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HEADER HYDROLASE 26-JUL-18 6E7K
TITLE STRUCTURE OF THE LIPOPROTEIN LIPASE GPIHBP1 COMPLEX THAT MEDIATES
TITLE 2 PLASMA TRIGLYCERIDE HYDROLYSIS
CAVEAT 6E7K ILE D 117 HAS WRONG CHIRALITY AT ATOM CA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPROTEIN LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 28-475;
COMPND 5 SYNONYM: LPL;
COMPND 6 EC: 3.1.1.34;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED HIGH DENSITY
COMPND 11 LIPOPROTEIN-BINDING PROTEIN 1;
COMPND 12 CHAIN: C, D;
COMPND 13 FRAGMENT: UNP RESIDUES 21-151;
COMPND 14 SYNONYM: GPIHBP1, GPI-ANCHORED HDL-BINDING PROTEIN 1, HIGH DENSITY
COMPND 15 LIPOPROTEIN-BINDING PROTEIN 1;
COMPND 16 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: LPL, LIPD;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HT1080;
SOURCE 10 EXPRESSION_SYSTEM_TISSUE: CONNECTIVE TISSUE;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PZ804N;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: GPIHBP1, HBP1;
SOURCE 18 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 19 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;
SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-1
KEYWDS HYDROLASE-COFACTOR COMPLEX, LIPID DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BIRRANE,M.MEIYAPPAN
REVDAT 1 19-DEC-18 6E7K 0
JRNL AUTH G.BIRRANE,A.BEIGNEUX,B.DWYER,B.STRACK-LOGUE,K.KRISTENSEN,
JRNL AUTH 2 O.FRANCONE,L.FONG,H.MERTENS,C.PAN,M.PLOUG,S.YOUNG,
JRNL AUTH 3 M.MEIYAPPAN
JRNL TITL STRUCTURE OF THE LIPOPROTEIN LIPASE-GPIHBP1 COMPLEX THAT
JRNL TITL 2 MEDIATES PLASMA TRIGLYCERIDE HYDROLYSIS
JRNL REF PROC.NATL.ACAD.SCI.USA 2018
JRNL REFN ESSN 1091-6490
JRNL DOI 10.1073/PNAS.1817984116
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 35568
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1833
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2611
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.3860
REMARK 3 BIN FREE R VALUE SET COUNT : 120
REMARK 3 BIN FREE R VALUE : 0.4010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7873
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 156
REMARK 3 SOLVENT ATOMS : 16
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 94.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.49000
REMARK 3 B22 (A**2) : -3.01000
REMARK 3 B33 (A**2) : 1.52000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.859
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.320
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.295
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.926
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8237 ; 0.010 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 7249 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11192 ; 1.433 ; 1.685
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17069 ; 0.887 ; 1.662
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 999 ; 8.572 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 392 ;38.007 ;22.806
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1373 ;18.225 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;18.563 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1124 ; 0.131 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9067 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1502 ; 0.002 ; 0.020
