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HEADER TRANSFERASE 11-DEC-14 4X96
TITLE LOW RESOLUTION CRYSTAL STRUCTURE OF LECITHIN:CHOLESTEROL
TITLE 2 ACYLTRANSFERASE (LCAT; RESIDUES 21-397)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLCHOLINE-STEROL ACYLTRANSFERASE;
COMPND 3 CHAIN: D, A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 45-421;
COMPND 5 SYNONYM: LECITHIN-CHOLESTEROL ACYLTRANSFERASE,PHOSPHOLIPID-
COMPND 6 CHOLESTEROL ACYLTRANSFERASE;
COMPND 7 EC: 2.3.1.43;
COMPND 8 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: LCAT;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS HYDROLASE, PHOSPHOLIPASE, ESTERASE, ACYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GLUKHOVA,J.J.G.TESMER
REVDAT 1 25-MAR-15 4X96 0
JRNL AUTH A.GLUKHOVA,V.HINKOVSKA-GALCHEVA,R.KELLY,A.ABE,J.A.SHAYMAN,
JRNL AUTH 2 J.J.TESMER
JRNL TITL STRUCTURE AND FUNCTION OF LYSOSOMAL PHOSPHOLIPASE A2 AND
JRNL TITL 2 LECITHIN:CHOLESTEROL ACYLTRANSFERASE.
JRNL REF NAT COMMUN V. 6 6250 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 25727495
JRNL DOI 10.1038/NCOMMS7250
REMARK 2
REMARK 2 RESOLUTION. 8.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 8.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 6954
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 367
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) : 8.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 8.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 332
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 26
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12044
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 368
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 359.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.92000
REMARK 3 B22 (A**2) : -1.92000
REMARK 3 B33 (A**2) : 6.22000
REMARK 3 B12 (A**2) : -0.96000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 2.754
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 2.221
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 733.098
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.869
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.837
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12824 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 11816 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17540 ; 1.170 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27068 ; 0.866 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1496 ; 5.729 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 580 ;28.359 ;23.379
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1936 ;14.454 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 76 ;12.762 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1944 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14160 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3032 ; 0.003 ; 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): 5996 ; 6.938 ;30.927
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5995 ; 6.937 ;30.927
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7488 ;12.791 ;46.384
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 D 22 396 A 22 396 21953 0.040 0.050
REMARK 3 2 D 22 396 B 22 396 21942 0.040 0.050
REMARK 3 3 D 22 396 C 22 396 21893 0.050 0.050
REMARK 3 4 A 22 396 B 22 396 22112 0.020 0.050
REMARK 3 5 A 22 396 C 22 396 22072 0.040 0.050
REMARK 3 6 B 22 396 C 22 396 22052 0.040 0.050
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 : D 22 D 471
REMARK 3 ORIGIN FOR THE GROUP (A): 386.3447 59.7561 -71.0904
REMARK 3 T TENSOR
REMARK 3 T11: 0.4864 T22: 0.7007
REMARK 3 T33: 0.6082 T12: -0.2164
REMARK 3 T13: -0.0838 T23: 0.5427
REMARK 3 L TENSOR
REMARK 3 L11: 2.0164 L22: 2.1867
REMARK 3 L33: 3.0547 L12: -0.8374
