.0582 T23: 0.2656
REMARK 3 L TENSOR
REMARK 3 L11: 8.2228 L22: 13.5165
REMARK 3 L33: 8.9103 L12: -2.1193
REMARK 3 L13: 1.2991 L23: -2.5863
REMARK 3 S TENSOR
REMARK 3 S11: 0.1070 S12: -0.1906 S13: 0.8084
REMARK 3 S21: 0.2181 S22: 0.0506 S23: 0.4435
REMARK 3 S31: -1.0122 S32: -0.7590 S33: -0.1576
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { H|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 60.7082 -45.5569 77.3554
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: -0.6079
REMARK 3 T33: -0.6079 T12: 0.3040
REMARK 3 T13: 0.0293 T23: 0.3039
REMARK 3 L TENSOR
REMARK 3 L11: 11.8136 L22: 14.7747
REMARK 3 L33: 7.9187 L12: 1.3800
REMARK 3 L13: -0.1260 L23: -3.2441
REMARK 3 S TENSOR
REMARK 3 S11: 0.0275 S12: 0.0485 S13: -0.5829
REMARK 3 S21: 0.7004 S22: -0.2451 S23: -0.1172
REMARK 3 S31: 1.0885 S32: 0.8628 S33: 0.2176
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6OAZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : 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) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.29
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55090
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.040
REMARK 200 RESOLUTION RANGE LOW (A) : 191.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.92200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1LPA, 2J8B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M CALCIUM ACETATE, 18% PEG3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 78.50000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 95.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 78.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 95.97000
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, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 28
REMARK 465 ASP A 29
REMARK 465 ILE A 245
REMARK 465 GLY A 246
REMARK 465 GLU A 247
REMARK 465 ALA A 248
REMARK 465 ILE A 249
REMARK 465 ARG A 250
REMARK 465 VAL A 251
REMARK 465 ILE A 252
REMARK 465 ALA A 253
REMARK 465 GLU A 254
REMARK 465 ARG A 255
REMARK 465 GLY A 256
REMARK 465 LEU A 257
REMARK 465 GLY A 258
REMARK 465 ASP A 259
REMARK 465 VAL A 260
REMARK 465 ASP A 261
REMARK 465 GLN A 262
REMARK 465 ASP A 412
REMARK 465 SER A 413
REMARK 465 TYR A 414
REMARK 465 PHE A 415
REMARK 465 SER A 416
REMARK 465 TRP A 417
REMARK 465 SER A 418
REMARK 465 ASP A 419
REMARK 465 LYS A 472
REMARK 465 LYS A 473
REMARK 465 SER A 474
REMARK 465 GLY A 475
REMARK 465 ALA B 28
REMARK 465 ASP B 29
REMARK 465 ILE B 245
REMARK 465 GLY B 246
REMARK 465 GLU B 247
REMARK 465 ALA B 248
REMARK 465 ILE B 249
REMARK 465 ARG B 250
REMARK 465 VAL B 251
REMARK 465 ILE B 252
REMARK 465 ALA B 253
REMARK 465 GLU B 254
REMARK 465 ARG B 255
REMARK 465 GLY B 256
REMARK 465 LEU B 257
REMARK 465 GLY B 258
REMARK 465 ASP B 259
REMARK 465 VAL B 260
REMARK 465 ASP B 261
REMARK 465 GLN B 262
REMARK 465 ASP B 412
REMARK 465 SER B 413
REMARK 465 TYR B 414
REMARK 465 PHE B 415
REMARK 465 SER B 416
REMARK 465 TRP B 417
REMARK 465 SER B 418
REMARK 465 ASP B 419
REMARK 465 LYS B 472
REMARK 465 LYS B 473
REMARK 465 SER B 474
REMARK 465 GLY B 475
REMARK 465 ALA C 28
REMARK 465 ASP C 29
REMARK 465 ILE C 245
REMARK 465 GLY C 246
REMARK 465 GLU C 247
REMARK 465 ALA C 248
REMARK 465 ILE C 249
REMARK 465 ARG C 250
REMARK 465 VAL C 251
REMARK 465 ILE C 252
REMARK 465 ALA C 253
REMARK 465 GLU C 254
REMARK 465 ARG C 255
REMARK 465 GLY C 256
REMARK 465 LEU C 257
REMARK 465 GLY C 258
REMARK 465 ASP C 259
REMARK 465 VAL C 260
REMARK 465 ASP C 261
REMARK 465 GLN C 262
REMARK 465 ASP C 412
REMARK 465 SER C 413
REMARK 465 TYR C 414
REMARK 465 PHE C 415
REMARK 465 SER C 416
REMARK 465 TRP C 417
REMARK 465 SER C 418
REMARK 465 ASP C 419
REMARK 465 LYS C 472
REMARK 465 LYS C 473
REMARK 465 SER C 474
REMARK 465 GLY C 475
REMARK 465 ALA D 28
REMARK 465 ASP D 29
REMARK 465 ILE D 245
REMARK 465 GLY D 246
REMARK 465 GLU D 247
REMARK 465 ALA D 248
REMARK 465 ILE D 249
REMARK 465 ARG D 250
REMARK 465 VAL D 251
REMARK 465 ILE D 252
REMARK 465 ALA D 253
REMARK 465 GLU D 254
REMARK 465 ARG D 255
REMARK 465 GLY D 256
REMARK 465 LEU D 257
REMARK 465 GLY D 258
REMARK 465 ASP D 259
REMARK 465 VAL D 260
REMARK 465 ASP D 261
REMARK 465 GLN D 262
REMARK 465 ASP D 412
REMARK 465 SER D 413
REMARK 465 TYR D 414
REMARK 465 PHE D 415
REMARK 465 SER D 416
REMARK 465 TRP D 417
REMARK 465 SER D 418
REMARK 465 ASP D 419
REMARK 465 LYS D 472
REMARK 465 LYS D 473
REMARK 465 SER D 474
REMARK 465 GLY D 475
REMARK 465 GLN E 21
REMARK 465 THR E 22
REMARK 465 GLN E 23
REMARK 465 GLN E 24
REMARK 465 GLU E 25
REMARK 465 GLU E 26
REMARK 465 GLU E 27
REMARK 465 GLU E 28
REMARK 465 GLU E 29
REMARK 465 ASP E 30
REMARK 465 GLU E 31
REMARK 465 ASP E 32
REMARK 465 HIS E 33
REMARK 465 GLY E 34
REMARK 465 PRO E 35
REMARK 465 ASP E 36
REMARK 465 ASP E 37
REMARK 465 TYR E 38
REMARK 465 ASP E 39
REMARK 465 GLU E 40
REMARK 465 GLU E 41
REMARK 465 ASP E 42
REMARK 465 GLU E 43
REMARK 465 ASP E 44
REMARK 465 GLU E 45
