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HEADER HYDROLASE/PROTEIN BINDING 18-MAR-19 6OAU
TITLE APO STRUCTURE OF WT LIPOPROTEIN LIPASE IN COMPLEX WITH GPIHBP1 MUTANT
TITLE 2 N78D N82D PRODUCED IN GNTI-DEFICIENT HEK293-F CELLS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPROTEIN LIPASE;
COMPND 3 CHAIN: A, B;
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: C, D;
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 6OAU 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. 2.48 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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 45819
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2308
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) : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 917
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2421
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 876
REMARK 3 BIN R VALUE (WORKING SET) : 0.2412
REMARK 3 BIN FREE R VALUE : 0.2616
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.47
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 41
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 : 7934
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.26680
REMARK 3 B22 (A**2) : 19.53750
REMARK 3 B33 (A**2) : -22.80430
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.34000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.380
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.379
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.247
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.410
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.257
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 : 0.860
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.846
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8220 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11157 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2834 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1378 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8220 ; 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 : 1088 ; 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 : 8780 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.15
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.40
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6OAU 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_1000240300.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-17
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45839
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 88.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.54600
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: BUSTER 2.11.7
REMARK 200 STARTING MODEL: 1LPA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM MALONATE, 20% PEG3350, 4%
REMARK 280 2-PROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 88.74000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.62500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 88.74000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.62500
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
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: 2720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 2440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 28
REMARK 465 ASP A 29
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 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 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 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 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 LYS B 472
REMARK 465 LYS B 473
REMARK 465 SER B 474
REMARK 465 GLY B 475
REMARK 465 GLN C 21
REMARK 465 THR C 22
REMARK 465 GLN C 23
REMARK 465 GLN C 24
REMARK 465 GLU C 25