REMARK 3 L13: 0.5613 L23: 1.9933
REMARK 3 S TENSOR
REMARK 3 S11: 0.8788 S12: -0.3205 S13: -0.2673
REMARK 3 S21: -0.6302 S22: -0.3620 S23: -0.4175
REMARK 3 S31: -0.1705 S32: -0.3598 S33: -0.5168
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 : A 22 A 471
REMARK 3 ORIGIN FOR THE GROUP (A): 382.6843 21.9454 -95.1927
REMARK 3 T TENSOR
REMARK 3 T11: 0.3095 T22: 0.3334
REMARK 3 T33: 0.6111 T12: -0.0974
REMARK 3 T13: -0.0882 T23: 0.2423
REMARK 3 L TENSOR
REMARK 3 L11: 0.9172 L22: 3.5983
REMARK 3 L33: 2.5128 L12: -0.9482
REMARK 3 L13: 1.2556 L23: -0.0579
REMARK 3 S TENSOR
REMARK 3 S11: 0.3098 S12: -0.0712 S13: -0.1083
REMARK 3 S21: -0.6020 S22: -0.5100 S23: 0.1860
REMARK 3 S31: 0.1409 S32: -0.1853 S33: 0.2002
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 : B 22 B 471
REMARK 3 ORIGIN FOR THE GROUP (A): 411.7275 92.7201 -50.1267
REMARK 3 T TENSOR
REMARK 3 T11: 0.3445 T22: 0.5947
REMARK 3 T33: 0.4234 T12: -0.0632
REMARK 3 T13: 0.0142 T23: -0.1581
REMARK 3 L TENSOR
REMARK 3 L11: 1.9980 L22: 3.3797
REMARK 3 L33: 2.3448 L12: -1.2969
REMARK 3 L13: -0.3747 L23: -2.1400
REMARK 3 S TENSOR
REMARK 3 S11: 0.3029 S12: -0.1108 S13: -0.3299
REMARK 3 S21: -0.0620 S22: 0.0691 S23: 0.5596
REMARK 3 S31: -0.2563 S32: 0.0792 S33: -0.3720
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 : C 22 C 471
REMARK 3 ORIGIN FOR THE GROUP (A): 395.9484 100.2498 -92.3567
REMARK 3 T TENSOR
REMARK 3 T11: 0.4269 T22: 0.5477
REMARK 3 T33: 0.1566 T12: 0.1263
REMARK 3 T13: 0.0403 T23: -0.1539
REMARK 3 L TENSOR
REMARK 3 L11: 3.6180 L22: 2.2189
REMARK 3 L33: 1.1426 L12: 1.0941
REMARK 3 L13: -1.3018 L23: -0.5534
REMARK 3 S TENSOR
REMARK 3 S11: 0.1507 S12: -0.6386 S13: 0.2419
REMARK 3 S21: -0.4321 S22: -0.3269 S23: -0.0253
REMARK 3 S31: 0.2277 S32: 0.0559 S33: 0.1762
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4X96 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-14
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 : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, AIMLESS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7324
REMARK 200 RESOLUTION RANGE HIGH (A) : 8.690
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.18900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 8.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 8.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.52900
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: 4X90
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 87.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 13.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA ACETATE PH 5.0, 13%
REMARK 280 ISOPROPANOL, AND 200 MM CACL2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 183.62900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 106.01825
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.35633
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 183.62900
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 106.01825
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 62.35633
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 183.62900
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 106.01825
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.35633
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 212.03651
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 124.71267
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 212.03651
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 124.71267
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 212.03651
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 124.71267
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 HIS D 21
REMARK 465 ALA D 397
REMARK 465 HIS D 398
REMARK 465 HIS D 399
REMARK 465 HIS D 400
REMARK 465 HIS D 401