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): 4020 ; 1.763 ; 6.302
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4019 ; 1.762 ; 6.302
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5011 ; 2.967 ; 9.448
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5012 ; 2.967 ; 9.448
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4217 ; 2.088 ; 6.682
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4215 ; 2.088 ; 6.682
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6181 ; 3.567 ; 9.948
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 33655 ; 7.556 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 33655 ; 7.556 ; 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 33 469 B 33 469 13308 0.10 0.05
REMARK 3 2 C 62 141 D 62 141 2194 0.14 0.05
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 33 A 470
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0970 11.1150 25.8150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0211 T22: 0.3354
REMARK 3 T33: 0.1821 T12: 0.0650
REMARK 3 T13: 0.0464 T23: 0.1829
REMARK 3 L TENSOR
REMARK 3 L11: 1.6711 L22: 0.4946
REMARK 3 L33: 5.1816 L12: 0.2312
REMARK 3 L13: -0.9660 L23: -0.1587
REMARK 3 S TENSOR
REMARK 3 S11: 0.0931 S12: 0.2195 S13: 0.1538
REMARK 3 S21: 0.0053 S22: -0.1119 S23: -0.0261
REMARK 3 S31: -0.1871 S32: -0.0473 S33: 0.0189
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 32 B 470
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8840 21.0510 -11.0730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0349 T22: 0.0982
REMARK 3 T33: 0.1219 T12: 0.0429
REMARK 3 T13: -0.0389 T23: -0.0832
REMARK 3 L TENSOR
REMARK 3 L11: 1.1839 L22: 1.4928
REMARK 3 L33: 5.9195 L12: -0.5826
REMARK 3 L13: -1.3362 L23: 1.1980
REMARK 3 S TENSOR
REMARK 3 S11: -0.1166 S12: -0.0976 S13: 0.0559
REMARK 3 S21: 0.1063 S22: -0.0198 S23: 0.0692
REMARK 3 S31: -0.0709 S32: -0.1251 S33: 0.1364
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 62 C 144
REMARK 3 ORIGIN FOR THE GROUP (A): 48.2140 8.8350 -4.0990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0387 T22: 0.9242
REMARK 3 T33: 0.3717 T12: 0.0791
REMARK 3 T13: 0.0643 T23: 0.0755
REMARK 3 L TENSOR
REMARK 3 L11: 5.9041 L22: 6.4923
REMARK 3 L33: 5.1739 L12: 1.1677
REMARK 3 L13: 1.0443 L23: 1.7541
REMARK 3 S TENSOR
REMARK 3 S11: 0.0911 S12: 0.6487 S13: 0.4850
REMARK 3 S21: -0.1937 S22: 0.2217 S23: -0.4395
REMARK 3 S31: -0.3378 S32: 0.3893 S33: -0.3128
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 62 D 142
REMARK 3 ORIGIN FOR THE GROUP (A): -35.8630 32.7640 19.5460
REMARK 3 T TENSOR
REMARK 3 T11: 0.2454 T22: 0.4164
REMARK 3 T33: 0.3066 T12: 0.0579
REMARK 3 T13: 0.1799 T23: -0.0799
REMARK 3 L TENSOR
REMARK 3 L11: 7.5915 L22: 9.6199
REMARK 3 L33: 5.4386 L12: -4.0875
REMARK 3 L13: 0.3419 L23: -1.8260
REMARK 3 S TENSOR
REMARK 3 S11: -0.3000 S12: -0.3979 S13: -0.1529
REMARK 3 S21: 0.4396 S22: 0.2645 S23: 0.7718
REMARK 3 S31: 0.4113 S32: -0.3712 S33: 0.0355
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6E7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235708.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-17