REMARK 465 VAL E 46
REMARK 465 GLU E 47
REMARK 465 GLU E 48
REMARK 465 GLU E 49
REMARK 465 GLU E 50
REMARK 465 THR E 51
REMARK 465 ASN E 52
REMARK 465 ARG E 53
REMARK 465 LEU E 54
REMARK 465 PRO E 55
REMARK 465 GLY E 56
REMARK 465 GLY E 57
REMARK 465 ARG E 58
REMARK 465 SER E 59
REMARK 465 ARG E 60
REMARK 465 SER E 144
REMARK 465 ARG E 145
REMARK 465 VAL E 146
REMARK 465 GLN E 147
REMARK 465 ASP E 148
REMARK 465 PRO E 149
REMARK 465 THR E 150
REMARK 465 GLY E 151
REMARK 465 GLN F 21
REMARK 465 THR F 22
REMARK 465 GLN F 23
REMARK 465 GLN F 24
REMARK 465 GLU F 25
REMARK 465 GLU F 26
REMARK 465 GLU F 27
REMARK 465 GLU F 28
REMARK 465 GLU F 29
REMARK 465 ASP F 30
REMARK 465 GLU F 31
REMARK 465 ASP F 32
REMARK 465 HIS F 33
REMARK 465 GLY F 34
REMARK 465 PRO F 35
REMARK 465 ASP F 36
REMARK 465 ASP F 37
REMARK 465 TYR F 38
REMARK 465 ASP F 39
REMARK 465 GLU F 40
REMARK 465 GLU F 41
REMARK 465 ASP F 42
REMARK 465 GLU F 43
REMARK 465 ASP F 44
REMARK 465 GLU F 45
REMARK 465 VAL F 46
REMARK 465 GLU F 47
REMARK 465 GLU F 48
REMARK 465 GLU F 49
REMARK 465 GLU F 50
REMARK 465 THR F 51
REMARK 465 ASN F 52
REMARK 465 ARG F 53
REMARK 465 LEU F 54
REMARK 465 PRO F 55
REMARK 465 GLY F 56
REMARK 465 GLY F 57
REMARK 465 ARG F 58
REMARK 465 SER F 59
REMARK 465 ARG F 60
REMARK 465 VAL F 61
REMARK 465 LEU F 62
REMARK 465 LEU F 63
REMARK 465 ARG F 64
REMARK 465 SER F 144
REMARK 465 ARG F 145
REMARK 465 VAL F 146
REMARK 465 GLN F 147
REMARK 465 ASP F 148
REMARK 465 PRO F 149
REMARK 465 THR F 150
REMARK 465 GLY F 151
REMARK 465 GLN G 21
REMARK 465 THR G 22
REMARK 465 GLN G 23
REMARK 465 GLN G 24
REMARK 465 GLU G 25
REMARK 465 GLU G 26
REMARK 465 GLU G 27
REMARK 465 GLU G 28
REMARK 465 GLU G 29
REMARK 465 ASP G 30
REMARK 465 GLU G 31
REMARK 465 ASP G 32
REMARK 465 HIS G 33
REMARK 465 GLY G 34
REMARK 465 PRO G 35
REMARK 465 ASP G 36
REMARK 465 ASP G 37
REMARK 465 TYR G 38
REMARK 465 ASP G 39
REMARK 465 GLU G 40
REMARK 465 GLU G 41
REMARK 465 ASP G 42
REMARK 465 GLU G 43
REMARK 465 ASP G 44
REMARK 465 GLU G 45
REMARK 465 VAL G 46
REMARK 465 GLU G 47
REMARK 465 GLU G 48
REMARK 465 GLU G 49
REMARK 465 GLU G 50
REMARK 465 THR G 51
REMARK 465 ASN G 52
REMARK 465 ARG G 53
REMARK 465 LEU G 54
REMARK 465 PRO G 55
REMARK 465 GLY G 56
REMARK 465 GLY G 57
REMARK 465 ARG G 58
REMARK 465 SER G 59
REMARK 465 ARG G 60
REMARK 465 VAL G 61
REMARK 465 LEU G 62
REMARK 465 SER G 144
REMARK 465 ARG G 145
REMARK 465 VAL G 146
REMARK 465 GLN G 147
REMARK 465 ASP G 148
REMARK 465 PRO G 149
REMARK 465 THR G 150
REMARK 465 GLY G 151
REMARK 465 GLN H 21
REMARK 465 THR H 22
REMARK 465 GLN H 23
REMARK 465 GLN H 24
REMARK 465 GLU H 25
REMARK 465 GLU H 26
REMARK 465 GLU H 27
REMARK 465 GLU H 28
REMARK 465 GLU H 29
REMARK 465 ASP H 30
REMARK 465 GLU H 31
REMARK 465 ASP H 32
REMARK 465 HIS H 33
REMARK 465 GLY H 34
REMARK 465 PRO H 35
REMARK 465 ASP H 36
REMARK 465 ASP H 37
REMARK 465 TYR H 38
REMARK 465 ASP H 39
REMARK 465 GLU H 40
REMARK 465 GLU H 41
REMARK 465 ASP H 42
REMARK 465 GLU H 43
REMARK 465 ASP H 44
REMARK 465 GLU H 45
REMARK 465 VAL H 46
REMARK 465 GLU H 47
REMARK 465 GLU H 48
REMARK 465 GLU H 49
REMARK 465 GLU H 50
REMARK 465 THR H 51
REMARK 465 ASN H 52
REMARK 465 ARG H 53
REMARK 465 LEU H 54
REMARK 465 PRO H 55
REMARK 465 GLY H 56
REMARK 465 GLY H 57
REMARK 465 ARG H 58
REMARK 465 SER H 59
REMARK 465 ARG H 60
REMARK 465 VAL H 61
REMARK 465 LEU H 62
REMARK 465 SER H 143
REMARK 465 SER H 144
REMARK 465 ARG H 145
REMARK 465 VAL H 146
REMARK 465 GLN H 147
REMARK 465 ASP H 148
REMARK 465 PRO H 149
REMARK 465 THR H 150
REMARK 465 GLY H 151
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 SER E 70 N - CA - C ANGL. DEV. = 16.6 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 HIS A 80 172.31 -59.34
REMARK 500 GLU A 119 -168.80 -171.75
REMARK 500 SER A 159 -122.48 58.56
REMARK 500 ASN A 177 -72.83 -53.34
REMARK 500 ASN A 188 -0.05 76.73
REMARK 500 TYR A 233 77.75 -118.95
REMARK 500 LEU A 303 17.16 -158.43
REMARK 500 ASN A 359 68.58 29.88
REMARK 500 LEU A 403 -50.32 -127.42
REMARK 500 SER A 423 137.99 -38.66
REMARK 500 SER B 159 -115.10 44.02
REMARK 500 ASN B 177 -73.78 -53.14
REMARK 500 ASP B 183 72.38 41.41
REMARK 500 TYR B 233 78.08 -119.54
REMARK 500 LEU B 303 16.42 -157.94
REMARK 500 ASN B 359 68.84 29.96
REMARK 500 SER B 423 137.31 -39.47
REMARK 500 HIS C 80 170.50 -58.83
REMARK 500 SER C 106 175.79 -59.73
REMARK 500 SER C 159 -131.72 49.82
REMARK 500 ASN C 177 -73.05 -52.94
REMARK 500 ASP C 183 73.19 42.76
REMARK 500 TYR C 233 78.38 -119.01
REMARK 500 LEU C 303 19.23 -158.37
REMARK 500 ASN C 359 68.30 29.67
REMARK 500 SER C 423 135.70 -39.49
REMARK 500 GLU D 119 -177.31 -66.10
REMARK 500 SER D 159 -113.60 37.28
REMARK 500 ASN D 177 -73.45 -53.83
REMARK 500 ASP D 183 73.15 43.51
REMARK 500 PHE D 212 60.97 -151.09
REMARK 500 TYR D 233 77.85 -119.52
REMARK 500 LEU D 303 19.56 -158.38
REMARK 500 ASN D 359 68.28 30.06
REMARK 500 LEU D 403 -50.79 -127.76
REMARK 500 SER D 423 137.01 -38.73