REMARK 465 HIS D 402
REMARK 465 HIS D 403
REMARK 465 HIS A 21
REMARK 465 ALA A 397
REMARK 465 HIS A 398
REMARK 465 HIS A 399
REMARK 465 HIS A 400
REMARK 465 HIS A 401
REMARK 465 HIS A 402
REMARK 465 HIS A 403
REMARK 465 HIS B 21
REMARK 465 ALA B 397
REMARK 465 HIS B 398
REMARK 465 HIS B 399
REMARK 465 HIS B 400
REMARK 465 HIS B 401
REMARK 465 HIS B 402
REMARK 465 HIS B 403
REMARK 465 HIS C 21
REMARK 465 ALA C 397
REMARK 465 HIS C 398
REMARK 465 HIS C 399
REMARK 465 HIS C 400
REMARK 465 HIS C 401
REMARK 465 HIS C 402
REMARK 465 HIS C 403
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 CA LEU D 285 OH TYR D 333 1.59
REMARK 500 OD1 ASP C 41 CE LYS C 53 1.72
REMARK 500 N LEU D 285 OH TYR D 333 1.90
REMARK 500 OD1 ASP C 41 NZ LYS C 53 1.97
REMARK 500 OD2 ASP C 63 CG MET C 66 2.10
REMARK 500 N ILE B 326 O GLY B 338 2.13
REMARK 500 N ILE C 326 O GLY C 338 2.13
REMARK 500 N ILE D 326 O GLY D 338 2.13
REMARK 500 N ILE A 326 O GLY A 338 2.13
REMARK 500 O ASP D 284 OH TYR D 333 2.14
REMARK 500 OG1 THR B 321 N ASP B 346 2.19
REMARK 500 OG1 THR D 321 N ASP D 346 2.19
REMARK 500 OG1 THR A 321 N ASP A 346 2.19
REMARK 500 OG1 THR C 321 N ASP C 346 2.19
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 ASP D 41 67.35 -151.81
REMARK 500 ASP D 136 -4.60 75.51
REMARK 500 GLU D 137 -63.33 -133.87
REMARK 500 SER D 181 -116.12 55.40
REMARK 500 TYR D 315 161.07 179.23
REMARK 500 TYR D 327 46.10 -109.05
REMARK 500 ASP D 346 -11.06 84.90
REMARK 500 THR D 347 -59.85 -142.00
REMARK 500 ASP A 41 67.48 -151.76
REMARK 500 ASP A 136 -4.59 75.56
REMARK 500 GLU A 137 -63.38 -133.95
REMARK 500 SER A 181 -116.11 55.28
REMARK 500 TYR A 315 161.06 179.20
REMARK 500 TYR A 327 45.79 -108.55
REMARK 500 ASP A 346 -11.09 84.88
REMARK 500 THR A 347 -59.83 -141.96
REMARK 500 ASP B 41 67.49 -151.73
REMARK 500 SER B 87 45.71 -150.83
REMARK 500 ASP B 136 -4.56 75.47
REMARK 500 GLU B 137 -63.39 -133.96
REMARK 500 SER B 181 -116.17 55.31
REMARK 500 TYR B 315 161.04 179.22
REMARK 500 TYR B 327 45.89 -108.60
REMARK 500 ASP B 346 -11.13 84.89
REMARK 500 THR B 347 -59.81 -141.98
REMARK 500 ASP C 41 67.09 -152.09
REMARK 500 ASP C 136 -4.60 75.51
REMARK 500 GLU C 137 -63.27 -133.94
REMARK 500 SER C 181 -116.13 55.33
REMARK 500 TYR C 315 161.06 179.24
REMARK 500 TYR C 327 45.85 -108.58
REMARK 500 ASP C 346 -10.99 84.73
REMARK 500 THR C 347 -59.80 -141.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 501 through BMA A 503 bound to ASN A 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 504 through BMA A 506 bound to ASN A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 507 bound
REMARK 800 to ASN A 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 501 through BMA B 503 bound to ASN B 84
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 800 504 through BMA B 506 bound to ASN B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 507 bound
REMARK 800 to ASN B 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 501 through BMA C 503 bound to ASN C 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 504 through BMA C 506 bound to ASN C 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 507 bound
REMARK 800 to ASN C 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 501 through BMA D 503 bound to ASN D 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 504 through BMA D 506 bound to ASN D 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 507 bound
REMARK 800 to ASN D 384
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X90 RELATED DB: PDB
REMARK 900 RELATED ID: 4X91 RELATED DB: PDB
REMARK 900 RELATED ID: 4X92 RELATED DB: PDB
REMARK 900 RELATED ID: 4X93 RELATED DB: PDB
REMARK 900 RELATED ID: 4X94 RELATED DB: PDB
REMARK 900 RELATED ID: 4X95 RELATED DB: PDB