REMARK 200 TEMPERATURE (KELVIN) : 125
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : BE CRL/SI ELLIPTICAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 V716.1
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 V716.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37662
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 95.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.01000
REMARK 200 FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.53000
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER V2.7.17
REMARK 200 STARTING MODEL: PDB ENTRY 1HPL
REMARK 200
REMARK 200 REMARK: CUBIC
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM MAGNESIUM ACETATE, 20% PEG3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 50.97400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.60300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.97400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.60300
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 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 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 GLN A 30
REMARK 465 ARG A 31
REMARK 465 ARG A 32
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 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 TRP A 420
REMARK 465 TRP A 421
REMARK 465 ASN A 471
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 GLN B 30
REMARK 465 ARG B 31
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 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 TRP B 420
REMARK 465 TRP B 421
REMARK 465 ASN B 471
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 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 SER D 143
REMARK 465 SER D 144
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASN B 359 O LEU B 380 1.86
REMARK 500 OG SER A 350 O ALA A 427 1.96
REMARK 500 OG1 THR B 45 O GLU B 47 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 447 NE ARG A 447 CZ 0.079
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN B 235 CB - CA - C ANGL. DEV. = 13.2 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 PHE A 34 49.36 -80.45
REMARK 500 ILE A 37 126.06 16.33
REMARK 500 ASN A 147 41.37 37.16
REMARK 500 SER A 159 -121.78 64.60
REMARK 500 ASP A 183 71.46 40.07
REMARK 500 ASN A 244 -55.91 -146.72
REMARK 500 ASP A 261 85.74 -165.07
REMARK 500 ASN A 284 47.65 -160.90
REMARK 500 CYS A 302 74.87 -119.84
REMARK 500 LEU A 303 -141.72 -90.21
REMARK 500 SER A 304 127.25 84.44
REMARK 500 ARG A 321 70.66 55.20
REMARK 500 SER A 325 -173.69 61.59
REMARK 500 SER A 326 -87.16 -143.81
REMARK 500 LYS A 327 99.45 88.42
REMARK 500 MET A 336 -139.07 -58.99
REMARK 500 PRO A 337 -36.59 7.67
REMARK 500 TYR A 338 -48.87 76.10
REMARK 500 ASN A 359 64.42 18.73
REMARK 500 LEU A 403 -52.29 -128.87
REMARK 500 SER A 423 64.20 156.24
REMARK 500 GLN A 439 55.31 33.55
REMARK 500 LYS A 455 125.57 -38.46
REMARK 500 LYS A 457 -169.70 -127.69
REMARK 500 ASP B 33 24.46 111.81
REMARK 500 PHE B 34 46.69 -76.53
REMARK 500 ILE B 37 125.20 19.50
REMARK 500 ASP B 48 72.55 68.06
REMARK 500 SER B 72 76.90 -113.81
REMARK 500 SER B 73 159.86 154.65
REMARK 500 ASN B 147 40.77 38.97