REMARK 465 GLU C 26
REMARK 465 GLU C 27
REMARK 465 GLU C 28
REMARK 465 GLU C 29
REMARK 465 ASP C 30
REMARK 465 GLU C 31
REMARK 465 ASP C 32
REMARK 465 HIS C 33
REMARK 465 GLY C 34
REMARK 465 PRO C 35
REMARK 465 ASP C 36
REMARK 465 ASP C 37
REMARK 465 TYR C 38
REMARK 465 ASP C 39
REMARK 465 GLU C 40
REMARK 465 GLU C 41
REMARK 465 ASP C 42
REMARK 465 GLU C 43
REMARK 465 ASP C 44
REMARK 465 GLU C 45
REMARK 465 VAL C 46
REMARK 465 GLU C 47
REMARK 465 GLU C 48
REMARK 465 GLU C 49
REMARK 465 GLU C 50
REMARK 465 THR C 51
REMARK 465 ASN C 52
REMARK 465 ARG C 53
REMARK 465 LEU C 54
REMARK 465 PRO C 55
REMARK 465 GLY C 56
REMARK 465 GLY C 57
REMARK 465 ARG C 58
REMARK 465 SER C 59
REMARK 465 ARG C 60
REMARK 465 VAL C 61
REMARK 465 LEU C 62
REMARK 465 SER C 144
REMARK 465 ARG C 145
REMARK 465 VAL C 146
REMARK 465 GLN C 147
REMARK 465 ASP C 148
REMARK 465 PRO C 149
REMARK 465 THR C 150
REMARK 465 GLY C 151
REMARK 465 GLN D 21
REMARK 465 THR D 22
REMARK 465 GLN D 23
REMARK 465 GLN D 24
REMARK 465 GLU D 25
REMARK 465 GLU D 26
REMARK 465 GLU D 27
REMARK 465 GLU D 28
REMARK 465 GLU D 29
REMARK 465 ASP D 30
REMARK 465 GLU D 31
REMARK 465 ASP D 32
REMARK 465 HIS D 33
REMARK 465 GLY D 34
REMARK 465 PRO D 35
REMARK 465 ASP D 36
REMARK 465 ASP D 37
REMARK 465 TYR D 38
REMARK 465 ASP D 39
REMARK 465 GLU D 40
REMARK 465 GLU D 41
REMARK 465 ASP D 42
REMARK 465 GLU D 43
REMARK 465 ASP D 44
REMARK 465 GLU D 45
REMARK 465 VAL D 46
REMARK 465 GLU D 47
REMARK 465 GLU D 48
REMARK 465 GLU D 49
REMARK 465 GLU D 50
REMARK 465 THR D 51
REMARK 465 ASN D 52
REMARK 465 ARG D 53
REMARK 465 LEU D 54
REMARK 465 PRO D 55
REMARK 465 GLY D 56
REMARK 465 GLY D 57
REMARK 465 ARG D 58
REMARK 465 SER D 59
REMARK 465 ARG D 60
REMARK 465 VAL D 61
REMARK 465 LEU D 62
REMARK 465 ARG D 145
REMARK 465 VAL D 146
REMARK 465 GLN D 147
REMARK 465 ASP D 148
REMARK 465 PRO D 149
REMARK 465 THR D 150
REMARK 465 GLY D 151
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 90 -8.70 -59.31
REMARK 500 GLN A 118 54.91 -111.52
REMARK 500 SER A 159 -103.11 58.54
REMARK 500 ASN A 188 -5.29 86.70
REMARK 500 PHE A 212 54.59 -145.39
REMARK 500 ASN A 284 76.31 -116.87
REMARK 500 LYS A 307 74.30 39.17
REMARK 500 LYS A 319 67.42 -68.49
REMARK 500 SER A 354 97.14 -67.51
REMARK 500 LEU A 403 -47.40 -130.37
REMARK 500 GLU A 448 -154.46 -91.11
REMARK 500 SER B 90 -8.92 -59.54
REMARK 500 SER B 159 -107.12 51.86
REMARK 500 ASN B 188 -8.36 85.32
REMARK 500 ASN B 284 75.37 -116.69
REMARK 500 LYS B 307 73.70 39.24
REMARK 500 LYS B 319 67.39 -67.62
REMARK 500 SER B 354 97.14 -66.80
REMARK 500 GLU B 448 -154.86 -93.27
REMARK 500 SER C 70 76.10 18.88
REMARK 500 ASP C 74 44.33 -98.95
REMARK 500 GLU C 99 34.74 -84.48
REMARK 500 SER C 100 14.97 -152.51
REMARK 500 SER D 70 77.40 19.48
REMARK 500 GLU D 99 33.49 -83.08
REMARK 500 SER D 100 14.04 -151.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NAG A 502
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 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 194 O
REMARK 620 2 ARG A 197 O 72.5
REMARK 620 3 ASP A 202 OD1 149.9 134.3
REMARK 620 4 ASP A 202 OD2 146.8 83.5 51.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 194 O
REMARK 620 2 ARG B 197 O 65.2
REMARK 620 3 ASP B 202 OD1 164.1 125.6
REMARK 620 4 ASP B 202 OD2 134.1 74.3 52.0
REMARK 620 5 HOH B 628 O 95.5 160.4 73.9 124.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
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: AC5
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: AC6
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: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound
REMARK 800 to ASN B 386
DBREF 6OAU A 28 475 UNP P06858 LIPL_HUMAN 28 475
DBREF 6OAU B 28 475 UNP P06858 LIPL_HUMAN 28 475
DBREF 6OAU C 21 151 UNP Q8IV16 HDBP1_HUMAN 21 151