REMARK 500 SER E 70 54.62 25.45
REMARK 500 ASP E 74 68.98 -104.30
REMARK 500 GLN E 132 38.31 -92.75
REMARK 500 SER F 70 73.89 34.22
REMARK 500 ASP F 74 43.91 -99.07
REMARK 500 CYS F 83 153.22 -44.81
REMARK 500 SER G 70 65.99 27.04
REMARK 500 GLN G 142 48.43 -107.25
REMARK 500 SER H 70 62.68 25.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 194 O
REMARK 620 2 ARG A 197 O 67.4
REMARK 620 3 SER A 199 OG 74.0 88.3
REMARK 620 4 ASP A 202 OD1 160.7 128.7 94.2
REMARK 620 5 ASP A 202 OD2 136.7 76.4 82.4 53.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 374 OE1
REMARK 620 2 GLU E 122 OE2 67.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 194 O
REMARK 620 2 ARG B 197 O 71.0
REMARK 620 3 SER B 199 OG 75.2 87.5
REMARK 620 4 ASP B 202 OD1 158.7 120.9 87.2
REMARK 620 5 ASP B 202 OD2 134.4 73.2 76.1 48.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 374 OE1
REMARK 620 2 GLU F 122 OE2 83.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 194 O
REMARK 620 2 ARG C 197 O 66.7
REMARK 620 3 SER C 199 OG 75.8 87.0
REMARK 620 4 ASP C 202 OD1 167.4 122.2 95.0
REMARK 620 5 ASP C 202 OD2 133.6 72.6 80.8 51.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 374 OE1
REMARK 620 2 GLU C 374 OE2 43.0
REMARK 620 3 GLU G 122 OE2 77.8 109.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA D 194 O
REMARK 620 2 ARG D 197 O 68.0
REMARK 620 3 SER D 199 OG 72.0 83.2
REMARK 620 4 ASP D 202 OD1 156.5 120.8 87.0
REMARK 620 5 ASP D 202 OD2 129.6 71.3 74.9 49.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 374 OE1
REMARK 620 2 GLU D 374 OE2 46.0
REMARK 620 3 GLU H 122 OE2 79.4 116.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound
REMARK 800 to ASN A 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 502 bound
REMARK 800 to ASN B 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound
REMARK 800 to ASN B 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 502 bound
REMARK 800 to ASN C 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 501 bound
REMARK 800 to ASN C 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 502 bound
REMARK 800 to ASN D 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 501 bound
REMARK 800 to ASN D 386
DBREF 6OAZ A 28 475 UNP P06858 LIPL_HUMAN 28 475
DBREF 6OAZ B 28 475 UNP P06858 LIPL_HUMAN 28 475
DBREF 6OAZ C 28 475 UNP P06858 LIPL_HUMAN 28 475
DBREF 6OAZ D 28 475 UNP P06858 LIPL_HUMAN 28 475
DBREF 6OAZ E 21 151 UNP Q8IV16 HDBP1_HUMAN 21 151
DBREF 6OAZ F 21 151 UNP Q8IV16 HDBP1_HUMAN 21 151
DBREF 6OAZ G 21 151 UNP Q8IV16 HDBP1_HUMAN 21 151
DBREF 6OAZ H 21 151 UNP Q8IV16 HDBP1_HUMAN 21 151
SEQADV 6OAZ ASP E 78 UNP Q8IV16 ASN 78 ENGINEERED MUTATION
SEQADV 6OAZ ASP E 82 UNP Q8IV16 ASN 82 ENGINEERED MUTATION
SEQADV 6OAZ ASP F 78 UNP Q8IV16 ASN 78 ENGINEERED MUTATION
SEQADV 6OAZ ASP F 82 UNP Q8IV16 ASN 82 ENGINEERED MUTATION
SEQADV 6OAZ ASP G 78 UNP Q8IV16 ASN 78 ENGINEERED MUTATION
SEQADV 6OAZ ASP G 82 UNP Q8IV16 ASN 82 ENGINEERED MUTATION
SEQADV 6OAZ ASP H 78 UNP Q8IV16 ASN 78 ENGINEERED MUTATION
SEQADV 6OAZ ASP H 82 UNP Q8IV16 ASN 82 ENGINEERED MUTATION
SEQRES 1 A 448 ALA ASP GLN ARG ARG ASP PHE ILE ASP ILE GLU SER LYS
SEQRES 2 A 448 PHE ALA LEU ARG THR PRO GLU ASP THR ALA GLU ASP THR
SEQRES 3 A 448 CYS HIS LEU ILE PRO GLY VAL ALA GLU SER VAL ALA THR
SEQRES 4 A 448 CYS HIS PHE ASN HIS SER SER LYS THR PHE MET VAL ILE
SEQRES 5 A 448 HIS GLY TRP THR VAL THR GLY MET TYR GLU SER TRP VAL
SEQRES 6 A 448 PRO LYS LEU VAL ALA ALA LEU TYR LYS ARG GLU PRO ASP
SEQRES 7 A 448 SER ASN VAL ILE VAL VAL ASP TRP LEU SER ARG ALA GLN
SEQRES 8 A 448 GLU HIS TYR PRO VAL SER ALA GLY TYR THR LYS LEU VAL
SEQRES 9 A 448 GLY GLN ASP VAL ALA ARG PHE ILE ASN TRP MET GLU GLU
SEQRES 10 A 448 GLU PHE ASN TYR PRO LEU ASP ASN VAL HIS LEU LEU GLY
SEQRES 11 A 448 TYR SER LEU GLY ALA HIS ALA ALA GLY ILE ALA GLY SER
SEQRES 12 A 448 LEU THR ASN LYS LYS VAL ASN ARG ILE THR GLY LEU ASP
SEQRES 13 A 448 PRO ALA GLY PRO ASN PHE GLU TYR ALA GLU ALA PRO SER
SEQRES 14 A 448 ARG LEU SER PRO ASP ASP ALA ASP PHE VAL ASP VAL LEU
SEQRES 15 A 448 HIS THR PHE THR ARG GLY SER PRO GLY ARG SER ILE GLY
SEQRES 16 A 448 ILE GLN LYS PRO VAL GLY HIS VAL ASP ILE TYR PRO ASN
SEQRES 17 A 448 GLY GLY THR PHE GLN PRO GLY CYS ASN ILE GLY GLU ALA
SEQRES 18 A 448 ILE ARG VAL ILE ALA GLU ARG GLY LEU GLY ASP VAL ASP
SEQRES 19 A 448 GLN LEU VAL LYS CYS SER HIS GLU ARG SER ILE HIS LEU
SEQRES 20 A 448 PHE ILE ASP SER LEU LEU ASN GLU GLU ASN PRO SER LYS
SEQRES 21 A 448 ALA TYR ARG CYS SER SER LYS GLU ALA PHE GLU LYS GLY
SEQRES 22 A 448 LEU CYS LEU SER CYS ARG LYS ASN ARG CYS ASN ASN LEU
SEQRES 23 A 448 GLY TYR GLU ILE ASN LYS VAL ARG ALA LYS ARG SER SER
SEQRES 24 A 448 LYS MET TYR LEU LYS THR ARG SER GLN MET PRO TYR LYS
SEQRES 25 A 448 VAL PHE HIS TYR GLN VAL LYS ILE HIS PHE SER GLY THR
SEQRES 26 A 448 GLU SER GLU THR HIS THR ASN GLN ALA PHE GLU ILE SER
SEQRES 27 A 448 LEU TYR GLY THR VAL ALA GLU SER GLU ASN ILE PRO PHE
SEQRES 28 A 448 THR LEU PRO GLU VAL SER THR ASN LYS THR TYR SER PHE