REMARK 900 RELATED ID: 4X97 RELATED DB: PDB
DBREF 4X96 D 21 400 UNP P04180 LCAT_HUMAN 45 424
DBREF 4X96 A 21 400 UNP P04180 LCAT_HUMAN 45 424
DBREF 4X96 B 21 400 UNP P04180 LCAT_HUMAN 45 424
DBREF 4X96 C 21 400 UNP P04180 LCAT_HUMAN 45 424
SEQADV 4X96 HIS D 398 UNP P04180 TYR 422 CONFLICT
SEQADV 4X96 HIS D 399 UNP P04180 ARG 423 CONFLICT
SEQADV 4X96 HIS D 400 UNP P04180 GLN 424 CONFLICT
SEQADV 4X96 HIS D 401 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS D 402 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS D 403 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS A 398 UNP P04180 TYR 422 CONFLICT
SEQADV 4X96 HIS A 399 UNP P04180 ARG 423 CONFLICT
SEQADV 4X96 HIS A 400 UNP P04180 GLN 424 CONFLICT
SEQADV 4X96 HIS A 401 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS A 402 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS A 403 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS B 398 UNP P04180 TYR 422 CONFLICT
SEQADV 4X96 HIS B 399 UNP P04180 ARG 423 CONFLICT
SEQADV 4X96 HIS B 400 UNP P04180 GLN 424 CONFLICT
SEQADV 4X96 HIS B 401 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS B 402 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS B 403 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS C 398 UNP P04180 TYR 422 CONFLICT
SEQADV 4X96 HIS C 399 UNP P04180 ARG 423 CONFLICT
SEQADV 4X96 HIS C 400 UNP P04180 GLN 424 CONFLICT
SEQADV 4X96 HIS C 401 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS C 402 UNP P04180 EXPRESSION TAG
SEQADV 4X96 HIS C 403 UNP P04180 EXPRESSION TAG
SEQRES 1 D 383 HIS THR ARG PRO VAL ILE LEU VAL PRO GLY CYS LEU GLY
SEQRES 2 D 383 ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO ASP VAL VAL
SEQRES 3 D 383 ASN TRP MET CYS TYR ARG LYS THR GLU ASP PHE PHE THR
SEQRES 4 D 383 ILE TRP LEU ASP LEU ASN MET PHE LEU PRO LEU GLY VAL
SEQRES 5 D 383 ASP CYS TRP ILE ASP ASN THR ARG VAL VAL TYR ASN ARG
SEQRES 6 D 383 SER SER GLY LEU VAL SER ASN ALA PRO GLY VAL GLN ILE
SEQRES 7 D 383 ARG VAL PRO GLY PHE GLY LYS THR TYR SER VAL GLU TYR
SEQRES 8 D 383 LEU ASP SER SER LYS LEU ALA GLY TYR LEU HIS THR LEU
SEQRES 9 D 383 VAL GLN ASN LEU VAL ASN ASN GLY TYR VAL ARG ASP GLU
SEQRES 10 D 383 THR VAL ARG ALA ALA PRO TYR ASP TRP ARG LEU GLU PRO
SEQRES 11 D 383 GLY GLN GLN GLU GLU TYR TYR ARG LYS LEU ALA GLY LEU
SEQRES 12 D 383 VAL GLU GLU MET HIS ALA ALA TYR GLY LYS PRO VAL PHE
SEQRES 13 D 383 LEU ILE GLY HIS SER LEU GLY CYS LEU HIS LEU LEU TYR
SEQRES 14 D 383 PHE LEU LEU ARG GLN PRO GLN ALA TRP LYS ASP ARG PHE
SEQRES 15 D 383 ILE ASP GLY PHE ILE SER LEU GLY ALA PRO TRP GLY GLY
SEQRES 16 D 383 SER ILE LYS PRO MET LEU VAL LEU ALA SER GLY ASP ASN
SEQRES 17 D 383 GLN GLY ILE PRO ILE MET SER SER ILE LYS LEU LYS GLU
SEQRES 18 D 383 GLU GLN ARG ILE THR THR THR SER PRO TRP MET PHE PRO
SEQRES 19 D 383 SER ARG MET ALA TRP PRO GLU ASP HIS VAL PHE ILE SER
SEQRES 20 D 383 THR PRO SER PHE ASN TYR THR GLY ARG ASP PHE GLN ARG
SEQRES 21 D 383 PHE PHE ALA ASP LEU HIS PHE GLU GLU GLY TRP TYR MET
SEQRES 22 D 383 TRP LEU GLN SER ARG ASP LEU LEU ALA GLY LEU PRO ALA
SEQRES 23 D 383 PRO GLY VAL GLU VAL TYR CYS LEU TYR GLY VAL GLY LEU
SEQRES 24 D 383 PRO THR PRO ARG THR TYR ILE TYR ASP HIS GLY PHE PRO
SEQRES 25 D 383 TYR THR ASP PRO VAL GLY VAL LEU TYR GLU ASP GLY ASP
SEQRES 26 D 383 ASP THR VAL ALA THR ARG SER THR GLU LEU CYS GLY LEU
SEQRES 27 D 383 TRP GLN GLY ARG GLN PRO GLN PRO VAL HIS LEU LEU PRO
SEQRES 28 D 383 LEU HIS GLY ILE GLN HIS LEU ASN MET VAL PHE SER ASN
SEQRES 29 D 383 LEU THR LEU GLU HIS ILE ASN ALA ILE LEU LEU GLY ALA
SEQRES 30 D 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 A 383 HIS THR ARG PRO VAL ILE LEU VAL PRO GLY CYS LEU GLY
SEQRES 2 A 383 ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO ASP VAL VAL