REMARK 500 SER B 159 -121.48 63.92
REMARK 500 ASP B 183 69.83 39.96
REMARK 500 ASN B 235 -140.78 58.72
REMARK 500 ASN B 244 -58.47 -149.38
REMARK 500 ASP B 261 84.83 -163.77
REMARK 500 ASN B 284 50.57 -161.39
REMARK 500 LEU B 303 -141.72 -89.11
REMARK 500 SER B 304 126.76 83.30
REMARK 500 SER B 325 -176.09 62.75
REMARK 500 SER B 326 -88.68 -145.39
REMARK 500 LYS B 327 100.31 86.62
REMARK 500 MET B 336 -139.44 -55.53
REMARK 500 PRO B 337 -36.30 5.76
REMARK 500 TYR B 338 -46.33 76.91
REMARK 500 ASN B 359 -98.79 56.34
REMARK 500 GLN B 360 123.80 70.75
REMARK 500 LEU B 403 -51.92 -128.17
REMARK 500 SER B 423 66.72 155.50
REMARK 500 GLN B 439 57.24 32.67
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 33 PHE A 34 141.64
REMARK 500 GLY A 86 MET A 87 -149.82
REMARK 500 CYS A 302 LEU A 303 145.51
REMARK 500 MET A 336 PRO A 337 -133.05
REMARK 500 ASP B 33 PHE B 34 135.77
REMARK 500 GLY B 236 GLY B 237 -141.28
REMARK 500 CYS B 302 LEU B 303 144.78
REMARK 500 MET B 336 PRO B 337 -131.45
REMARK 500 GLY D 101 LEU D 102 138.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 178 0.12 SIDE CHAIN
REMARK 500 ARG B 32 0.09 SIDE CHAIN
REMARK 500 ARG B 116 0.11 SIDE CHAIN
REMARK 500 ARG B 321 0.08 SIDE CHAIN
REMARK 500 ARG C 64 0.08 SIDE CHAIN
REMARK 500 ARG D 64 0.11 SIDE CHAIN
REMARK 500 ARG D 76 0.08 SIDE CHAIN
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 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 194 O
REMARK 620 2 ARG A 197 O 63.8
REMARK 620 3 SER A 199 OG 105.0 100.9
REMARK 620 4 ASP A 202 OD1 168.4 123.7 83.0
REMARK 620 5 ASP A 202 OD2 138.0 74.2 81.3 50.6
REMARK 620 6 HOH A 602 O 89.4 73.8 160.9 84.9 79.7
REMARK 620 7 HOH A 601 O 102.4 165.7 86.0 69.3 119.5 103.5
REMARK 620 N 1 2 3 4 5 6
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 61.8
REMARK 620 3 SER B 199 OG 105.0 102.2
REMARK 620 4 ASP B 202 OD1 165.1 128.0 84.8
REMARK 620 5 ASP B 202 OD2 137.9 76.2 84.4 53.0
REMARK 620 6 HOH B 607 O 86.4 81.3 168.4 84.5 85.8
REMARK 620 7 HOH B 602 O 97.9 156.3 94.7 69.7 122.6 85.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 505 through BMA A 508 bound to ASN A 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 502 through BMA A 504 bound to ASN A 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 501 through NAG B 503 bound to ASN B 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 504 bound
REMARK 800 to ASN B 386
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 201 bound
REMARK 800 to ASN C 78
DBREF 6E7K A 28 475 UNP P06858 LIPL_HUMAN 28 475
DBREF 6E7K B 28 475 UNP P06858 LIPL_HUMAN 28 475
DBREF 6E7K C 21 151 UNP Q8IV16 HDBP1_HUMAN 21 151
DBREF 6E7K D 21 151 UNP Q8IV16 HDBP1_HUMAN 21 151
SEQADV 6E7K ALA A 324 UNP P06858 ARG 324 ENGINEERED MUTATION
SEQADV 6E7K ALA B 324 UNP P06858 ARG 324 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 ALA 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 ALA 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 ASN LEU THR GLN ASN 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 ASN LEU THR GLN ASN 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 CA A 501 1
HET NAG A 502 14
HET NAG A 503 14
HET BMA A 504 11
HET NAG A 505 14
HET FUC A 506 10
HET NAG A 507 14