SEQRES 29 A 448 LEU ILE TYR THR GLU VAL ASP ILE GLY GLU LEU LEU MET
SEQRES 30 A 448 LEU LYS LEU LYS TRP LYS SER ASP SER TYR PHE SER TRP
SEQRES 31 A 448 SER ASP TRP TRP SER SER PRO GLY PHE ALA ILE GLN LYS
SEQRES 32 A 448 ILE ARG VAL LYS ALA GLY GLU THR GLN LYS LYS VAL ILE
SEQRES 33 A 448 PHE CYS SER ARG GLU LYS VAL SER HIS LEU GLN LYS GLY
SEQRES 34 A 448 LYS ALA PRO ALA VAL PHE VAL LYS CYS HIS ASP LYS SER
SEQRES 35 A 448 LEU ASN LYS LYS SER GLY
SEQRES 1 B 448 ALA ASP GLN ARG ARG ASP PHE ILE ASP ILE GLU SER LYS
SEQRES 2 B 448 PHE ALA LEU ARG THR PRO GLU ASP THR ALA GLU ASP THR
SEQRES 3 B 448 CYS HIS LEU ILE PRO GLY VAL ALA GLU SER VAL ALA THR
SEQRES 4 B 448 CYS HIS PHE ASN HIS SER SER LYS THR PHE MET VAL ILE
SEQRES 5 B 448 HIS GLY TRP THR VAL THR GLY MET TYR GLU SER TRP VAL
SEQRES 6 B 448 PRO LYS LEU VAL ALA ALA LEU TYR LYS ARG GLU PRO ASP
SEQRES 7 B 448 SER ASN VAL ILE VAL VAL ASP TRP LEU SER ARG ALA GLN
SEQRES 8 B 448 GLU HIS TYR PRO VAL SER ALA GLY TYR THR LYS LEU VAL
SEQRES 9 B 448 GLY GLN ASP VAL ALA ARG PHE ILE ASN TRP MET GLU GLU
SEQRES 10 B 448 GLU PHE ASN TYR PRO LEU ASP ASN VAL HIS LEU LEU GLY
SEQRES 11 B 448 TYR SER LEU GLY ALA HIS ALA ALA GLY ILE ALA GLY SER
SEQRES 12 B 448 LEU THR ASN LYS LYS VAL ASN ARG ILE THR GLY LEU ASP
SEQRES 13 B 448 PRO ALA GLY PRO ASN PHE GLU TYR ALA GLU ALA PRO SER
SEQRES 14 B 448 ARG LEU SER PRO ASP ASP ALA ASP PHE VAL ASP VAL LEU
SEQRES 15 B 448 HIS THR PHE THR ARG GLY SER PRO GLY ARG SER ILE GLY
SEQRES 16 B 448 ILE GLN LYS PRO VAL GLY HIS VAL ASP ILE TYR PRO ASN
SEQRES 17 B 448 GLY GLY THR PHE GLN PRO GLY CYS ASN ILE GLY GLU ALA
SEQRES 18 B 448 ILE ARG VAL ILE ALA GLU ARG GLY LEU GLY ASP VAL ASP
SEQRES 19 B 448 GLN LEU VAL LYS CYS SER HIS GLU ARG SER ILE HIS LEU
SEQRES 20 B 448 PHE ILE ASP SER LEU LEU ASN GLU GLU ASN PRO SER LYS
SEQRES 21 B 448 ALA TYR ARG CYS SER SER LYS GLU ALA PHE GLU LYS GLY
SEQRES 22 B 448 LEU CYS LEU SER CYS ARG LYS ASN ARG CYS ASN ASN LEU
SEQRES 23 B 448 GLY TYR GLU ILE ASN LYS VAL ARG ALA LYS ARG SER SER
SEQRES 24 B 448 LYS MET TYR LEU LYS THR ARG SER GLN MET PRO TYR LYS
SEQRES 25 B 448 VAL PHE HIS TYR GLN VAL LYS ILE HIS PHE SER GLY THR
SEQRES 26 B 448 GLU SER GLU THR HIS THR ASN GLN ALA PHE GLU ILE SER
SEQRES 27 B 448 LEU TYR GLY THR VAL ALA GLU SER GLU ASN ILE PRO PHE
SEQRES 28 B 448 THR LEU PRO GLU VAL SER THR ASN LYS THR TYR SER PHE
SEQRES 29 B 448 LEU ILE TYR THR GLU VAL ASP ILE GLY GLU LEU LEU MET
SEQRES 30 B 448 LEU LYS LEU LYS TRP LYS SER ASP SER TYR PHE SER TRP
SEQRES 31 B 448 SER ASP TRP TRP SER SER PRO GLY PHE ALA ILE GLN LYS
SEQRES 32 B 448 ILE ARG VAL LYS ALA GLY GLU THR GLN LYS LYS VAL ILE
SEQRES 33 B 448 PHE CYS SER ARG GLU LYS VAL SER HIS LEU GLN LYS GLY
SEQRES 34 B 448 LYS ALA PRO ALA VAL PHE VAL LYS CYS HIS ASP LYS SER
SEQRES 35 B 448 LEU ASN LYS LYS SER GLY
SEQRES 1 C 448 ALA ASP GLN ARG ARG ASP PHE ILE ASP ILE GLU SER LYS
SEQRES 2 C 448 PHE ALA LEU ARG THR PRO GLU ASP THR ALA GLU ASP THR
SEQRES 3 C 448 CYS HIS LEU ILE PRO GLY VAL ALA GLU SER VAL ALA THR
SEQRES 4 C 448 CYS HIS PHE ASN HIS SER SER LYS THR PHE MET VAL ILE
SEQRES 5 C 448 HIS GLY TRP THR VAL THR GLY MET TYR GLU SER TRP VAL
SEQRES 6 C 448 PRO LYS LEU VAL ALA ALA LEU TYR LYS ARG GLU PRO ASP
SEQRES 7 C 448 SER ASN VAL ILE VAL VAL ASP TRP LEU SER ARG ALA GLN
SEQRES 8 C 448 GLU HIS TYR PRO VAL SER ALA GLY TYR THR LYS LEU VAL
SEQRES 9 C 448 GLY GLN ASP VAL ALA ARG PHE ILE ASN TRP MET GLU GLU
SEQRES 10 C 448 GLU PHE ASN TYR PRO LEU ASP ASN VAL HIS LEU LEU GLY
SEQRES 11 C 448 TYR SER LEU GLY ALA HIS ALA ALA GLY ILE ALA GLY SER
SEQRES 12 C 448 LEU THR ASN LYS LYS VAL ASN ARG ILE THR GLY LEU ASP
SEQRES 13 C 448 PRO ALA GLY PRO ASN PHE GLU TYR ALA GLU ALA PRO SER
SEQRES 14 C 448 ARG LEU SER PRO ASP ASP ALA ASP PHE VAL ASP VAL LEU
SEQRES 15 C 448 HIS THR PHE THR ARG GLY SER PRO GLY ARG SER ILE GLY
SEQRES 16 C 448 ILE GLN LYS PRO VAL GLY HIS VAL ASP ILE TYR PRO ASN
SEQRES 17 C 448 GLY GLY THR PHE GLN PRO GLY CYS ASN ILE GLY GLU ALA
SEQRES 18 C 448 ILE ARG VAL ILE ALA GLU ARG GLY LEU GLY ASP VAL ASP
SEQRES 19 C 448 GLN LEU VAL LYS CYS SER HIS GLU ARG SER ILE HIS LEU
SEQRES 20 C 448 PHE ILE ASP SER LEU LEU ASN GLU GLU ASN PRO SER LYS
SEQRES 21 C 448 ALA TYR ARG CYS SER SER LYS GLU ALA PHE GLU LYS GLY
SEQRES 22 C 448 LEU CYS LEU SER CYS ARG LYS ASN ARG CYS ASN ASN LEU
SEQRES 23 C 448 GLY TYR GLU ILE ASN LYS VAL ARG ALA LYS ARG SER SER
SEQRES 24 C 448 LYS MET TYR LEU LYS THR ARG SER GLN MET PRO TYR LYS
SEQRES 25 C 448 VAL PHE HIS TYR GLN VAL LYS ILE HIS PHE SER GLY THR
SEQRES 26 C 448 GLU SER GLU THR HIS THR ASN GLN ALA PHE GLU ILE SER
SEQRES 27 C 448 LEU TYR GLY THR VAL ALA GLU SER GLU ASN ILE PRO PHE
SEQRES 28 C 448 THR LEU PRO GLU VAL SER THR ASN LYS THR TYR SER PHE
SEQRES 29 C 448 LEU ILE TYR THR GLU VAL ASP ILE GLY GLU LEU LEU MET
SEQRES 30 C 448 LEU LYS LEU LYS TRP LYS SER ASP SER TYR PHE SER TRP
SEQRES 31 C 448 SER ASP TRP TRP SER SER PRO GLY PHE ALA ILE GLN LYS