SEQRES 3 A 383 ASN TRP MET CYS TYR ARG LYS THR GLU ASP PHE PHE THR
SEQRES 4 A 383 ILE TRP LEU ASP LEU ASN MET PHE LEU PRO LEU GLY VAL
SEQRES 5 A 383 ASP CYS TRP ILE ASP ASN THR ARG VAL VAL TYR ASN ARG
SEQRES 6 A 383 SER SER GLY LEU VAL SER ASN ALA PRO GLY VAL GLN ILE
SEQRES 7 A 383 ARG VAL PRO GLY PHE GLY LYS THR TYR SER VAL GLU TYR
SEQRES 8 A 383 LEU ASP SER SER LYS LEU ALA GLY TYR LEU HIS THR LEU
SEQRES 9 A 383 VAL GLN ASN LEU VAL ASN ASN GLY TYR VAL ARG ASP GLU
SEQRES 10 A 383 THR VAL ARG ALA ALA PRO TYR ASP TRP ARG LEU GLU PRO
SEQRES 11 A 383 GLY GLN GLN GLU GLU TYR TYR ARG LYS LEU ALA GLY LEU
SEQRES 12 A 383 VAL GLU GLU MET HIS ALA ALA TYR GLY LYS PRO VAL PHE
SEQRES 13 A 383 LEU ILE GLY HIS SER LEU GLY CYS LEU HIS LEU LEU TYR
SEQRES 14 A 383 PHE LEU LEU ARG GLN PRO GLN ALA TRP LYS ASP ARG PHE
SEQRES 15 A 383 ILE ASP GLY PHE ILE SER LEU GLY ALA PRO TRP GLY GLY
SEQRES 16 A 383 SER ILE LYS PRO MET LEU VAL LEU ALA SER GLY ASP ASN
SEQRES 17 A 383 GLN GLY ILE PRO ILE MET SER SER ILE LYS LEU LYS GLU
SEQRES 18 A 383 GLU GLN ARG ILE THR THR THR SER PRO TRP MET PHE PRO
SEQRES 19 A 383 SER ARG MET ALA TRP PRO GLU ASP HIS VAL PHE ILE SER
SEQRES 20 A 383 THR PRO SER PHE ASN TYR THR GLY ARG ASP PHE GLN ARG
SEQRES 21 A 383 PHE PHE ALA ASP LEU HIS PHE GLU GLU GLY TRP TYR MET
SEQRES 22 A 383 TRP LEU GLN SER ARG ASP LEU LEU ALA GLY LEU PRO ALA
SEQRES 23 A 383 PRO GLY VAL GLU VAL TYR CYS LEU TYR GLY VAL GLY LEU
SEQRES 24 A 383 PRO THR PRO ARG THR TYR ILE TYR ASP HIS GLY PHE PRO
SEQRES 25 A 383 TYR THR ASP PRO VAL GLY VAL LEU TYR GLU ASP GLY ASP
SEQRES 26 A 383 ASP THR VAL ALA THR ARG SER THR GLU LEU CYS GLY LEU
SEQRES 27 A 383 TRP GLN GLY ARG GLN PRO GLN PRO VAL HIS LEU LEU PRO
SEQRES 28 A 383 LEU HIS GLY ILE GLN HIS LEU ASN MET VAL PHE SER ASN
SEQRES 29 A 383 LEU THR LEU GLU HIS ILE ASN ALA ILE LEU LEU GLY ALA
SEQRES 30 A 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 383 HIS THR ARG PRO VAL ILE LEU VAL PRO GLY CYS LEU GLY
SEQRES 2 B 383 ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO ASP VAL VAL
SEQRES 3 B 383 ASN TRP MET CYS TYR ARG LYS THR GLU ASP PHE PHE THR
SEQRES 4 B 383 ILE TRP LEU ASP LEU ASN MET PHE LEU PRO LEU GLY VAL
SEQRES 5 B 383 ASP CYS TRP ILE ASP ASN THR ARG VAL VAL TYR ASN ARG
SEQRES 6 B 383 SER SER GLY LEU VAL SER ASN ALA PRO GLY VAL GLN ILE
SEQRES 7 B 383 ARG VAL PRO GLY PHE GLY LYS THR TYR SER VAL GLU TYR
SEQRES 8 B 383 LEU ASP SER SER LYS LEU ALA GLY TYR LEU HIS THR LEU
SEQRES 9 B 383 VAL GLN ASN LEU VAL ASN ASN GLY TYR VAL ARG ASP GLU
SEQRES 10 B 383 THR VAL ARG ALA ALA PRO TYR ASP TRP ARG LEU GLU PRO
SEQRES 11 B 383 GLY GLN GLN GLU GLU TYR TYR ARG LYS LEU ALA GLY LEU
SEQRES 12 B 383 VAL GLU GLU MET HIS ALA ALA TYR GLY LYS PRO VAL PHE
SEQRES 13 B 383 LEU ILE GLY HIS SER LEU GLY CYS LEU HIS LEU LEU TYR
SEQRES 14 B 383 PHE LEU LEU ARG GLN PRO GLN ALA TRP LYS ASP ARG PHE
SEQRES 15 B 383 ILE ASP GLY PHE ILE SER LEU GLY ALA PRO TRP GLY GLY
SEQRES 16 B 383 SER ILE LYS PRO MET LEU VAL LEU ALA SER GLY ASP ASN
SEQRES 17 B 383 GLN GLY ILE PRO ILE MET SER SER ILE LYS LEU LYS GLU
SEQRES 18 B 383 GLU GLN ARG ILE THR THR THR SER PRO TRP MET PHE PRO
SEQRES 19 B 383 SER ARG MET ALA TRP PRO GLU ASP HIS VAL PHE ILE SER
SEQRES 20 B 383 THR PRO SER PHE ASN TYR THR GLY ARG ASP PHE GLN ARG
SEQRES 21 B 383 PHE PHE ALA ASP LEU HIS PHE GLU GLU GLY TRP TYR MET
SEQRES 22 B 383 TRP LEU GLN SER ARG ASP LEU LEU ALA GLY LEU PRO ALA
SEQRES 23 B 383 PRO GLY VAL GLU VAL TYR CYS LEU TYR GLY VAL GLY LEU
SEQRES 24 B 383 PRO THR PRO ARG THR TYR ILE TYR ASP HIS GLY PHE PRO
SEQRES 25 B 383 TYR THR ASP PRO VAL GLY VAL LEU TYR GLU ASP GLY ASP
SEQRES 26 B 383 ASP THR VAL ALA THR ARG SER THR GLU LEU CYS GLY LEU
SEQRES 27 B 383 TRP GLN GLY ARG GLN PRO GLN PRO VAL HIS LEU LEU PRO
SEQRES 28 B 383 LEU HIS GLY ILE GLN HIS LEU ASN MET VAL PHE SER ASN