HET BMA A 508 11
HET NAG B 501 14
HET FUC B 502 10
HET NAG B 503 14
HET NAG B 504 14
HET CA B 505 1
HET NAG C 201 14
HETNAM CA CALCIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM FUC ALPHA-L-FUCOSE
FORMUL 5 CA 2(CA 2+)
FORMUL 6 NAG 8(C8 H15 N O6)
FORMUL 6 BMA 2(C6 H12 O6)
FORMUL 7 FUC 2(C6 H12 O5)
FORMUL 12 HOH *16(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 ASN A 147 1 21
HELIX 6 AA6 PRO A 149 ASP A 151 5 3
HELIX 7 AA7 LEU A 160 SER A 170 1 11
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 ASP A 261 LEU A 280 1 20
HELIX 11 AB2 SER A 293 LYS A 299 1 7
HELIX 12 AB3 CYS A 305 ASN A 308 5 4
HELIX 13 AB4 VAL B 60 CYS B 67 1 8
HELIX 14 AB5 SER B 90 GLU B 103 1 14
HELIX 15 AB6 SER B 115 GLU B 119 5 5
HELIX 16 AB7 HIS B 120 TYR B 127 1 8
HELIX 17 AB8 TYR B 127 ASN B 147 1 21
HELIX 18 AB9 PRO B 149 ASP B 151 5 3
HELIX 19 AC1 LEU B 160 SER B 170 1 11
HELIX 20 AC2 GLU B 193 ARG B 197 5 5
HELIX 21 AC3 SER B 199 ALA B 203 5 5
HELIX 22 AC4 ASP B 261 LEU B 280 1 20
HELIX 23 AC5 SER B 293 LYS B 299 1 7
SHEET 1 AA110 LYS A 40 ARG A 44 0
SHEET 2 AA110 ASN A 107 ASP A 112 -1 O ASP A 112 N LYS A 40
SHEET 3 AA110 THR A 75 ILE A 79 1 N PHE A 76 O ILE A 109
SHEET 4 AA110 VAL A 153 TYR A 158 1 O LEU A 156 N MET A 77
SHEET 5 AA110 ARG A 178 LEU A 182 1 O LEU A 182 N GLY A 157
SHEET 6 AA110 PHE A 205 LEU A 209 1 O ASP A 207 N GLY A 181
SHEET 7 AA110 VAL A 230 PRO A 234 1 O ILE A 232 N VAL A 208
SHEET 8 AA110 MET A 328 LEU A 330 1 O MET A 328 N TYR A 233
SHEET 9 AA110 LYS A 287 ARG A 290 -1 N TYR A 289 O TYR A 329
SHEET 10 AA110 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 ALA A 460 N LEU A 407
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 AA410 LYS B 40 ARG B 44 0
SHEET 2 AA410 ASN B 107 ASP B 112 -1 O VAL B 110 N ALA B 42
SHEET 3 AA410 THR B 75 ILE B 79 1 N PHE B 76 O ILE B 109
SHEET 4 AA410 VAL B 153 TYR B 158 1 O LEU B 156 N MET B 77
SHEET 5 AA410 ARG B 178 LEU B 182 1 O LEU B 182 N GLY B 157
SHEET 6 AA410 PHE B 205 LEU B 209 1 O ASP B 207 N GLY B 181
SHEET 7 AA410 VAL B 230 PRO B 234 1 O ILE B 232 N VAL B 208
SHEET 8 AA410 MET B 328 LEU B 330 1 O MET B 328 N TYR B 233
SHEET 9 AA410 LYS B 287 ARG B 290 -1 N TYR B 289 O TYR B 329
SHEET 10 AA410 CYS B 310 ASN B 312 -1 O ASN B 311 N ALA B 288
SHEET 1 AA5 8 GLU B 372 THR B 379 0
SHEET 2 AA5 8 ALA B 361 GLY B 368 -1 N PHE B 362 O PHE B 378
SHEET 3 AA5 8 LEU B 402 LYS B 410 -1 O LYS B 408 N GLU B 363
SHEET 4 AA5 8 ALA B 460 SER B 469 -1 O ALA B 460 N LEU B 407
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 ILE B 393 N TYR B 343
SHEET 1 AA6 2 THR B 356 THR B 358 0
SHEET 2 AA6 2 GLU B 382 SER B 384 -1 O VAL B 383 N HIS B 357
SHEET 1 AA7 2 ALA B 427 ILE B 428 0
SHEET 2 AA7 2 SER B 451 HIS B 452 -1 O SER B 451 N ILE B 428
SHEET 1 AA8 2 LEU C 63 TYR C 66 0
SHEET 2 AA8 2 THR C 80 CYS C 83 -1 O CYS C 83 N LEU C 63
SHEET 1 AA9 5 CYS C 68 PRO C 72 0
SHEET 2 AA9 5 LEU C 102 THR C 111 -1 O HIS C 106 N LEU C 71
SHEET 3 AA9 5 THR C 88 ASN C 97 -1 N GLY C 96 O LEU C 103
SHEET 4 AA9 5 GLN C 125 CYS C 131 -1 O THR C 127 N ILE C 93
SHEET 5 AA9 5 ILE C 117 LYS C 119 -1 N LYS C 119 O VAL C 126
SHEET 1 AB1 2 ARG D 64 TYR D 66 0
SHEET 2 AB1 2 THR D 80 ASN D 82 -1 O GLN D 81 N CYS D 65