SEQRES 32 C 448 ILE ARG VAL LYS ALA GLY GLU THR GLN LYS LYS VAL ILE
SEQRES 33 C 448 PHE CYS SER ARG GLU LYS VAL SER HIS LEU GLN LYS GLY
SEQRES 34 C 448 LYS ALA PRO ALA VAL PHE VAL LYS CYS HIS ASP LYS SER
SEQRES 35 C 448 LEU ASN LYS LYS SER GLY
SEQRES 1 D 448 ALA ASP GLN ARG ARG ASP PHE ILE ASP ILE GLU SER LYS
SEQRES 2 D 448 PHE ALA LEU ARG THR PRO GLU ASP THR ALA GLU ASP THR
SEQRES 3 D 448 CYS HIS LEU ILE PRO GLY VAL ALA GLU SER VAL ALA THR
SEQRES 4 D 448 CYS HIS PHE ASN HIS SER SER LYS THR PHE MET VAL ILE
SEQRES 5 D 448 HIS GLY TRP THR VAL THR GLY MET TYR GLU SER TRP VAL
SEQRES 6 D 448 PRO LYS LEU VAL ALA ALA LEU TYR LYS ARG GLU PRO ASP
SEQRES 7 D 448 SER ASN VAL ILE VAL VAL ASP TRP LEU SER ARG ALA GLN
SEQRES 8 D 448 GLU HIS TYR PRO VAL SER ALA GLY TYR THR LYS LEU VAL
SEQRES 9 D 448 GLY GLN ASP VAL ALA ARG PHE ILE ASN TRP MET GLU GLU
SEQRES 10 D 448 GLU PHE ASN TYR PRO LEU ASP ASN VAL HIS LEU LEU GLY
SEQRES 11 D 448 TYR SER LEU GLY ALA HIS ALA ALA GLY ILE ALA GLY SER
SEQRES 12 D 448 LEU THR ASN LYS LYS VAL ASN ARG ILE THR GLY LEU ASP
SEQRES 13 D 448 PRO ALA GLY PRO ASN PHE GLU TYR ALA GLU ALA PRO SER
SEQRES 14 D 448 ARG LEU SER PRO ASP ASP ALA ASP PHE VAL ASP VAL LEU
SEQRES 15 D 448 HIS THR PHE THR ARG GLY SER PRO GLY ARG SER ILE GLY
SEQRES 16 D 448 ILE GLN LYS PRO VAL GLY HIS VAL ASP ILE TYR PRO ASN
SEQRES 17 D 448 GLY GLY THR PHE GLN PRO GLY CYS ASN ILE GLY GLU ALA
SEQRES 18 D 448 ILE ARG VAL ILE ALA GLU ARG GLY LEU GLY ASP VAL ASP
SEQRES 19 D 448 GLN LEU VAL LYS CYS SER HIS GLU ARG SER ILE HIS LEU
SEQRES 20 D 448 PHE ILE ASP SER LEU LEU ASN GLU GLU ASN PRO SER LYS
SEQRES 21 D 448 ALA TYR ARG CYS SER SER LYS GLU ALA PHE GLU LYS GLY
SEQRES 22 D 448 LEU CYS LEU SER CYS ARG LYS ASN ARG CYS ASN ASN LEU
SEQRES 23 D 448 GLY TYR GLU ILE ASN LYS VAL ARG ALA LYS ARG SER SER
SEQRES 24 D 448 LYS MET TYR LEU LYS THR ARG SER GLN MET PRO TYR LYS
SEQRES 25 D 448 VAL PHE HIS TYR GLN VAL LYS ILE HIS PHE SER GLY THR
SEQRES 26 D 448 GLU SER GLU THR HIS THR ASN GLN ALA PHE GLU ILE SER
SEQRES 27 D 448 LEU TYR GLY THR VAL ALA GLU SER GLU ASN ILE PRO PHE
SEQRES 28 D 448 THR LEU PRO GLU VAL SER THR ASN LYS THR TYR SER PHE
SEQRES 29 D 448 LEU ILE TYR THR GLU VAL ASP ILE GLY GLU LEU LEU MET
SEQRES 30 D 448 LEU LYS LEU LYS TRP LYS SER ASP SER TYR PHE SER TRP
SEQRES 31 D 448 SER ASP TRP TRP SER SER PRO GLY PHE ALA ILE GLN LYS
SEQRES 32 D 448 ILE ARG VAL LYS ALA GLY GLU THR GLN LYS LYS VAL ILE
SEQRES 33 D 448 PHE CYS SER ARG GLU LYS VAL SER HIS LEU GLN LYS GLY
SEQRES 34 D 448 LYS ALA PRO ALA VAL PHE VAL LYS CYS HIS ASP LYS SER
SEQRES 35 D 448 LEU ASN LYS LYS SER GLY
SEQRES 1 E 131 GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS
SEQRES 2 E 131 GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL
SEQRES 3 E 131 GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER
SEQRES 4 E 131 ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO
SEQRES 5 E 131 ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS
SEQRES 6 E 131 GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR
SEQRES 7 E 131 GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR
SEQRES 8 E 131 ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR
SEQRES 9 E 131 GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN
SEQRES 10 E 131 VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR
SEQRES 11 E 131 GLY
SEQRES 1 F 131 GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS
SEQRES 2 F 131 GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL
SEQRES 3 F 131 GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER
SEQRES 4 F 131 ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO
SEQRES 5 F 131 ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS
SEQRES 6 F 131 GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR
SEQRES 7 F 131 GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR
SEQRES 8 F 131 ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR
SEQRES 9 F 131 GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN
SEQRES 10 F 131 VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR
SEQRES 11 F 131 GLY
SEQRES 1 G 131 GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS
SEQRES 2 G 131 GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL
SEQRES 3 G 131 GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER
SEQRES 4 G 131 ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO
SEQRES 5 G 131 ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS
SEQRES 6 G 131 GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR
SEQRES 7 G 131 GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR
SEQRES 8 G 131 ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR
SEQRES 9 G 131 GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN
SEQRES 10 G 131 VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR
SEQRES 11 G 131 GLY
SEQRES 1 H 131 GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS
SEQRES 2 H 131 GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL
SEQRES 3 H 131 GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER
SEQRES 4 H 131 ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO
SEQRES 5 H 131 ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS
SEQRES 6 H 131 GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR
SEQRES 7 H 131 GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR
SEQRES 8 H 131 ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR
SEQRES 9 H 131 GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN
SEQRES 10 H 131 VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR
SEQRES 11 H 131 GLY
HET NAG A 501 14
HET NAG A 502 14
HET EDO A 503 4
HET EDO A 504 4
HET CA A 505 1
HET CA A 506 1
HET NAG B 501 14
HET NAG B 502 14
HET EDO B 503 4
HET EDO B 504 4
HET CA B 505 1
HET CA B 506 1
HET NAG C 501 14
HET NAG C 502 14
HET EDO C 503 4
HET EDO C 504 4
HET CA C 505 1
HET CA C 506 1
HET NAG D 501 14
HET NAG D 502 14
HET EDO D 503 4
HET EDO D 504 4
HET CA D 505 1
HET CA D 506 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CA CALCIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 9 NAG 8(C8 H15 N O6)
FORMUL 11 EDO 8(C2 H6 O2)
FORMUL 13 CA 8(CA 2+)
FORMUL 33 HOH *21(H2 O)
HELIX 1 AA1 VAL A 60 CYS A 67 1 8
HELIX 2 AA2 SER A 90 GLU A 103 1 14
HELIX 3 AA3 TRP A 113 GLN A 118 1 6
HELIX 4 AA4 HIS A 120 TYR A 127 1 8
HELIX 5 AA5 TYR A 127 PHE A 146 1 20
HELIX 6 AA6 PRO A 149 ASP A 151 5 3
HELIX 7 AA7 LEU A 160 THR A 172 1 13
HELIX 8 AA8 GLU A 193 ARG A 197 5 5
HELIX 9 AA9 SER A 199 ALA A 203 5 5
HELIX 10 AB1 GLY A 236 THR A 238 5 3
HELIX 11 AB2 LYS A 265 ASN A 281 1 17
HELIX 12 AB3 SER A 293 GLU A 298 1 6
HELIX 13 AB4 CYS A 305 ASN A 308 5 4
HELIX 14 AB5 GLN B 30 PHE B 34 5 5
HELIX 15 AB6 VAL B 60 CYS B 67 1 8
HELIX 16 AB7 SER B 90 GLU B 103 1 14
HELIX 17 AB8 TRP B 113 GLN B 118 1 6
HELIX 18 AB9 HIS B 120 TYR B 127 1 8
HELIX 19 AC1 TYR B 127 ASN B 147 1 21
HELIX 20 AC2 PRO B 149 ASP B 151 5 3
HELIX 21 AC3 LEU B 160 THR B 172 1 13
HELIX 22 AC4 GLU B 193 ARG B 197 5 5
HELIX 23 AC5 SER B 199 ALA B 203 5 5
HELIX 24 AC6 GLY B 236 THR B 238 5 3
HELIX 25 AC7 LYS B 265 ASN B 281 1 17
HELIX 26 AC8 SER B 293 LYS B 299 1 7
HELIX 27 AC9 CYS B 305 ASN B 308 5 4
HELIX 28 AD1 GLN C 30 PHE C 34 5 5
HELIX 29 AD2 VAL C 60 CYS C 67 1 8
HELIX 30 AD3 SER C 90 GLU C 103 1 14
HELIX 31 AD4 TRP C 113 GLN C 118 1 6
HELIX 32 AD5 HIS C 120 TYR C 127 1 8
HELIX 33 AD6 TYR C 127 ASN C 147 1 21
HELIX 34 AD7 PRO C 149 ASP C 151 5 3
HELIX 35 AD8 SER C 159 THR C 172 1 14
HELIX 36 AD9 GLU C 193 ARG C 197 5 5
HELIX 37 AE1 SER C 199 ALA C 203 5 5
HELIX 38 AE2 GLY C 236 THR C 238 5 3
HELIX 39 AE3 LYS C 265 ASN C 281 1 17
HELIX 40 AE4 SER C 293 LYS C 299 1 7
HELIX 41 AE5 CYS C 305 ASN C 308 5 4
HELIX 42 AE6 GLN D 30 PHE D 34 5 5
HELIX 43 AE7 VAL D 60 CYS D 67 1 8
HELIX 44 AE8 SER D 90 GLU D 103 1 14
HELIX 45 AE9 TRP D 113 GLN D 118 1 6
HELIX 46 AF1 HIS D 120 TYR D 127 1 8
HELIX 47 AF2 TYR D 127 ASN D 147 1 21
HELIX 48 AF3 LEU D 160 THR D 172 1 13
HELIX 49 AF4 GLU D 193 ARG D 197 5 5
HELIX 50 AF5 SER D 199 ALA D 203 5 5
HELIX 51 AF6 LYS D 265 ASN D 281 1 17
HELIX 52 AF7 SER D 293 LYS D 299 1 7
HELIX 53 AF8 CYS D 305 ASN D 308 5 4
HELIX 54 AF9 PRO F 139 SER F 143 5 5
HELIX 55 AG1 PRO G 139 SER G 143 5 5
SHEET 1 AA111 HIS A 55 LEU A 56 0
SHEET 2 AA111 LYS A 40 ARG A 44 -1 N PHE A 41 O LEU A 56
SHEET 3 AA111 ASN A 107 ASP A 112 -1 O VAL A 110 N ALA A 42
SHEET 4 AA111 THR A 75 ILE A 79 1 N PHE A 76 O ASN A 107
SHEET 5 AA111 VAL A 153 SER A 159 1 O LEU A 156 N MET A 77
SHEET 6 AA111 ARG A 178 PRO A 184 1 O LEU A 182 N GLY A 157
SHEET 7 AA111 PHE A 205 LEU A 209 1 O LEU A 209 N GLY A 181
SHEET 8 AA111 VAL A 230 PRO A 234 1 O ILE A 232 N VAL A 208
SHEET 9 AA111 SER A 326 LEU A 330 1 O MET A 328 N TYR A 233
SHEET 10 AA111 LYS A 287 ARG A 290 -1 N TYR A 289 O TYR A 329
SHEET 11 AA111 CYS A 310 ASN A 312 -1 O ASN A 311 N ALA A 288
SHEET 1 AA2 8 GLU A 372 SER A 384 0
SHEET 2 AA2 8 THR A 356 GLY A 368 -1 N PHE A 362 O PHE A 378
SHEET 3 AA2 8 LEU A 402 LYS A 410 -1 O LEU A 403 N TYR A 367
SHEET 4 AA2 8 ALA A 460 SER A 469 -1 O LYS A 464 N LEU A 403
SHEET 5 AA2 8 LYS A 440 SER A 446 -1 N ILE A 443 O CYS A 465
SHEET 6 AA2 8 LYS A 430 ALA A 435 -1 N VAL A 433 O VAL A 442
SHEET 7 AA2 8 PHE A 341 PHE A 349 -1 N LYS A 346 O ARG A 432
SHEET 8 AA2 8 LYS A 387 THR A 395 -1 O PHE A 391 N VAL A 345
SHEET 1 AA3 2 GLY A 425 ILE A 428 0
SHEET 2 AA3 2 SER A 451 GLN A 454 -1 O LEU A 453 N PHE A 426
SHEET 1 AA411 HIS B 55 LEU B 56 0
SHEET 2 AA411 LYS B 40 ARG B 44 -1 N PHE B 41 O LEU B 56
SHEET 3 AA411 ASN B 107 ASP B 112 -1 O ASP B 112 N LYS B 40
SHEET 4 AA411 THR B 75 ILE B 79 1 N PHE B 76 O ASN B 107
SHEET 5 AA411 VAL B 153 SER B 159 1 O LEU B 156 N MET B 77
SHEET 6 AA411 ARG B 178 PRO B 184 1 O LEU B 182 N GLY B 157
SHEET 7 AA411 PHE B 205 LEU B 209 1 O LEU B 209 N GLY B 181
SHEET 8 AA411 VAL B 230 PRO B 234 1 O ILE B 232 N VAL B 208
SHEET 9 AA411 SER B 326 LEU B 330 1 O MET B 328 N TYR B 233
SHEET 10 AA411 LYS B 287 ARG B 290 -1 N TYR B 289 O TYR B 329