SEQRES 29 B 383 LEU THR LEU GLU HIS ILE ASN ALA ILE LEU LEU GLY ALA
SEQRES 30 B 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 383 HIS THR ARG PRO VAL ILE LEU VAL PRO GLY CYS LEU GLY
SEQRES 2 C 383 ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO ASP VAL VAL
SEQRES 3 C 383 ASN TRP MET CYS TYR ARG LYS THR GLU ASP PHE PHE THR
SEQRES 4 C 383 ILE TRP LEU ASP LEU ASN MET PHE LEU PRO LEU GLY VAL
SEQRES 5 C 383 ASP CYS TRP ILE ASP ASN THR ARG VAL VAL TYR ASN ARG
SEQRES 6 C 383 SER SER GLY LEU VAL SER ASN ALA PRO GLY VAL GLN ILE
SEQRES 7 C 383 ARG VAL PRO GLY PHE GLY LYS THR TYR SER VAL GLU TYR
SEQRES 8 C 383 LEU ASP SER SER LYS LEU ALA GLY TYR LEU HIS THR LEU
SEQRES 9 C 383 VAL GLN ASN LEU VAL ASN ASN GLY TYR VAL ARG ASP GLU
SEQRES 10 C 383 THR VAL ARG ALA ALA PRO TYR ASP TRP ARG LEU GLU PRO
SEQRES 11 C 383 GLY GLN GLN GLU GLU TYR TYR ARG LYS LEU ALA GLY LEU
SEQRES 12 C 383 VAL GLU GLU MET HIS ALA ALA TYR GLY LYS PRO VAL PHE
SEQRES 13 C 383 LEU ILE GLY HIS SER LEU GLY CYS LEU HIS LEU LEU TYR
SEQRES 14 C 383 PHE LEU LEU ARG GLN PRO GLN ALA TRP LYS ASP ARG PHE
SEQRES 15 C 383 ILE ASP GLY PHE ILE SER LEU GLY ALA PRO TRP GLY GLY
SEQRES 16 C 383 SER ILE LYS PRO MET LEU VAL LEU ALA SER GLY ASP ASN
SEQRES 17 C 383 GLN GLY ILE PRO ILE MET SER SER ILE LYS LEU LYS GLU
SEQRES 18 C 383 GLU GLN ARG ILE THR THR THR SER PRO TRP MET PHE PRO
SEQRES 19 C 383 SER ARG MET ALA TRP PRO GLU ASP HIS VAL PHE ILE SER
SEQRES 20 C 383 THR PRO SER PHE ASN TYR THR GLY ARG ASP PHE GLN ARG
SEQRES 21 C 383 PHE PHE ALA ASP LEU HIS PHE GLU GLU GLY TRP TYR MET
SEQRES 22 C 383 TRP LEU GLN SER ARG ASP LEU LEU ALA GLY LEU PRO ALA
SEQRES 23 C 383 PRO GLY VAL GLU VAL TYR CYS LEU TYR GLY VAL GLY LEU
SEQRES 24 C 383 PRO THR PRO ARG THR TYR ILE TYR ASP HIS GLY PHE PRO
SEQRES 25 C 383 TYR THR ASP PRO VAL GLY VAL LEU TYR GLU ASP GLY ASP
SEQRES 26 C 383 ASP THR VAL ALA THR ARG SER THR GLU LEU CYS GLY LEU
SEQRES 27 C 383 TRP GLN GLY ARG GLN PRO GLN PRO VAL HIS LEU LEU PRO
SEQRES 28 C 383 LEU HIS GLY ILE GLN HIS LEU ASN MET VAL PHE SER ASN
SEQRES 29 C 383 LEU THR LEU GLU HIS ILE ASN ALA ILE LEU LEU GLY ALA
SEQRES 30 C 383 HIS HIS HIS HIS HIS HIS
HET NAG D 501 14
HET NAG D 502 14
HET BMA D 503 11
HET NAG D 504 14
HET NAG D 505 14
HET BMA D 506 11
HET NAG D 507 14
HET NAG A 501 14
HET NAG A 502 14
HET BMA A 503 11
HET NAG A 504 14
HET NAG A 505 14
HET BMA A 506 11
HET NAG A 507 14
HET NAG B 501 14
HET NAG B 502 14
HET BMA B 503 11
HET NAG B 504 14
HET NAG B 505 14
HET BMA B 506 11
HET NAG B 507 14
HET NAG C 501 14
HET NAG C 502 14
HET BMA C 503 11
HET NAG C 504 14
HET NAG C 505 14
HET BMA C 506 11
HET NAG C 507 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
FORMUL 5 NAG 20(C8 H15 N O6)
FORMUL 5 BMA 8(C6 H12 O6)
HELIX 1 AA1 LEU D 64 PHE D 67 5 4
HELIX 2 AA2 LEU D 68 ARG D 80 1 13
HELIX 3 AA3 THR D 106 TYR D 111 1 6
HELIX 4 AA4 LEU D 121 GLY D 132 1 12
HELIX 5 AA5 GLU D 149 GLN D 152 5 4
HELIX 6 AA6 GLN D 153 GLY D 172 1 20
HELIX 7 AA7 LEU D 182 GLN D 194 1 13
HELIX 8 AA8 PRO D 195 PHE D 202 1 8
HELIX 9 AA9 LYS D 218 SER D 225 1 8
HELIX 10 AB1 SER D 235 ARG D 244 1 10
HELIX 11 AB2 THR D 247 MET D 252 1 6
HELIX 12 AB3 ASP D 277 LEU D 285 1 9
HELIX 13 AB4 PHE D 287 ASP D 299 1 13
HELIX 14 AB5 ALA D 349 THR D 353 5 5
HELIX 15 AB6 GLU D 354 TRP D 359 1 6
HELIX 16 AB7 LEU D 378 SER D 383 1 6
HELIX 17 AB8 SER D 383 GLY D 396 1 14
HELIX 18 AB9 LEU A 64 PHE A 67 5 4
HELIX 19 AC1 LEU A 68 ARG A 80 1 13
HELIX 20 AC2 THR A 106 TYR A 111 1 6
HELIX 21 AC3 LEU A 121 GLY A 132 1 12
HELIX 22 AC4 GLU A 149 GLN A 152 5 4
HELIX 23 AC5 GLN A 153 GLY A 172 1 20
HELIX 24 AC6 LEU A 182 GLN A 194 1 13
HELIX 25 AC7 PRO A 195 PHE A 202 1 8
HELIX 26 AC8 LYS A 218 SER A 225 1 8
HELIX 27 AC9 SER A 235 ARG A 244 1 10