SHEET 1 AB2 5 CYS D 68 PRO D 72 0
SHEET 2 AB2 5 LEU D 102 THR D 111 -1 O HIS D 106 N LEU D 71
SHEET 3 AB2 5 THR D 88 ASN D 97 -1 N LEU D 92 O SER D 107
SHEET 4 AB2 5 GLN D 125 CYS D 131 -1 O THR D 127 N ILE D 93
SHEET 5 AB2 5 ILE D 117 LYS D 119 -1 N LYS D 119 O VAL D 126
SSBOND 1 CYS A 54 CYS A 67 1555 1555 2.07
SSBOND 2 CYS A 243 CYS A 266 1555 1555 2.43
SSBOND 3 CYS A 291 CYS A 302 1555 1555 2.08
SSBOND 4 CYS A 305 CYS A 310 1555 1555 2.12
SSBOND 5 CYS A 445 CYS A 465 1555 1555 2.13
SSBOND 6 CYS B 54 CYS B 67 1555 1555 2.08
SSBOND 7 CYS B 243 CYS B 266 1555 1555 2.16
SSBOND 8 CYS B 291 CYS B 302 1555 1555 2.06
SSBOND 9 CYS B 305 CYS B 310 1555 1555 2.08
SSBOND 10 CYS B 445 CYS B 465 1555 1555 2.16
SSBOND 11 CYS C 68 CYS C 77 1555 1555 2.06
SSBOND 12 CYS C 83 CYS C 110 1555 1555 2.07
SSBOND 13 CYS C 89 CYS C 131 1555 1555 2.12
SSBOND 14 CYS C 89 CYS C 136 1555 1555 2.31
SSBOND 15 CYS C 114 CYS C 130 1555 1555 2.08
SSBOND 16 CYS C 131 CYS C 136 1555 1555 2.05
SSBOND 17 CYS D 65 CYS D 89 1555 1555 2.05
SSBOND 18 CYS D 68 CYS D 77 1555 1555 2.07
SSBOND 19 CYS D 83 CYS D 110 1555 1555 2.12
SSBOND 20 CYS D 114 CYS D 130 1555 1555 2.30
SSBOND 21 CYS D 131 CYS D 136 1555 1555 2.06
LINK ND2 ASN A 70 C1 NAG A 505 1555 1555 1.44
LINK O ALA A 194 CA CA A 501 1555 1555 2.36
LINK O ARG A 197 CA CA A 501 1555 1555 2.65
LINK OG SER A 199 CA CA A 501 1555 1555 2.66
LINK OD1 ASP A 202 CA CA A 501 1555 1555 2.61
LINK OD2 ASP A 202 CA CA A 501 1555 1555 2.55
LINK ND2 ASN A 386 C1 NAG A 502 1555 1555 1.40
LINK ND2 ASN B 70 C1 NAG B 501 1555 1555 1.43
LINK O ALA B 194 CA CA B 505 1555 1555 2.47
LINK O ARG B 197 CA CA B 505 1555 1555 2.67
LINK OG SER B 199 CA CA B 505 1555 1555 2.59
LINK OD1 ASP B 202 CA CA B 505 1555 1555 2.57
LINK OD2 ASP B 202 CA CA B 505 1555 1555 2.44
LINK ND2 ASN B 386 C1 NAG B 504 1555 1555 1.47
LINK ND2 ASN C 78 C1 NAG C 201 1555 1555 1.45
LINK CA CA A 501 O HOH A 602 1555 1555 2.46
LINK CA CA A 501 O HOH A 601 1555 1555 2.40
LINK O4 NAG A 502 C1 NAG A 503 1555 1555 1.43
LINK O4 NAG A 503 C1 BMA A 504 1555 1555 1.45
LINK O4 NAG A 505 C1 NAG A 507 1555 1555 1.45
LINK O6 NAG A 505 C1 FUC A 506 1555 1555 1.45
LINK O4 NAG A 507 C1 BMA A 508 1555 1555 1.47
LINK O4 NAG B 501 C1 NAG B 503 1555 1555 1.45
LINK O6 NAG B 501 C1 FUC B 502 1555 1555 1.45
LINK CA CA B 505 O HOH B 607 1555 1555 2.41
LINK CA CA B 505 O HOH B 602 1555 1555 2.38
SITE 1 AC1 7 ALA A 194 ARG A 197 SER A 199 ASP A 201
SITE 2 AC1 7 ASP A 202 HOH A 601 HOH A 602
SITE 1 AC2 6 ALA B 194 ARG B 197 SER B 199 ASP B 202
SITE 2 AC2 6 HOH B 602 HOH B 607
SITE 1 AC3 4 ASN A 70 SER A 72 SER A 73 ASP A 105
SITE 1 AC4 4 GLY A 351 THR A 352 ASN A 386 GLN D 81
SITE 1 AC5 3 ASN B 70 SER B 72 SER B 73
SITE 1 AC6 3 GLY B 351 THR B 352 ASN B 386
SITE 1 AC7 1 ASN C 78
CRYST1 101.948 153.206 95.783 90.00 90.00 90.00 P 21 21 2 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 0.009809 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006527 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010440 0.00000
TER 3311 LEU A 470
TER 6633 LEU B 470
TER 7261 SER C 144
TER 7877 GLN D 142
MASTER 698 0 14 23 56 0 9 6 8045 4 216 92
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