SHEET 11 AA411 CYS B 310 ASN B 312 -1 O ASN B 311 N ALA B 288
SHEET 1 AA5 8 GLU B 372 SER B 384 0
SHEET 2 AA5 8 THR B 356 GLY B 368 -1 N PHE B 362 O PHE B 378
SHEET 3 AA5 8 LEU B 402 LYS B 410 -1 O LEU B 403 N TYR B 367
SHEET 4 AA5 8 ALA B 460 SER B 469 -1 O LYS B 464 N LEU B 403
SHEET 5 AA5 8 LYS B 440 SER B 446 -1 N ILE B 443 O CYS B 465
SHEET 6 AA5 8 LYS B 430 ALA B 435 -1 N VAL B 433 O VAL B 442
SHEET 7 AA5 8 PHE B 341 PHE B 349 -1 N LYS B 346 O ARG B 432
SHEET 8 AA5 8 LYS B 387 THR B 395 -1 O PHE B 391 N VAL B 345
SHEET 1 AA6 2 GLY B 425 ILE B 428 0
SHEET 2 AA6 2 SER B 451 GLN B 454 -1 O LEU B 453 N PHE B 426
SHEET 1 AA711 HIS C 55 LEU C 56 0
SHEET 2 AA711 LYS C 40 ARG C 44 -1 N PHE C 41 O LEU C 56
SHEET 3 AA711 ASN C 107 ASP C 112 -1 O ASP C 112 N LYS C 40
SHEET 4 AA711 THR C 75 ILE C 79 1 N PHE C 76 O ASN C 107
SHEET 5 AA711 VAL C 153 TYR C 158 1 O LEU C 156 N MET C 77
SHEET 6 AA711 ARG C 178 LEU C 182 1 O LEU C 182 N GLY C 157
SHEET 7 AA711 PHE C 205 LEU C 209 1 O LEU C 209 N GLY C 181
SHEET 8 AA711 VAL C 230 PRO C 234 1 O ILE C 232 N VAL C 208
SHEET 9 AA711 SER C 326 LEU C 330 1 O MET C 328 N TYR C 233
SHEET 10 AA711 LYS C 287 ARG C 290 -1 N TYR C 289 O TYR C 329
SHEET 11 AA711 CYS C 310 ASN C 312 -1 O ASN C 311 N ALA C 288
SHEET 1 AA8 8 GLU C 372 SER C 384 0
SHEET 2 AA8 8 THR C 356 GLY C 368 -1 N PHE C 362 O PHE C 378
SHEET 3 AA8 8 LEU C 402 LYS C 410 -1 O LEU C 403 N TYR C 367
SHEET 4 AA8 8 ALA C 460 SER C 469 -1 O LYS C 464 N LEU C 403
SHEET 5 AA8 8 LYS C 440 SER C 446 -1 N ILE C 443 O CYS C 465
SHEET 6 AA8 8 LYS C 430 ALA C 435 -1 N VAL C 433 O VAL C 442
SHEET 7 AA8 8 PHE C 341 PHE C 349 -1 N LYS C 346 O ARG C 432
SHEET 8 AA8 8 LYS C 387 THR C 395 -1 O PHE C 391 N VAL C 345
SHEET 1 AA9 2 GLY C 425 ILE C 428 0
SHEET 2 AA9 2 SER C 451 GLN C 454 -1 O SER C 451 N ILE C 428
SHEET 1 AB111 HIS D 55 LEU D 56 0
SHEET 2 AB111 LYS D 40 ARG D 44 -1 N PHE D 41 O LEU D 56
SHEET 3 AB111 ASN D 107 ASP D 112 -1 O ASP D 112 N LYS D 40
SHEET 4 AB111 THR D 75 ILE D 79 1 N PHE D 76 O ASN D 107
SHEET 5 AB111 VAL D 153 TYR D 158 1 O LEU D 156 N MET D 77
SHEET 6 AB111 ARG D 178 LEU D 182 1 O LEU D 182 N GLY D 157
SHEET 7 AB111 PHE D 205 LEU D 209 1 O ASP D 207 N GLY D 181
SHEET 8 AB111 VAL D 230 PRO D 234 1 O ILE D 232 N VAL D 208
SHEET 9 AB111 SER D 326 LEU D 330 1 O MET D 328 N TYR D 233
SHEET 10 AB111 LYS D 287 ARG D 290 -1 N TYR D 289 O TYR D 329
SHEET 11 AB111 CYS D 310 ASN D 312 -1 O ASN D 311 N ALA D 288
SHEET 1 AB2 8 GLU D 372 SER D 384 0
SHEET 2 AB2 8 THR D 356 GLY D 368 -1 N PHE D 362 O PHE D 378
SHEET 3 AB2 8 LEU D 402 LYS D 410 -1 O LEU D 403 N TYR D 367
SHEET 4 AB2 8 ALA D 460 SER D 469 -1 O LYS D 464 N LEU D 403
SHEET 5 AB2 8 LYS D 440 SER D 446 -1 N ILE D 443 O CYS D 465
SHEET 6 AB2 8 LYS D 430 ALA D 435 -1 N VAL D 433 O VAL D 442
SHEET 7 AB2 8 PHE D 341 PHE D 349 -1 N LYS D 346 O ARG D 432
SHEET 8 AB2 8 LYS D 387 THR D 395 -1 O PHE D 391 N VAL D 345
SHEET 1 AB3 2 GLY D 425 ILE D 428 0
SHEET 2 AB3 2 SER D 451 GLN D 454 -1 O SER D 451 N ILE D 428
SHEET 1 AB4 2 ARG E 64 TYR E 66 0
SHEET 2 AB4 2 THR E 80 ASP E 82 -1 O GLN E 81 N CYS E 65
SHEET 1 AB5 5 CYS E 68 PRO E 72 0
SHEET 2 AB5 5 LEU E 102 THR E 111 -1 O THR E 108 N CYS E 68
SHEET 3 AB5 5 THR E 88 ASN E 97 -1 N LEU E 92 O SER E 107
SHEET 4 AB5 5 THR E 124 CYS E 131 -1 O THR E 127 N ILE E 93
SHEET 5 AB5 5 THR E 118 VAL E 121 -1 N LYS E 119 O VAL E 126
SHEET 1 AB6 5 CYS F 68 PRO F 72 0
SHEET 2 AB6 5 LEU F 102 THR F 111 -1 O HIS F 106 N LEU F 71
SHEET 3 AB6 5 THR F 88 ASN F 97 -1 N GLY F 96 O LEU F 103
SHEET 4 AB6 5 THR F 124 CYS F 131 -1 O THR F 127 N ILE F 93
SHEET 5 AB6 5 ILE F 117 VAL F 121 -1 N ILE F 117 O MET F 128
SHEET 1 AB7 2 ARG G 64 TYR G 66 0
SHEET 2 AB7 2 THR G 80 ASP G 82 -1 O GLN G 81 N CYS G 65
SHEET 1 AB8 5 CYS G 68 PRO G 72 0
SHEET 2 AB8 5 LEU G 102 THR G 111 -1 O HIS G 106 N LEU G 71
SHEET 3 AB8 5 THR G 88 ASN G 97 -1 N LEU G 92 O SER G 107
SHEET 4 AB8 5 THR G 124 CYS G 131 -1 O GLN G 125 N HIS G 95
SHEET 5 AB8 5 ILE G 117 VAL G 121 -1 N LYS G 119 O VAL G 126
SHEET 1 AB9 2 ARG H 64 TYR H 66 0
SHEET 2 AB9 2 THR H 80 ASP H 82 -1 O GLN H 81 N CYS H 65
SHEET 1 AC1 5 CYS H 68 PRO H 72 0
SHEET 2 AC1 5 LEU H 102 THR H 111 -1 O HIS H 106 N LEU H 71
SHEET 3 AC1 5 THR H 88 ASN H 97 -1 N LEU H 92 O SER H 107
SHEET 4 AC1 5 THR H 124 CYS H 131 -1 O CYS H 131 N CYS H 89
SHEET 5 AC1 5 ILE H 117 VAL H 121 -1 N LYS H 119 O VAL H 126
SSBOND 1 CYS A 54 CYS A 67 1555 1555 2.05
SSBOND 2 CYS A 243 CYS A 266 1555 1555 2.05
SSBOND 3 CYS A 291 CYS A 302 1555 1555 2.05
SSBOND 4 CYS A 305 CYS A 310 1555 1555 2.06
SSBOND 5 CYS A 445 CYS A 465 1555 1555 2.08
SSBOND 6 CYS B 54 CYS B 67 1555 1555 2.05
SSBOND 7 CYS B 243 CYS B 266 1555 1555 2.05
SSBOND 8 CYS B 291 CYS B 302 1555 1555 2.05
SSBOND 9 CYS B 305 CYS B 310 1555 1555 2.08
SSBOND 10 CYS B 445 CYS B 465 1555 1555 2.06
SSBOND 11 CYS C 54 CYS C 67 1555 1555 2.05
SSBOND 12 CYS C 243 CYS C 266 1555 1555 2.05
SSBOND 13 CYS C 291 CYS C 302 1555 1555 2.05