HELIX 28 AD1 THR A 247 MET A 252 1 6
HELIX 29 AD2 ASP A 277 LEU A 285 1 9
HELIX 30 AD3 PHE A 287 ASP A 299 1 13
HELIX 31 AD4 ALA A 349 THR A 353 5 5
HELIX 32 AD5 GLU A 354 TRP A 359 1 6
HELIX 33 AD6 LEU A 378 SER A 383 1 6
HELIX 34 AD7 SER A 383 GLY A 396 1 14
HELIX 35 AD8 LEU B 64 PHE B 67 5 4
HELIX 36 AD9 LEU B 68 ARG B 80 1 13
HELIX 37 AE1 THR B 106 TYR B 111 1 6
HELIX 38 AE2 LEU B 121 GLY B 132 1 12
HELIX 39 AE3 GLU B 149 GLN B 152 5 4
HELIX 40 AE4 GLN B 153 GLY B 172 1 20
HELIX 41 AE5 LEU B 182 GLN B 194 1 13
HELIX 42 AE6 PRO B 195 PHE B 202 1 8
HELIX 43 AE7 LYS B 218 SER B 225 1 8
HELIX 44 AE8 SER B 235 ARG B 244 1 10
HELIX 45 AE9 THR B 247 MET B 252 1 6
HELIX 46 AF1 ASP B 277 LEU B 285 1 9
HELIX 47 AF2 PHE B 287 ASP B 299 1 13
HELIX 48 AF3 ALA B 349 THR B 353 5 5
HELIX 49 AF4 GLU B 354 TRP B 359 1 6
HELIX 50 AF5 LEU B 378 SER B 383 1 6
HELIX 51 AF6 SER B 383 GLY B 396 1 14
HELIX 52 AF7 LEU C 64 PHE C 67 5 4
HELIX 53 AF8 LEU C 68 ARG C 80 1 13
HELIX 54 AF9 THR C 106 TYR C 111 1 6
HELIX 55 AG1 LEU C 121 GLY C 132 1 12
HELIX 56 AG2 GLU C 149 GLN C 152 5 4
HELIX 57 AG3 GLN C 153 GLY C 172 1 20
HELIX 58 AG4 LEU C 182 GLN C 194 1 13
HELIX 59 AG5 PRO C 195 PHE C 202 1 8
HELIX 60 AG6 LYS C 218 SER C 225 1 8
HELIX 61 AG7 SER C 235 ARG C 244 1 10
HELIX 62 AG8 THR C 247 MET C 252 1 6
HELIX 63 AG9 ASP C 277 LEU C 285 1 9
HELIX 64 AH1 PHE C 287 ASP C 299 1 13
HELIX 65 AH2 ALA C 349 THR C 353 5 5
HELIX 66 AH3 GLU C 354 TRP C 359 1 6
HELIX 67 AH4 LEU C 378 SER C 383 1 6
HELIX 68 AH5 SER C 383 GLY C 396 1 14
SHEET 1 AA1 6 VAL D 139 ALA D 141 0
SHEET 2 AA1 6 VAL D 25 VAL D 28 1 N VAL D 25 O ARG D 140
SHEET 3 AA1 6 VAL D 175 HIS D 180 1 O ILE D 178 N ILE D 26
SHEET 4 AA1 6 ILE D 203 LEU D 209 1 O LEU D 209 N GLY D 179
SHEET 5 AA1 6 VAL D 311 CYS D 313 1 O TYR D 312 N SER D 208
SHEET 6 AA1 6 VAL D 367 LEU D 369 1 O HIS D 368 N VAL D 311
SHEET 1 AA2 3 PHE D 58 TRP D 61 0
SHEET 2 AA2 3 LEU D 36 LEU D 40 -1 N LEU D 36 O TRP D 61
SHEET 3 AA2 3 VAL D 96 ARG D 99 -1 O ARG D 99 N GLU D 37
SHEET 1 AA3 4 ASN D 272 THR D 274 0
SHEET 2 AA3 4 VAL D 264 SER D 267 -1 N ILE D 266 O TYR D 273
SHEET 3 AA3 4 LEU D 319 ILE D 326 1 O TYR D 325 N PHE D 265
SHEET 4 AA3 4 GLY D 338 GLY D 344 -1 O GLY D 338 N ILE D 326
SHEET 1 AA4 2 GLY D 316 VAL D 317 0
SHEET 2 AA4 2 LEU D 372 HIS D 373 1 O LEU D 372 N VAL D 317
SHEET 1 AA5 6 VAL A 139 ALA A 141 0
SHEET 2 AA5 6 VAL A 25 VAL A 28 1 N VAL A 25 O ARG A 140
SHEET 3 AA5 6 VAL A 175 HIS A 180 1 O ILE A 178 N ILE A 26
SHEET 4 AA5 6 ILE A 203 LEU A 209 1 O LEU A 209 N GLY A 179
SHEET 5 AA5 6 VAL A 311 CYS A 313 1 O TYR A 312 N SER A 208
SHEET 6 AA5 6 VAL A 367 LEU A 369 1 O HIS A 368 N VAL A 311
SHEET 1 AA6 3 PHE A 58 TRP A 61 0
SHEET 2 AA6 3 LEU A 36 LEU A 40 -1 N LEU A 36 O TRP A 61
SHEET 3 AA6 3 VAL A 96 ARG A 99 -1 O ARG A 99 N GLU A 37
SHEET 1 AA7 4 ASN A 272 THR A 274 0
SHEET 2 AA7 4 VAL A 264 SER A 267 -1 N ILE A 266 O TYR A 273
SHEET 3 AA7 4 LEU A 319 ILE A 326 1 O TYR A 325 N PHE A 265
SHEET 4 AA7 4 GLY A 338 GLY A 344 -1 O GLY A 338 N ILE A 326
SHEET 1 AA8 2 GLY A 316 VAL A 317 0
SHEET 2 AA8 2 LEU A 372 HIS A 373 1 O LEU A 372 N VAL A 317
SHEET 1 AA9 6 VAL B 139 ALA B 141 0
SHEET 2 AA9 6 VAL B 25 VAL B 28 1 N VAL B 25 O ARG B 140
SHEET 3 AA9 6 VAL B 175 HIS B 180 1 O ILE B 178 N ILE B 26
SHEET 4 AA9 6 ILE B 203 LEU B 209 1 O LEU B 209 N GLY B 179
SHEET 5 AA9 6 VAL B 311 CYS B 313 1 O TYR B 312 N SER B 208
SHEET 6 AA9 6 VAL B 367 LEU B 369 1 O HIS B 368 N VAL B 311
SHEET 1 AB1 3 PHE B 58 TRP B 61 0
SHEET 2 AB1 3 LEU B 36 LEU B 40 -1 N LEU B 36 O TRP B 61
SHEET 3 AB1 3 VAL B 96 ARG B 99 -1 O ARG B 99 N GLU B 37
SHEET 1 AB2 4 ASN B 272 THR B 274 0
SHEET 2 AB2 4 VAL B 264 SER B 267 -1 N ILE B 266 O TYR B 273
SHEET 3 AB2 4 LEU B 319 ILE B 326 1 O TYR B 325 N PHE B 265