DBREF 6OAU D 21 151 UNP Q8IV16 HDBP1_HUMAN 21 151
SEQADV 6OAU ASP C 78 UNP Q8IV16 ASN 78 ENGINEERED MUTATION
SEQADV 6OAU ASP C 82 UNP Q8IV16 ASN 82 ENGINEERED MUTATION
SEQADV 6OAU ASP D 78 UNP Q8IV16 ASN 78 ENGINEERED MUTATION
SEQADV 6OAU ASP D 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 131 GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS
SEQRES 2 C 131 GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL
SEQRES 3 C 131 GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER
SEQRES 4 C 131 ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO
SEQRES 5 C 131 ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS
SEQRES 6 C 131 GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR
SEQRES 7 C 131 GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR
SEQRES 8 C 131 ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR
SEQRES 9 C 131 GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN
SEQRES 10 C 131 VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR
SEQRES 11 C 131 GLY
SEQRES 1 D 131 GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS
SEQRES 2 D 131 GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL
SEQRES 3 D 131 GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER
SEQRES 4 D 131 ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO
SEQRES 5 D 131 ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS
SEQRES 6 D 131 GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR
SEQRES 7 D 131 GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR
SEQRES 8 D 131 ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR
SEQRES 9 D 131 GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN
SEQRES 10 D 131 VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR
SEQRES 11 D 131 GLY
HET NAG A 501 14
HET NAG A 502 14
HET MLI A 503 7
HET CA A 504 1
HET NAG B 501 14
HET NAG B 502 14
HET CA B 503 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MLI MALONATE ION
HETNAM CA CALCIUM ION
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 7 MLI C3 H2 O4 2-
FORMUL 8 CA 2(CA 2+)
FORMUL 12 HOH *83(H2 O)
HELIX 1 AA1 GLN A 30 ILE A 35 5 6
HELIX 2 AA2 VAL A 60 CYS A 67 1 8
HELIX 3 AA3 SER A 90 GLU A 103 1 14
HELIX 4 AA4 TRP A 113 GLN A 118 1 6
HELIX 5 AA5 HIS A 120 ALA A 125 1 6
HELIX 6 AA6 TYR A 127 ASN A 147 1 21
HELIX 7 AA7 PRO A 149 ASP A 151 5 3
HELIX 8 AA8 SER A 159 SER A 170 1 12
HELIX 9 AA9 GLU A 193 ARG A 197 5 5
HELIX 10 AB1 SER A 199 ASP A 201 5 3
HELIX 11 AB2 ASP A 261 ASN A 281 1 21
HELIX 12 AB3 SER A 293 LYS A 299 1 7
HELIX 13 AB4 GLN B 30 ILE B 35 5 6
HELIX 14 AB5 VAL B 60 CYS B 67 1 8
HELIX 15 AB6 SER B 90 GLU B 103 1 14
HELIX 16 AB7 TRP B 113 GLN B 118 1 6
HELIX 17 AB8 HIS B 120 TYR B 127 1 8
HELIX 18 AB9 TYR B 127 ASN B 147 1 21
HELIX 19 AC1 PRO B 149 ASP B 151 5 3
HELIX 20 AC2 SER B 159 SER B 170 1 12
HELIX 21 AC3 GLU B 193 ARG B 197 5 5
HELIX 22 AC4 SER B 199 ASP B 201 5 3
HELIX 23 AC5 ASP B 261 ASN B 281 1 21
HELIX 24 AC6 SER B 293 LYS B 299 1 7
HELIX 25 AC7 PRO D 139 SER D 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 ASP A 112 N LYS A 40
SHEET 4 AA111 THR A 75 ILE A 79 1 N VAL A 78 O VAL A 111
SHEET 5 AA111 VAL A 153 TYR A 158 1 O LEU A 156 N MET A 77
SHEET 6 AA111 VAL A 176 LEU A 182 1 O THR A 180 N LEU A 155
SHEET 7 AA111 ALA A 203 LEU A 209 1 O ASP A 204 N VAL A 176
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 ASP A 231
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 LEU A 366 O SER A 373
SHEET 3 AA2 8 LEU A 402 TRP A 409 -1 O LYS A 408 N GLU A 363
SHEET 4 AA2 8 ALA A 460 SER A 469 -1 O PHE A 462 N LEU A 405
SHEET 5 AA2 8 LYS A 440 SER A 446 -1 N CYS A 445 O VAL A 463
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 ILE A 393 N TYR A 343
SHEET 1 AA3 2 GLY A 425 ILE A 428 0
SHEET 2 AA3 2 SER A 451 GLN A 454 -1 O SER A 451 N ILE A 428