SSBOND 14 CYS C 305 CYS C 310 1555 1555 2.06
SSBOND 15 CYS C 445 CYS C 465 1555 1555 2.07
SSBOND 16 CYS D 54 CYS D 67 1555 1555 2.05
SSBOND 17 CYS D 243 CYS D 266 1555 1555 2.04
SSBOND 18 CYS D 291 CYS D 302 1555 1555 2.05
SSBOND 19 CYS D 305 CYS D 310 1555 1555 2.09
SSBOND 20 CYS D 445 CYS D 465 1555 1555 2.07
SSBOND 21 CYS E 65 CYS E 89 1555 1555 2.02
SSBOND 22 CYS E 68 CYS E 77 1555 1555 2.04
SSBOND 23 CYS E 83 CYS E 110 1555 1555 2.04
SSBOND 24 CYS E 114 CYS E 130 1555 1555 2.04
SSBOND 25 CYS E 131 CYS E 136 1555 1555 2.04
SSBOND 26 CYS F 65 CYS F 89 1555 1555 2.03
SSBOND 27 CYS F 68 CYS F 77 1555 1555 2.03
SSBOND 28 CYS F 83 CYS F 110 1555 1555 2.04
SSBOND 29 CYS F 114 CYS F 130 1555 1555 2.04
SSBOND 30 CYS F 131 CYS F 136 1555 1555 2.04
SSBOND 31 CYS G 65 CYS G 89 1555 1555 2.03
SSBOND 32 CYS G 68 CYS G 77 1555 1555 2.04
SSBOND 33 CYS G 83 CYS G 110 1555 1555 2.04
SSBOND 34 CYS G 114 CYS G 130 1555 1555 2.04
SSBOND 35 CYS G 131 CYS G 136 1555 1555 2.04
SSBOND 36 CYS H 65 CYS H 89 1555 1555 2.03
SSBOND 37 CYS H 68 CYS H 77 1555 1555 2.04
SSBOND 38 CYS H 83 CYS H 110 1555 1555 2.05
SSBOND 39 CYS H 114 CYS H 130 1555 1555 2.04
SSBOND 40 CYS H 131 CYS H 136 1555 1555 2.04
LINK ND2 ASN A 70 C1 NAG A 502 1555 1555 1.44
LINK O ALA A 194 CA CA A 505 1555 1555 2.53
LINK O ARG A 197 CA CA A 505 1555 1555 2.70
LINK OG SER A 199 CA CA A 505 1555 1555 2.24
LINK OD1 ASP A 202 CA CA A 505 1555 1555 2.39
LINK OD2 ASP A 202 CA CA A 505 1555 1555 2.51
LINK OE1 GLU A 374 CA CA A 506 1555 1555 3.19
LINK ND2 ASN A 386 C1 NAG A 501 1555 1555 1.43
LINK ND2 ASN B 70 C1 NAG B 502 1555 1555 1.44
LINK O ALA B 194 CA CA B 505 1555 1555 2.34
LINK O ARG B 197 CA CA B 505 1555 1555 2.64
LINK OG SER B 199 CA CA B 505 1555 1555 2.36
LINK OD1 ASP B 202 CA CA B 505 1555 1555 2.57
LINK OD2 ASP B 202 CA CA B 505 1555 1555 2.76
LINK OE1 GLU B 374 CA CA B 506 1555 1555 2.60
LINK ND2 ASN B 386 C1 NAG B 501 1555 1555 1.43
LINK ND2 ASN C 70 C1 NAG C 502 1555 1555 1.44
LINK O ALA C 194 CA CA C 505 1555 1555 2.48
LINK O ARG C 197 CA CA C 505 1555 1555 2.78
LINK OG SER C 199 CA CA C 505 1555 1555 2.21
LINK OD1 ASP C 202 CA CA C 505 1555 1555 2.42
LINK OD2 ASP C 202 CA CA C 505 1555 1555 2.65
LINK OE1 GLU C 374 CA CA C 506 1555 1555 2.69
LINK OE2 GLU C 374 CA CA C 506 1555 1555 3.19
LINK ND2 ASN C 386 C1 NAG C 501 1555 1555 1.43
LINK ND2 ASN D 70 C1 NAG D 502 1555 1555 1.44
LINK O ALA D 194 CA CA D 505 1555 1555 2.45
LINK O ARG D 197 CA CA D 505 1555 1555 2.75
LINK OG SER D 199 CA CA D 505 1555 1555 2.45
LINK OD1 ASP D 202 CA CA D 505 1555 1555 2.49
LINK OD2 ASP D 202 CA CA D 505 1555 1555 2.72
LINK OE1 GLU D 374 CA CA D 506 1555 1555 2.66
LINK OE2 GLU D 374 CA CA D 506 1555 1555 2.94
LINK ND2 ASN D 386 C1 NAG D 501 1555 1555 1.43
LINK OE2 GLU E 122 CA CA A 506 1555 1555 2.81
LINK OE2 GLU F 122 CA CA B 506 1555 1555 2.73
LINK OE2 GLU G 122 CA CA C 506 1555 1555 2.45
LINK OE2 GLU H 122 CA CA D 506 1555 1555 2.69
CISPEP 1 MET A 336 PRO A 337 0 -2.55
CISPEP 2 MET B 336 PRO B 337 0 -2.24
CISPEP 3 MET C 336 PRO C 337 0 -2.87
CISPEP 4 MET D 336 PRO D 337 0 -3.13
SITE 1 AC1 8 HIS A 80 GLY A 81 TRP A 82 MET A 87
SITE 2 AC1 8 TYR A 88 GLU A 89 TRP A 91 TYR A 158
SITE 1 AC2 5 GLU A 38 ASP A 112 TRP A 113 SER A 115
SITE 2 AC2 5 ARG A 116
SITE 1 AC3 4 ALA A 194 ARG A 197 SER A 199 ASP A 202
SITE 1 AC4 2 GLU A 374 GLU E 122
SITE 1 AC5 7 HIS B 80 GLY B 81 TRP B 82 MET B 87
SITE 2 AC5 7 TYR B 88 GLU B 89 TRP B 91
SITE 1 AC6 4 GLU B 38 ASP B 112 TRP B 113 SER B 115
SITE 1 AC7 5 ALA B 194 PRO B 195 ARG B 197 SER B 199
SITE 2 AC7 5 ASP B 202
SITE 1 AC8 2 GLU B 374 GLU F 122
SITE 1 AC9 6 HIS C 80 GLY C 81 TRP C 82 MET C 87
SITE 2 AC9 6 TYR C 88 GLU C 89
SITE 1 AD1 6 GLU C 38 SER C 39 ASP C 112 TRP C 113
SITE 2 AD1 6 SER C 115 ARG C 116
SITE 1 AD2 4 ALA C 194 ARG C 197 SER C 199 ASP C 202
SITE 1 AD3 2 GLU C 374 GLU G 122
SITE 1 AD4 7 HIS D 80 GLY D 81 TRP D 82 MET D 87
SITE 2 AD4 7 TYR D 88 GLU D 89 TYR D 158
SITE 1 AD5 6 GLU D 38 ASP D 112 TRP D 113 LEU D 114
SITE 2 AD5 6 SER D 115 ARG D 116
SITE 1 AD6 5 ALA D 194 PRO D 195 ARG D 197 SER D 199
SITE 2 AD6 5 ASP D 202
SITE 1 AD7 2 GLU D 374 GLU H 122
SITE 1 AD8 3 ASN A 70 SER A 73 ASP A 105
SITE 1 AD9 4 GLY A 351 THR A 352 THR A 385 ASN A 386
SITE 1 AE1 3 ASN B 70 SER B 73 ASP B 105
SITE 1 AE2 4 GLY B 351 THR B 352 THR B 385 ASN B 386
SITE 1 AE3 3 ASN C 70 SER C 73 ASP C 105
SITE 1 AE4 4 GLY C 351 THR C 352 THR C 385 ASN C 386
SITE 1 AE5 3 ASN D 70 SER D 73 ASP D 105
SITE 1 AE6 4 LYS A 307 GLY D 351 THR D 352 ASN D 386
CRYST1 157.000 191.940 96.060 90.00 90.00 90.00 P 21 21 2 16
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 0.006369 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005210 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010410 0.00000
TER 3308 ASN A 471
TER 6616 ASN B 471
TER 9924 ASN C 471
TER 13232 ASN D 471
TER 13861 SER E 143
TER 14456 SER F 143
TER 15070 SER G 143
TER 15678 GLN H 142
MASTER 976 0 24 55 110 0 33 615843 8 274 184
END |