SHEET 4 AB2 4 GLY B 338 GLY B 344 -1 O GLY B 338 N ILE B 326
SHEET 1 AB3 2 GLY B 316 VAL B 317 0
SHEET 2 AB3 2 LEU B 372 HIS B 373 1 O LEU B 372 N VAL B 317
SHEET 1 AB4 6 VAL C 139 ALA C 141 0
SHEET 2 AB4 6 VAL C 25 VAL C 28 1 N VAL C 25 O ARG C 140
SHEET 3 AB4 6 VAL C 175 HIS C 180 1 O ILE C 178 N ILE C 26
SHEET 4 AB4 6 ILE C 203 LEU C 209 1 O LEU C 209 N GLY C 179
SHEET 5 AB4 6 VAL C 311 CYS C 313 1 O TYR C 312 N SER C 208
SHEET 6 AB4 6 VAL C 367 LEU C 369 1 O HIS C 368 N VAL C 311
SHEET 1 AB5 3 PHE C 58 TRP C 61 0
SHEET 2 AB5 3 LEU C 36 LEU C 40 -1 N LEU C 36 O TRP C 61
SHEET 3 AB5 3 VAL C 96 ARG C 99 -1 O ARG C 99 N GLU C 37
SHEET 1 AB6 4 ASN C 272 THR C 274 0
SHEET 2 AB6 4 VAL C 264 SER C 267 -1 N ILE C 266 O TYR C 273
SHEET 3 AB6 4 LEU C 319 ILE C 326 1 O TYR C 325 N PHE C 265
SHEET 4 AB6 4 GLY C 338 GLY C 344 -1 O GLY C 338 N ILE C 326
SHEET 1 AB7 2 GLY C 316 VAL C 317 0
SHEET 2 AB7 2 LEU C 372 HIS C 373 1 O LEU C 372 N VAL C 317
SSBOND 1 CYS D 50 CYS D 74 1555 1555 2.03
SSBOND 2 CYS D 313 CYS D 356 1555 1555 2.04
SSBOND 3 CYS A 50 CYS A 74 1555 1555 2.03
SSBOND 4 CYS A 313 CYS A 356 1555 1555 2.04
SSBOND 5 CYS B 50 CYS B 74 1555 1555 2.03
SSBOND 6 CYS B 313 CYS B 356 1555 1555 2.04
SSBOND 7 CYS C 50 CYS C 74 1555 1555 2.03
SSBOND 8 CYS C 313 CYS C 356 1555 1555 2.04
LINK ND2 ASN D 84 C1 NAG D 501 1555 1555 1.47
LINK ND2 ASN D 272 C1 NAG D 504 1555 1555 1.47
LINK ND2 ASN D 384 C1 NAG D 507 1555 1555 1.47
LINK ND2 ASN A 84 C1 NAG A 501 1555 1555 1.46
LINK ND2 ASN A 272 C1 NAG A 504 1555 1555 1.48
LINK ND2 ASN A 384 C1 NAG A 507 1555 1555 1.46
LINK ND2 ASN B 84 C1 NAG B 501 1555 1555 1.48
LINK ND2 ASN B 272 C1 NAG B 504 1555 1555 1.47
LINK ND2 ASN B 384 C1 NAG B 507 1555 1555 1.46
LINK ND2 ASN C 84 C1 NAG C 501 1555 1555 1.46
LINK ND2 ASN C 272 C1 NAG C 504 1555 1555 1.47
LINK ND2 ASN C 384 C1 NAG C 507 1555 1555 1.47
LINK O4 NAG D 501 C1 NAG D 502 1555 1555 1.44
LINK O4 NAG D 502 C1 BMA D 503 1555 1555 1.44
LINK O4 NAG D 504 C1 NAG D 505 1555 1555 1.43
LINK O4 NAG D 505 C1 BMA D 506 1555 1555 1.44
LINK O4 NAG A 501 C1 NAG A 502 1555 1555 1.44
LINK O4 NAG A 502 C1 BMA A 503 1555 1555 1.45
LINK O4 NAG A 504 C1 NAG A 505 1555 1555 1.43
LINK O4 NAG A 505 C1 BMA A 506 1555 1555 1.43
LINK O4 NAG B 501 C1 NAG B 502 1555 1555 1.43
LINK O4 NAG B 502 C1 BMA B 503 1555 1555 1.44
LINK O4 NAG B 504 C1 NAG B 505 1555 1555 1.43
LINK O4 NAG B 505 C1 BMA B 506 1555 1555 1.43
LINK O4 NAG C 501 C1 NAG C 502 1555 1555 1.44
LINK O4 NAG C 502 C1 BMA C 503 1555 1555 1.44
LINK O4 NAG C 504 C1 NAG C 505 1555 1555 1.42
LINK O4 NAG C 505 C1 BMA C 506 1555 1555 1.43
CISPEP 1 TRP D 61 LEU D 62 0 -1.15
CISPEP 2 PHE D 331 PRO D 332 0 4.11
CISPEP 3 TRP A 61 LEU A 62 0 -1.25
CISPEP 4 PHE A 331 PRO A 332 0 0.96
CISPEP 5 TRP B 61 LEU B 62 0 -1.21
CISPEP 6 PHE B 331 PRO B 332 0 0.48
CISPEP 7 TRP C 61 LEU C 62 0 2.06
CISPEP 8 PHE C 331 PRO C 332 0 0.32
SITE 1 AC1 3 ASN A 84 SER A 86 SER A 87
SITE 1 AC2 4 SER A 267 THR A 268 PHE A 271 ASN A 272
SITE 1 AC3 2 LYS A 53 ASN A 384
SITE 1 AC4 3 ASN B 84 SER B 86 SER B 87
SITE 1 AC5 4 SER B 267 THR B 268 PHE B 271 ASN B 272
SITE 1 AC6 1 ASN B 384
SITE 1 AC7 3 ASN C 84 SER C 86 SER C 87
SITE 1 AC8 4 SER C 267 THR C 268 PHE C 271 ASN C 272
SITE 1 AC9 1 ASN C 384
SITE 1 AD1 3 ASN D 84 SER D 86 SER D 87
SITE 1 AD2 4 SER D 267 THR D 268 PHE D 271 ASN D 272
SITE 1 AD3 1 ASN D 384
CRYST1 367.258 367.258 187.069 90.00 90.00 120.00 H 3 36
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 0.002723 0.001572 0.000000 0.00000
SCALE2 0.000000 0.003144 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005346 0.00000
TER 3012 GLY D 396
TER 6024 GLY A 396
TER 9036 GLY B 396
TER 12048 GLY C 396
MASTER 537 0 28 68 60 0 12 612412 4 396 120
END |