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 VAL B 78 O VAL B 111
SHEET 5 AA411 VAL B 153 TYR B 158 1 O LEU B 156 N ILE B 79
SHEET 6 AA411 VAL B 176 LEU B 182 1 O THR B 180 N LEU B 155
SHEET 7 AA411 ALA B 203 LEU B 209 1 O ASP B 204 N VAL B 176
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 ASP B 231
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 LEU B 366 O SER B 373
SHEET 3 AA5 8 LEU B 402 TRP B 409 -1 O LEU B 403 N TYR B 367
SHEET 4 AA5 8 ALA B 460 SER B 469 -1 O PHE B 462 N LEU B 405
SHEET 5 AA5 8 LYS B 440 SER B 446 -1 N CYS B 445 O VAL B 463
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 SER B 451 N ILE B 428
SHEET 1 AA7 2 ARG C 64 TYR C 66 0
SHEET 2 AA7 2 THR C 80 ASP C 82 -1 O GLN C 81 N CYS C 65
SHEET 1 AA8 5 CYS C 68 PRO C 72 0
SHEET 2 AA8 5 GLY C 101 THR C 111 -1 O HIS C 106 N LEU C 71
SHEET 3 AA8 5 THR C 88 THR C 98 -1 N GLY C 96 O LEU C 103
SHEET 4 AA8 5 THR C 124 CYS C 131 -1 O THR C 127 N ILE C 93
SHEET 5 AA8 5 ILE C 117 THR C 120 -1 N ILE C 117 O MET C 128
SHEET 1 AA9 2 ARG D 64 TYR D 66 0
SHEET 2 AA9 2 THR D 80 ASP D 82 -1 O GLN D 81 N CYS D 65
SHEET 1 AB1 5 CYS D 68 PRO D 72 0
SHEET 2 AB1 5 GLY D 101 THR D 111 -1 O THR D 108 N CYS D 68
SHEET 3 AB1 5 THR D 88 THR D 98 -1 N GLY D 96 O LEU D 103
SHEET 4 AB1 5 THR D 124 CYS D 131 -1 O THR D 127 N ILE D 93
SHEET 5 AB1 5 ILE D 117 THR D 120 -1 N ILE D 117 O MET D 128
SSBOND 1 CYS A 54 CYS A 67 1555 1555 2.06
SSBOND 2 CYS A 243 CYS A 266 1555 1555 2.06
SSBOND 3 CYS A 291 CYS A 302 1555 1555 2.05
SSBOND 4 CYS A 305 CYS A 310 1555 1555 2.05
SSBOND 5 CYS A 445 CYS A 465 1555 1555 2.06
SSBOND 6 CYS B 54 CYS B 67 1555 1555 2.06
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 2.07
SSBOND 10 CYS B 445 CYS B 465 1555 1555 2.07
SSBOND 11 CYS C 65 CYS C 89 1555 1555 2.04
SSBOND 12 CYS C 68 CYS C 77 1555 1555 2.03
SSBOND 13 CYS C 83 CYS C 110 1555 1555 2.04
SSBOND 14 CYS C 114 CYS C 130 1555 1555 2.05
SSBOND 15 CYS C 131 CYS C 136 1555 1555 2.03
SSBOND 16 CYS D 65 CYS D 89 1555 1555 2.02
SSBOND 17 CYS D 68 CYS D 77 1555 1555 2.04
SSBOND 18 CYS D 83 CYS D 110 1555 1555 2.05
SSBOND 19 CYS D 114 CYS D 130 1555 1555 2.03
SSBOND 20 CYS D 131 CYS D 136 1555 1555 2.04
LINK ND2 ASN A 70 C1 NAG A 502 1555 1555 1.43
LINK O ALA A 194 CA CA A 504 1555 1555 2.36
LINK O ARG A 197 CA CA A 504 1555 1555 2.59
LINK OD1 ASP A 202 CA CA A 504 1555 1555 2.61
LINK OD2 ASP A 202 CA CA A 504 1555 1555 2.47
LINK ND2 ASN A 386 C1 NAG A 501 1555 1555 1.44
LINK ND2 ASN B 70 C1 NAG B 502 1555 1555 1.43
LINK O ALA B 194 CA CA B 503 1555 1555 2.45
LINK O ARG B 197 CA CA B 503 1555 1555 2.97
LINK OD1 ASP B 202 CA CA B 503 1555 1555 2.39
LINK OD2 ASP B 202 CA CA B 503 1555 1555 2.58
LINK ND2 ASN B 386 C1 NAG B 501 1555 1555 1.43
LINK CA CA B 503 O HOH B 628 1555 1555 2.62
CISPEP 1 MET A 336 PRO A 337 0 3.21
CISPEP 2 MET B 336 PRO B 337 0 -0.89
SITE 1 AC1 8 GLU A 38 SER A 39 LYS A 40 ASP A 112
SITE 2 AC1 8 TRP A 113 LEU A 114 SER A 115 ARG A 116
SITE 1 AC2 4 ALA A 194 ARG A 197 SER A 199 ASP A 202
SITE 1 AC3 5 ALA B 194 ARG B 197 SER B 199 ASP B 202
SITE 2 AC3 5 HOH B 628
SITE 1 AC4 2 ASN A 70 SER A 73
SITE 1 AC5 7 GLY A 351 THR A 352 GLU A 353 SER A 354
SITE 2 AC5 7 THR A 385 ASN A 386 ARG B 324
SITE 1 AC6 3 ASN B 70 SER B 72 SER B 73
SITE 1 AC7 6 GLY B 351 THR B 352 GLU B 353 SER B 354
SITE 2 AC7 6 THR B 385 ASN B 386
CRYST1 177.480 97.250 77.210 90.00 93.47 90.00 C 1 2 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 0.005634 0.000000 0.000342 0.00000
SCALE2 0.000000 0.010283 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012975 0.00000
TER 3352 ASN A 471
TER 6714 ASN B 471
TER 7328 SER C 143
TER 7948 SER D 144
MASTER 493 0 7 25 56 0 11 6 8082 4 119 92
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